2n1g - Revision history

OCA at 07:03, 1 May 2024

2024-05-01T07:03:27Z

←Older revision		Revision as of 07:03, 1 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[2n1g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N1G FirstGlance]. <br>		<table><tr><td colspan='2'>[[2n1g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N1G FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1g OCA], [https://pdbe.org/2n1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n1g RCSB], [https://www.ebi.ac.uk/pdbsum/2n1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1g ProSAT]</span></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1g OCA], [https://pdbe.org/2n1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n1g RCSB], [https://www.ebi.ac.uk/pdbsum/2n1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[https://www.uniprot.org/uniprot/REV1_HUMAN REV1_HUMAN] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:10536157</ref> <ref>PMID:10760286</ref> <ref>PMID:11278384</ref> <ref>PMID:11485998</ref> <ref>PMID:22266823</ref>		[https://www.uniprot.org/uniprot/REV1_HUMAN REV1_HUMAN] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:10536157</ref> <ref>PMID:10760286</ref> <ref>PMID:11278384</ref> <ref>PMID:11485998</ref> <ref>PMID:22266823</ref>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Translesion synthesis (TLS) is a mutagenic branch of cellular DNA damage tolerance that enables bypass replication over DNA lesions carried out by specialized low-fidelity DNA polymerases. The replicative bypass of most types of DNA damage is performed in a two-step process of Rev1/Polzeta-dependent TLS. In the first step, a Y-family TLS enzyme, typically Poleta, Poliota, or Polkappa, inserts a nucleotide across a DNA lesion. In the second step, a four-subunit B-family DNA polymerase Polzeta (Rev3/Rev7/PolD2/PolD3 complex) extends the distorted DNA primer-template. The coordinated action of error-prone TLS enzymes is regulated through their interactions with the two scaffold proteins, the sliding clamp PCNA and the TLS polymerase Rev1. Rev1 interactions with all other TLS enzymes are mediated by its C-terminal domain (Rev1-CT), which can simultaneously bind the Rev7 subunit of Polzeta and Rev1-interacting regions (RIRs) from Poleta, Poliota, or Polkappa. In this work, we identified a previously unknown RIR motif in the C-terminal part of PolD3 subunit of Polzeta whose interaction with the Rev1-CT is among the tightest mediated by RIR motifs. Three-dimensional structure of the Rev1-CT/PolD3-RIR complex determined by NMR spectroscopy revealed a structural basis for the relatively high affinity of this interaction. The unexpected discovery of PolD3-RIR motif suggests a mechanism of "inserter" to "extender" DNA polymerase switch upon Rev1/Polzeta-dependent TLS, in which the PolD3-RIR binding to the Rev1-CT (i) helps displace the "inserter" Poleta, Poliota, or Polkappa from its complex with Rev1, and (ii) facilitates assembly of the four-subunit "extender" Polzeta through simultaneous interaction of Rev1-CT with Rev7 and PolD3 subunits.
-
-	Interaction between the Rev1 C-Terminal Domain and the PolD3 Subunit of Polzeta Suggests a Mechanism of Polymerase Exchange upon Rev1/Polzeta-Dependent Translesion Synthesis.,Pustovalova Y, Magalhaes MT, D'Souza S, Rizzo AA, Korza G, Walker GC, Korzhnev DM Biochemistry. 2016 Apr 5;55(13):2043-53. doi: 10.1021/acs.biochem.5b01282. Epub, 2016 Mar 24. PMID:26982350<ref>PMID:26982350</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 2n1g" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 08:13, 8 March 2023

2023-03-08T08:13:39Z

←Older revision		Revision as of 08:13, 8 March 2023
Line 1:		Line 1:

	==Structure of C-terminal domain of human polymerase Rev1 in complex with PolD3 RIR-motif==		==Structure of C-terminal domain of human polymerase Rev1 in complex with PolD3 RIR-motif==
-	<StructureSection load='2n1g' size='340' side='right'caption='[[2n1g~~]], [[NMR_Ensembles_of_Models \| 20 NMR models~~]]' scene=''>	+	<StructureSection load='2n1g' size='340' side='right'caption='[[2n1g]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2n1g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N1G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2n1g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N1G FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">REV1, REV1L ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), KIAA0039, POLD3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1g OCA], [https://pdbe.org/2n1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n1g RCSB], [https://www.ebi.ac.uk/pdbsum/2n1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1g ProSAT]</span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1g OCA], [https://pdbe.org/2n1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n1g RCSB], [https://www.ebi.ac.uk/pdbsum/2n1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1g ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/REV1_HUMAN REV1_HUMAN]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:10536157</ref> <ref>PMID:10760286</ref> <ref>PMID:11278384</ref> <ref>PMID:11485998</ref> <ref>PMID:22266823</ref> ~~[[https://www.uniprot.org/uniprot/DPOD3_HUMAN DPOD3_HUMAN]] Required for optimal DNA polymerase delta activity.<ref>PMID:10219083</ref> <ref>PMID:10852724</ref> <ref>PMID:16510448</ref>~~	+	[https://www.uniprot.org/uniprot/REV1_HUMAN REV1_HUMAN] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:10536157</ref> <ref>PMID:10760286</ref> <ref>PMID:11278384</ref> <ref>PMID:11485998</ref> <ref>PMID:22266823</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 18:		Line 17:
	</div>		</div>
	<div class="pdbe-citations 2n1g" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 2n1g" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[DNA polymerase 3D structures\|DNA polymerase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Korzhnev, D]]	+	[[Category: Korzhnev D]]
-	[[Category: Pustovalova, Y]]	+	[[Category: Pustovalova Y]]
-	~~[[Category: Pold3]]~~	+
-	~~[[Category: Rev1]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 15:25, 2 June 2021

2021-06-02T15:25:11Z

←Older revision		Revision as of 15:25, 2 June 2021
Line 1:		Line 1:

	==Structure of C-terminal domain of human polymerase Rev1 in complex with PolD3 RIR-motif==		==Structure of C-terminal domain of human polymerase Rev1 in complex with PolD3 RIR-motif==
-	<StructureSection load='2n1g' size='340' side='right' caption='[[2n1g]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>	+	<StructureSection load='2n1g' size='340' side='right'caption='[[2n1g]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2n1g]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1G OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2N1G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2n1g]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N1G FirstGlance]. <br>
-	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">REV1, REV1L ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), KIAA0039, POLD3 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">REV1, REV1L ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), KIAA0039, POLD3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2n1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1g OCA], [~~http~~://pdbe.org/2n1g PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2n1g RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2n1g PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1g ProSAT]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2n1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1g OCA], [https://pdbe.org/2n1g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n1g RCSB], [https://www.ebi.ac.uk/pdbsum/2n1g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/REV1_HUMAN REV1_HUMAN]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:10536157</ref> <ref>PMID:10760286</ref> <ref>PMID:11278384</ref> <ref>PMID:11485998</ref> <ref>PMID:22266823</ref> [[~~http~~://www.uniprot.org/uniprot/DPOD3_HUMAN DPOD3_HUMAN]] Required for optimal DNA polymerase delta activity.<ref>PMID:10219083</ref> <ref>PMID:10852724</ref> <ref>PMID:16510448</ref>	+	[[https://www.uniprot.org/uniprot/REV1_HUMAN REV1_HUMAN]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:10536157</ref> <ref>PMID:10760286</ref> <ref>PMID:11278384</ref> <ref>PMID:11485998</ref> <ref>PMID:22266823</ref> [[https://www.uniprot.org/uniprot/DPOD3_HUMAN DPOD3_HUMAN]] Required for optimal DNA polymerase delta activity.<ref>PMID:10219083</ref> <ref>PMID:10852724</ref> <ref>PMID:16510448</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 23:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Korzhnev, D]]		[[Category: Korzhnev, D]]
	[[Category: Pustovalova, Y]]		[[Category: Pustovalova, Y]]

OCA at 12:52, 16 November 2017

2017-11-16T12:52:11Z

←Older revision		Revision as of 12:52, 16 November 2017
Line 3:		Line 3:
	<StructureSection load='2n1g' size='340' side='right' caption='[[2n1g]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>		<StructureSection load='2n1g' size='340' side='right' caption='[[2n1g]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[2n1g]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N1G FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[2n1g]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N1G FirstGlance]. <br>
-	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1g OCA], [http://pdbe.org/2n1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n1g RCSB], [http://www.ebi.ac.uk/pdbsum/2n1g PDBsum]</span></td></tr>	+	</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">REV1, REV1L ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), KIAA0039, POLD3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1g OCA], [http://pdbe.org/2n1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n1g RCSB], [http://www.ebi.ac.uk/pdbsum/2n1g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2n1g ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 21:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Korzhnev, D]]		[[Category: Korzhnev, D]]
	[[Category: Pustovalova, Y]]		[[Category: Pustovalova, Y]]

OCA at 17:51, 10 May 2016

2016-05-10T17:51:09Z

←Older revision		Revision as of 17:51, 10 May 2016
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry~~ 2n1g is ~~ON HOLD~~ ~~until Paper~~ Publication	+	==Structure of C-terminal domain of human polymerase Rev1 in complex with PolD3 RIR-motif==
		+	<StructureSection load='2n1g' size='340' side='right' caption='[[2n1g]], [[NMR_Ensembles_of_Models \| 20 NMR models]]' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[2n1g]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N1G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2N1G FirstGlance]. <br>
		+	</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2n1g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n1g OCA], [http://pdbe.org/2n1g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2n1g RCSB], [http://www.ebi.ac.uk/pdbsum/2n1g PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/REV1_HUMAN REV1_HUMAN]] Deoxycytidyl transferase involved in DNA repair. Transfers a dCMP residue from dCTP to the 3'-end of a DNA primer in a template-dependent reaction. May assist in the first step in the bypass of abasic lesions by the insertion of a nucleotide opposite the lesion. Required for normal induction of mutations by physical and chemical agents.<ref>PMID:10536157</ref> <ref>PMID:10760286</ref> <ref>PMID:11278384</ref> <ref>PMID:11485998</ref> <ref>PMID:22266823</ref> [[http://www.uniprot.org/uniprot/DPOD3_HUMAN DPOD3_HUMAN]] Required for optimal DNA polymerase delta activity.<ref>PMID:10219083</ref> <ref>PMID:10852724</ref> <ref>PMID:16510448</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Translesion synthesis (TLS) is a mutagenic branch of cellular DNA damage tolerance that enables bypass replication over DNA lesions carried out by specialized low-fidelity DNA polymerases. The replicative bypass of most types of DNA damage is performed in a two-step process of Rev1/Polzeta-dependent TLS. In the first step, a Y-family TLS enzyme, typically Poleta, Poliota, or Polkappa, inserts a nucleotide across a DNA lesion. In the second step, a four-subunit B-family DNA polymerase Polzeta (Rev3/Rev7/PolD2/PolD3 complex) extends the distorted DNA primer-template. The coordinated action of error-prone TLS enzymes is regulated through their interactions with the two scaffold proteins, the sliding clamp PCNA and the TLS polymerase Rev1. Rev1 interactions with all other TLS enzymes are mediated by its C-terminal domain (Rev1-CT), which can simultaneously bind the Rev7 subunit of Polzeta and Rev1-interacting regions (RIRs) from Poleta, Poliota, or Polkappa. In this work, we identified a previously unknown RIR motif in the C-terminal part of PolD3 subunit of Polzeta whose interaction with the Rev1-CT is among the tightest mediated by RIR motifs. Three-dimensional structure of the Rev1-CT/PolD3-RIR complex determined by NMR spectroscopy revealed a structural basis for the relatively high affinity of this interaction. The unexpected discovery of PolD3-RIR motif suggests a mechanism of "inserter" to "extender" DNA polymerase switch upon Rev1/Polzeta-dependent TLS, in which the PolD3-RIR binding to the Rev1-CT (i) helps displace the "inserter" Poleta, Poliota, or Polkappa from its complex with Rev1, and (ii) facilitates assembly of the four-subunit "extender" Polzeta through simultaneous interaction of Rev1-CT with Rev7 and PolD3 subunits.

-	~~Authors: Pustovalova~~, Y., ~~Korzhnev~~, D.	+	Interaction between the Rev1 C-Terminal Domain and the PolD3 Subunit of Polzeta Suggests a Mechanism of Polymerase Exchange upon Rev1/Polzeta-Dependent Translesion Synthesis.,Pustovalova Y, Magalhaes MT, D'Souza S, Rizzo AA, Korza G, Walker GC, Korzhnev DM Biochemistry. 2016 Apr 5;55(13):2043-53. doi: 10.1021/acs.biochem.5b01282. Epub, 2016 Mar 24. PMID:26982350<ref>PMID:26982350</ref>

-	~~Description: Structure~~ of ~~C-terminal domain~~ of ~~human polymerase Rev1 in complex with PolD3 RIR-motif~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[Category: Unreleased Structures]]~~	+	</div>
-	~~[[Category~~: ~~Pustovalova, Y]]~~	+	<div class="pdbe-citations 2n1g" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Korzhnev, D]]		[[Category: Korzhnev, D]]
		+	[[Category: Pustovalova, Y]]
		+	[[Category: Pold3]]
		+	[[Category: Rev1]]
		+	[[Category: Transferase]]

OCA at 10:35, 27 May 2015

2015-05-27T10:35:37Z

←Older revision		Revision as of 10:35, 27 May 2015
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 2n1g is ON HOLD	+	The entry 2n1g is ON HOLD until Paper Publication

	Authors: Pustovalova, Y., Korzhnev, D.		Authors: Pustovalova, Y., Korzhnev, D.

OCA: Protected "2n1g" [edit=sysop:move=sysop]

2015-04-08T06:03:47Z

Protected "2n1g" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:03, 8 April 2015

OCA: New page: '''Unreleased structure''' The entry 2n1g is ON HOLD Authors: Pustovalova, Y., Korzhnev, D. Description: Structure of C-terminal domain of human polymerase Rev1 in complex with PolD3 R...

2015-04-08T06:03:46Z

New page: '''Unreleased structure''' The entry 2n1g is ON HOLD Authors: Pustovalova, Y., Korzhnev, D. Description: Structure of C-terminal domain of human polymerase Rev1 in complex with PolD3 R...

New page

'''Unreleased structure'''

The entry 2n1g is ON HOLD

Authors: Pustovalova, Y., Korzhnev, D.

Description: Structure of C-terminal domain of human polymerase Rev1 in complex with PolD3 RIR-motif
[[Category: Unreleased Structures]]
[[Category: Pustovalova, Y]]
[[Category: Korzhnev, D]]