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4bjj

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Revision as of 23:11, 24 December 2014

Sfc1-Sfc7 dimerization module

Structural highlights

4bjj is a 2 chain structure with sequence from Schizosaccharomyces pombe. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4bji
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[SFC1_SCHPO] TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes. Participates in the interconnection of tauA with tauB via its contacts with sfc3 and sfc6. Serves as a scaffold critical for tauA-DNA spatial configuration and tauB-DNA stability. Localizes to chromatin insulator sequence without recruiting RNA polymerase III and plays a role in nuclear organization.^[1] ^[2] [SFC7_SCHPO] TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes (By similarity).[UniProtKB:Q12415]

Publication Abstract from PubMed

Transcription of tRNA-encoding genes by RNA polymerase (Pol) III requires the six-subunit general transcription factor IIIC that uses subcomplexes tauA and tauB to recognize two gene-internal promoter elements named A- and B-box. The Schizosaccharomyces pombe tauA subcomplex comprises subunits Sfc1, Sfc4 and Sfc7. The crystal structure of the Sfc1/Sfc7 heterodimer reveals similar domains and overall domain architecture to the Pol II-specific general transcription factor TFIIF Rap30/Rap74. The N-terminal Sfc1/Sfc7 dimerization module consists of a triple beta-barrel similar to the N-terminal TFIIF Rap30/Rap74 dimerization module, whereas the C-terminal Sfc1 DNA-binding domain contains a winged-helix domain most similar to the TFIIF Rap30 C-terminal winged-helix domain. Sfc1 DNA-binding domain recognizes single and double-stranded DNA by an unknown mechanism. Several features observed for A-box recognition by tauA resemble the recognition of promoters by bacterial RNA polymerase, where sigma factor unfolds double-stranded DNA and stabilizes the non-coding DNA strand in an open conformation. Such a function has also been proposed for TFIIF, suggesting that the observed structural similarity between Sfc1/Sfc7 and TFIIF Rap30/Rap74 might also reflect similar functions.

RNA polymerase III-specific general transcription factor IIIC contains a heterodimer resembling TFIIF Rap30/Rap74.,Taylor NM, Baudin F, von Scheven G, Muller CW Nucleic Acids Res. 2013 Aug 5. PMID:23921640^[3]

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

References

↑ Huang Y, Hamada M, Maraia RJ. Isolation and cloning of four subunits of a fission yeast TFIIIC complex that includes an ortholog of the human regulatory protein TFIIICbeta. J Biol Chem. 2000 Oct 6;275(40):31480-7. PMID:10906331 doi:10.1074/jbc.M004635200
↑ Noma K, Cam HP, Maraia RJ, Grewal SI. A role for TFIIIC transcription factor complex in genome organization. Cell. 2006 Jun 2;125(5):859-72. PMID:16751097 doi:10.1016/j.cell.2006.04.028
↑ Taylor NM, Baudin F, von Scheven G, Muller CW. RNA polymerase III-specific general transcription factor IIIC contains a heterodimer resembling TFIIF Rap30/Rap74. Nucleic Acids Res. 2013 Aug 5. PMID:23921640 doi:10.1093/nar/gkt664

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4bjj"

@@ Line 7: / Line 7: @@
 <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=4bjj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bjj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4bjj RCSB], [http://www.ebi.ac.uk/pdbsum/4bjj PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/SFC1_SCHPO SFC1_SCHPO]] TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes. Participates in the interconnection of tauA with tauB via its contacts with sfc3 and sfc6. Serves as a scaffold critical for tauA-DNA spatial configuration and tauB-DNA stability. Localizes to chromatin insulator sequence without recruiting RNA polymerase III and plays a role in nuclear organization.<ref>PMID:10906331</ref> <ref>PMID:16751097</ref>  [[http://www.uniprot.org/uniprot/SFC7_SCHPO SFC7_SCHPO]] TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes (By similarity).[UniProtKB:Q12415]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4bjj

From Proteopedia

Revision as of 23:11, 24 December 2014

Sfc1-Sfc7 dimerization module

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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