This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

2k06

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 12:55, 10 September 2015

Solution structure of the aminoterminal domain of E. coli NusG

Structural highlights

2k06 is a 1 chain structure with sequence from Escherichia coli. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	nusG (Escherichia coli)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[NUSG_ECOLI] Participates in transcription elongation, termination and antitermination. In the absence of Rho, increases the rate of transcription elongation by the RNA polymerase (RNAP), probably by partially suppressing pausing. In the presence of Rho, modulates most Rho-dependent termination events by interacting with the RNAP to render the complex more susceptible to the termination activity of Rho. May be required to overcome a kinetic limitation of Rho to function at certain terminators. Also involved in ribosomal RNA and phage lambda N-mediated transcriptional antitermination.^[1] ^[2] ^[3] ^[4] ^[5] ^[6] ^[7] ^[8] ^[9]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

NusG is a conserved regulatory protein that interacts with elongation complexes (ECs) of RNA polymerase, DNA, and RNA to modulate transcription in multiple and sometimes opposite ways. In Escherichia coli, NusG suppresses pausing and increases elongation rate, enhances termination by E. coli rho and phage HK022 Nun protein, and promotes antitermination by lambdaN and in ribosomal RNA operons. We report NMR studies that suggest that E. coli NusG consists of two largely independent N- and C-terminal structural domains, NTD and CTD, respectively. Based on tests of the functions of the NTD and CTD and variants of NusG in vivo and in vitro, we find that NTD alone is sufficient to suppress pausing and enhance transcript elongation in vitro. However, neither domain alone can enhance rho-dependent termination or support antitermination, indicating that interactions of both domains with ECs are required for these processes. We propose that the two domains of NusG mediate distinct interactions with ECs: the NTD interacts with RNA polymerase and the CTD interacts with rho and other regulators, providing NusG with different combinations of interactions to effect different regulatory outcomes.

Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators.,Mooney RA, Schweimer K, Rosch P, Gottesman M, Landick R J Mol Biol. 2009 Aug 14;391(2):341-58. Epub 2009 Jun 3. PMID:19500594^[10]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Li J, Horwitz R, McCracken S, Greenblatt J. NusG, a new Escherichia coli elongation factor involved in transcriptional antitermination by the N protein of phage lambda. J Biol Chem. 1992 Mar 25;267(9):6012-9. PMID:1532577
↑ Sullivan SL, Gottesman ME. Requirement for E. coli NusG protein in factor-dependent transcription termination. Cell. 1992 Mar 6;68(5):989-94. PMID:1547498
↑ Nehrke KW, Zalatan F, Platt T. NusG alters rho-dependent termination of transcription in vitro independent of kinetic coupling. Gene Expr. 1993;3(2):119-33. PMID:7505669
↑ Li J, Mason SW, Greenblatt J. Elongation factor NusG interacts with termination factor rho to regulate termination and antitermination of transcription. Genes Dev. 1993 Jan;7(1):161-72. PMID:8422985
↑ Burova E, Hung SC, Sagitov V, Stitt BL, Gottesman ME. Escherichia coli NusG protein stimulates transcription elongation rates in vivo and in vitro. J Bacteriol. 1995 Mar;177(5):1388-92. PMID:7868616
↑ Burns CM, Richardson JP. NusG is required to overcome a kinetic limitation to Rho function at an intragenic terminator. Proc Natl Acad Sci U S A. 1995 May 23;92(11):4738-42. PMID:7761393
↑ Zellars M, Squires CL. Antiterminator-dependent modulation of transcription elongation rates by NusB and NusG. Mol Microbiol. 1999 Jun;32(6):1296-304. PMID:10383769
↑ Pasman Z, von Hippel PH. Regulation of rho-dependent transcription termination by NusG is specific to the Escherichia coli elongation complex. Biochemistry. 2000 May 9;39(18):5573-85. PMID:10820031
↑ Torres M, Balada JM, Zellars M, Squires C, Squires CL. In vivo effect of NusB and NusG on rRNA transcription antitermination. J Bacteriol. 2004 Mar;186(5):1304-10. PMID:14973028
↑ Mooney RA, Schweimer K, Rosch P, Gottesman M, Landick R. Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators. J Mol Biol. 2009 Aug 14;391(2):341-58. Epub 2009 Jun 3. PMID:19500594 doi:http://dx.doi.org/10.1016/j.jmb.2009.05.078

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2k06"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[2k06]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K06 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2K06 FirstGlance]. <br>
 </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">nusG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</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=2k06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k06 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2k06 RCSB], [http://www.ebi.ac.uk/pdbsum/2k06 PDBsum]</span></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=2k06 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k06 OCA], [http://pdbe.org/2k06 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2k06 RCSB], [http://www.ebi.ac.uk/pdbsum/2k06 PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 26: / Line 26: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2k06" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

2k06

From Proteopedia

Revision as of 12:55, 10 September 2015

Solution structure of the aminoterminal domain of E. coli NusG

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox