UBC13 MMS2 - Revision history

http://52.214.119.220/wiki/index.php?action=history&feed=atom&title=UBC13_MMS2 UBC13 MMS2 - Revision history 2026-04-09T02:50:32Z Revision history for this page on the wiki MediaWiki 1.11.2 http://52.214.119.220/wiki/index.php?title=UBC13_MMS2&diff=2577048&oldid=prev Michal Harel at 09:46, 28 February 2016 2016-02-28T09:46:03Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 09:46, 28 February 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 1:</td> <td colspan="2" class="diff-lineno">Line 1:</td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><Structure load='1J7D' size='350' scene='69/695700/Ubc13_mms2_overall/1' caption='Human ubiquitin conjugating enzyme E2 13 complex with HMM2 (PDB code [[1j7d]]) ></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><Structure load='1J7D' size='350' scene='69/695700/Ubc13_mms2_overall/1' caption='Human ubiquitin conjugating enzyme E2 13 complex with HMM2 (PDB code [[1j7d]])<ins style="color: red; font-weight: bold; text-decoration: none;">' </ins>></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Summary==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Summary==</div></td></tr> </table>

Michal Harel http://52.214.119.220/wiki/index.php?title=UBC13_MMS2&diff=2577047&oldid=prev Michal Harel at 09:45, 28 February 2016 2016-02-28T09:45:16Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 09:45, 28 February 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 1:</td> <td colspan="2" class="diff-lineno">Line 1:</td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><Structure load='1J7D' size='<del style="color: red; font-weight: bold; text-decoration: none;">450</del>' scene='69/695700/Ubc13_mms2_overall/1'></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><Structure load='1J7D' size='<ins style="color: red; font-weight: bold; text-decoration: none;">350</ins>' scene='69/695700/Ubc13_mms2_overall/1' <ins style="color: red; font-weight: bold; text-decoration: none;">caption='Human ubiquitin conjugating enzyme E2 13 complex with HMM2 (PDB code [[1j7d]]) </ins>></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Summary==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Summary==</div></td></tr> </table>

Michal Harel http://52.214.119.220/wiki/index.php?title=UBC13_MMS2&diff=2518440&oldid=prev Michal Harel at 07:32, 11 January 2016 2016-01-11T07:32:10Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 07:32, 11 January 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 36:</td> <td colspan="2" class="diff-lineno">Line 36:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The exact mechanism for how Ubc13 transfers ubiquitin is not known, however the mechanism occurs in either a step-wise or concerted reaction. Ubc13, as an E2, froms a covalent bond with ubiquitin and then transfers the ubiquitin to the target protein via a thioester intermediate. Ubiquitin is removed from Ubc13 and Mms2 complex and placed onto PCNA.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>The exact mechanism for how Ubc13 transfers ubiquitin is not known, however the mechanism occurs in either a step-wise or concerted reaction. Ubc13, as an E2, froms a covalent bond with ubiquitin and then transfers the ubiquitin to the target protein via a thioester intermediate. Ubiquitin is removed from Ubc13 and Mms2 complex and placed onto PCNA.</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>==3D structure of Ubc13==</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td colspan="2"> </td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>[[Ubiquitin conjugating enzyme]]</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== References ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== References ==</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><references/></div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div><references/></div></td></tr> </table>

Michal Harel http://52.214.119.220/wiki/index.php?title=UBC13_MMS2&diff=2518438&oldid=prev Michal Harel at 07:28, 11 January 2016 2016-01-11T07:28:31Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 07:28, 11 January 2016</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 3:</td> <td colspan="2" class="diff-lineno">Line 3:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Summary==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Summary==</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Ubc13 is an E2 ubiquitin-conjugating enzyme that can form a heterodimer with Mms2 to function as a part of the translesion synthesis (TLS) pathway,<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref><ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>. When bound to Mms2, Ubc13 will polyubiquitinate proliferating cell nuclear antigen (PCNA), a sliding clamp protein at the DNA transcription fork<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref>. Ubc13-Mms2 functions to polyubiquitinate PCNA following the initial monoubiquitination by Rad6-Rad18 (another E2 complex)<ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>. It is important to note that Ubc13 lacks the ability to be catalytically active without Mms2, hinting at inaccuracies within the statement "structure determines function."</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><ins style="color: red; font-weight: bold; text-decoration: none;">'''</ins>Ubc13<ins style="color: red; font-weight: bold; text-decoration: none;">''' </ins>is an <ins style="color: red; font-weight: bold; text-decoration: none;">'''</ins>E2 ubiquitin-conjugating enzyme<ins style="color: red; font-weight: bold; text-decoration: none;">''' </ins>that can form a heterodimer with Mms2 to function as a part of the translesion synthesis (TLS) pathway,<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref><ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>. When bound to Mms2, Ubc13 will polyubiquitinate proliferating cell nuclear antigen (PCNA), a sliding clamp protein at the DNA transcription fork<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref>. Ubc13-Mms2 functions to polyubiquitinate PCNA following the initial monoubiquitination by Rad6-Rad18 (another E2 complex)<ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>. It is important to note that Ubc13 lacks the ability to be catalytically active without Mms2, hinting at inaccuracies within the statement "structure determines function."</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td></tr> </table>

Michal Harel http://52.214.119.220/wiki/index.php?title=UBC13_MMS2&diff=2379638&oldid=prev Nicholas R. Dunham at 20:50, 26 February 2015 2015-02-26T20:50:10Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 20:50, 26 February 2015</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 1:</td> <td colspan="2" class="diff-lineno">Line 1:</td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div><Structure load='1J7D' size='<del style="color: red; font-weight: bold; text-decoration: none;">350</del>' scene='69/695700/Ubc13_mms2_overall/1'></div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div><Structure load='1J7D' size='<ins style="color: red; font-weight: bold; text-decoration: none;">450</ins>' scene='69/695700/Ubc13_mms2_overall/1'></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Summary==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Summary==</div></td></tr> </table>

Nicholas R. Dunham http://52.214.119.220/wiki/index.php?title=UBC13_MMS2&diff=2379622&oldid=prev David A Taves at 15:51, 26 February 2015 2015-02-26T15:51:55Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 15:51, 26 February 2015</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 17:</td> <td colspan="2" class="diff-lineno">Line 17:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>* Another E2 complex, Rad6-Rad18, starts the process of DNA repair by monoubiquitinating PCNA near the replication fork of DNA. This DNA repair will arrest cell cycle progression until DNA repair is complete<ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>* Another E2 complex, Rad6-Rad18, starts the process of DNA repair by monoubiquitinating PCNA near the replication fork of DNA. This DNA repair will arrest cell cycle progression until DNA repair is complete<ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>.</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>* UEV1A, another cofactor enzyme that binds to Ubc13, is thought to compete with Mms2 for binding to Ubc13. This is thought to be a regulatory mechanism for Ubc13 activity in the nucleus of cells<ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>* UEV1A, another cofactor enzyme that binds to Ubc13, is thought to compete with Mms2 for binding to Ubc13. This is thought to be a regulatory mechanism for Ubc13 activity in the nucleus of cells<ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>.</div></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>*Several DNA polymerases such as rev1, pol eta, and pol zeta contain Ubiquitin-binding domains that recognize K164 polyubiquitination of PCNA<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref>.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>*Several DNA polymerases such as rev1, pol eta, and pol zeta contain Ubiquitin-binding domains that recognize <ins style="color: red; font-weight: bold; text-decoration: none;"><scene name='69/695700/Pcna/1'></ins>K164<ins style="color: red; font-weight: bold; text-decoration: none;"></scene> </ins>polyubiquitination of PCNA<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref>.</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>*Rad5, an E3 RING (Really Interesting New Gene) protein, interacts with the Ubc13-Mms2 heterodimer in order to ligate the ubiquitin on the PCNA. Rad5, as well as Rad18 (RING proteins) are involved in the recruitment of Ubc13-Mms2 heterodimer formation<ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>.</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>*Rad5, an E3 RING (Really Interesting New Gene) protein, interacts with the Ubc13-Mms2 heterodimer in order to ligate the ubiquitin on the PCNA. Rad5, as well as Rad18 (RING proteins) are involved in the recruitment of Ubc13-Mms2 heterodimer formation<ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>.</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> </table>

David A Taves http://52.214.119.220/wiki/index.php?title=UBC13_MMS2&diff=2379617&oldid=prev David A Taves at 15:41, 26 February 2015 2015-02-26T15:41:44Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 15:41, 26 February 2015</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 3:</td> <td colspan="2" class="diff-lineno">Line 3:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Summary==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Summary==</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Ubc13 is an E2 ubiquitin-conjugating enzyme that can form a heterodimer with Mms2 to function as a part of the translesion synthesis (TLS) pathway,<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref><ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>. When bound to Mms2, Ubc13 will polyubiquitinate proliferating cell nuclear antigen (PCNA), a sliding clamp protein at the DNA transcription fork<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref>. Ubc13-Mms2 functions to polyubiquitinate PCNA following the initial monoubiquitination by Rad6-Rad18 (another E2 complex)<ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>. It is important to note that Ubc13 lacks the ability to be catalytically active without Mms2, hinting at inaccuracies within the statement "structure determines function<del style="color: red; font-weight: bold; text-decoration: none;">"</del>.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Ubc13 is an E2 ubiquitin-conjugating enzyme that can form a heterodimer with Mms2 to function as a part of the translesion synthesis (TLS) pathway,<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref><ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>. When bound to Mms2, Ubc13 will polyubiquitinate proliferating cell nuclear antigen (PCNA), a sliding clamp protein at the DNA transcription fork<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref>. Ubc13-Mms2 functions to polyubiquitinate PCNA following the initial monoubiquitination by Rad6-Rad18 (another E2 complex)<ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>. It is important to note that Ubc13 lacks the ability to be catalytically active without Mms2, hinting at inaccuracies within the statement "structure determines function.<ins style="color: red; font-weight: bold; text-decoration: none;">"</ins></div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td></tr> </table>

David A Taves http://52.214.119.220/wiki/index.php?title=UBC13_MMS2&diff=2379579&oldid=prev David A Taves at 03:30, 26 February 2015 2015-02-26T03:30:31Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 03:30, 26 February 2015</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 3:</td> <td colspan="2" class="diff-lineno">Line 3:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Summary==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Summary==</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>Ubc13 is an E2 ubiquitin-conjugating enzyme that can form a heterodimer with Mms2 to function as a part of the translesion synthesis (TLS) pathway,<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref><ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>. When bound to Mms2, Ubc13 will polyubiquitinate proliferating cell nuclear antigen (PCNA), a sliding clamp protein at the DNA transcription fork<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref>. Ubc13-Mms2 functions to polyubiquitinate PCNA following the initial monoubiquitination by Rad6-Rad18 (another E2 complex)<ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>.</div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>Ubc13 is an E2 ubiquitin-conjugating enzyme that can form a heterodimer with Mms2 to function as a part of the translesion synthesis (TLS) pathway,<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref><ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref>. When bound to Mms2, Ubc13 will polyubiquitinate proliferating cell nuclear antigen (PCNA), a sliding clamp protein at the DNA transcription fork<ref name=halas>3. Halas, A.; Podlaska, A. F.; Derkacz, J. F.; McIntyre, J. F.; Skoneczna, A. F.; Sledziewska-Gojska, E. The roles of PCNA SUMOylation, Mms2-Ubc13 and Rad5 in translesion DNA synthesis in Saccharomyces cerevisiae. Molecular microbiology JID - 8712028 0809.</ref>. Ubc13-Mms2 functions to polyubiquitinate PCNA following the initial monoubiquitination by Rad6-Rad18 (another E2 complex)<ref name=anderson>1. Andersen, P. L.; Zhou, H. F.; Pastushok, L. F.; Moraes, T. F.; McKenna, S. F.; Ziola B FAU - Ellison, Michael,J.; FAU, E. M.; FAU, D. V.; Xiao, W. Distinct regulation of Ubc13 functions by the two ubiquitin-conjugating enzyme variants Mms2 and Uev1A. The Journal of cell biology JID - 0375356 1107.</ref><ins style="color: red; font-weight: bold; text-decoration: none;">. It is important to note that Ubc13 lacks the ability to be catalytically active without Mms2, hinting at inaccuracies within the statement "structure determines function"</ins>.</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>== Function ==</div></td></tr> </table>

David A Taves http://52.214.119.220/wiki/index.php?title=UBC13_MMS2&diff=2379578&oldid=prev David A Taves at 03:25, 26 February 2015 2015-02-26T03:25:13Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 03:25, 26 February 2015</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 34:</td> <td colspan="2" class="diff-lineno">Line 34:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Mechanism==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Mechanism==</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>The exact mechanism for how Ubc13 transfers ubiquitin is not known, however the mechanism occurs in either a step-wise or concerted reaction. Ubc13, as an E2, froms a covalent bond with ubiquitin and then transfers the ubiquitin to the target protein via a thioester intermediate. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>The exact mechanism for how Ubc13 transfers ubiquitin is not known, however the mechanism occurs in either a step-wise or concerted reaction. Ubc13, as an E2, froms a covalent bond with ubiquitin and then transfers the ubiquitin to the target protein via a thioester intermediate<ins style="color: red; font-weight: bold; text-decoration: none;">. Ubiquitin is removed from Ubc13 and Mms2 complex and placed onto PCNA</ins>.</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> </table>

David A Taves http://52.214.119.220/wiki/index.php?title=UBC13_MMS2&diff=2379576&oldid=prev David A Taves at 03:24, 26 February 2015 2015-02-26T03:24:14Z

<p></p> <table style="background-color: white; color:black;"> <col class='diff-marker' /> <col class='diff-content' /> <col class='diff-marker' /> <col class='diff-content' /> <tr> <td colspan='2' style="background-color: white; color:black;">←Older revision</td> <td colspan='2' style="background-color: white; color:black;">Revision as of 03:24, 26 February 2015</td> </tr> <tr><td colspan="2" class="diff-lineno">Line 34:</td> <td colspan="2" class="diff-lineno">Line 34:</td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Mechanism==</div></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"><div>==Mechanism==</div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'>-</td><td style="background: #ffa; color:black; font-size: smaller;"><div>The exact mechanism for how Ubc13 transfers ubiquitin is not known, however the mechanism occurs in either a step-wise or concerted reaction. </div></td><td class='diff-marker'>+</td><td style="background: #cfc; color:black; font-size: smaller;"><div>The exact mechanism for how Ubc13 transfers ubiquitin is not known, however the mechanism occurs in either a step-wise or concerted reaction<ins style="color: red; font-weight: bold; text-decoration: none;">. Ubc13, as an E2, froms a covalent bond with ubiquitin and then transfers the ubiquitin to the target protein via a thioester intermediate</ins>. </div></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> <tr><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td><td class='diff-marker'> </td><td style="background: #eee; color:black; font-size: smaller;"></td></tr> </table>

David A Taves