7luv: Difference between revisions

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'''Unreleased structure'''


The entry 7luv is ON HOLD
==Cryo-EM structure of the yeast THO-Sub2 complex==
<StructureSection load='7luv' size='340' side='right'caption='[[7luv]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7luv]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_bayanus Saccharomyces bayanus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7LUV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7LUV FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7&#8491;</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=7luv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7luv OCA], [https://pdbe.org/7luv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7luv RCSB], [https://www.ebi.ac.uk/pdbsum/7luv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7luv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/HPR1_YEAST HPR1_YEAST] Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export-competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA.<ref>PMID:12093753</ref> <ref>PMID:12871933</ref> <ref>PMID:14527416</ref> <ref>PMID:15192704</ref>


Authors:  
==See Also==
 
*[[Helicase 3D structures|Helicase 3D structures]]
Description:  
== References ==
[[Category: Unreleased Structures]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces bayanus]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Ren Y]]
[[Category: Xie Y]]

Latest revision as of 18:00, 6 March 2024

Cryo-EM structure of the yeast THO-Sub2 complexCryo-EM structure of the yeast THO-Sub2 complex

Structural highlights

7luv is a 6 chain structure with sequence from Saccharomyces bayanus and Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HPR1_YEAST Component the THO subcomplex of the TREX complex, which operates in coupling transcription elongation to mRNA export. The THO complex is recruited to transcribed genes and moves along the gene with the elongating polymerase during transcription. THO is important for stabilizing nascent RNA in the RNA polymerase II elongation complex by preventing formation of DNA:RNA hybrids behind the elongating polymerase. It functions in cotranscriptional formation of an export-competent messenger ribonucleoprotein particle (mRNP) by facilitating the loading of ATP-dependent RNA helicase SUB2 and the mRNA export factor YRA1 along the nascent mRNA.[1] [2] [3] [4]

See Also

References

  1. ↑ Jimeno S, Rondon AG, Luna R, Aguilera A. The yeast THO complex and mRNA export factors link RNA metabolism with transcription and genome instability. EMBO J. 2002 Jul 1;21(13):3526-35. PMID:12093753 doi:http://dx.doi.org/10.1093/emboj/cdf335
  2. ↑ Rondon AG, Jimeno S, Garcia-Rubio M, Aguilera A. Molecular evidence that the eukaryotic THO/TREX complex is required for efficient transcription elongation. J Biol Chem. 2003 Oct 3;278(40):39037-43. Epub 2003 Jul 18. PMID:12871933 doi:http://dx.doi.org/10.1074/jbc.M305718200
  3. ↑ Huertas P, Aguilera A. Cotranscriptionally formed DNA:RNA hybrids mediate transcription elongation impairment and transcription-associated recombination. Mol Cell. 2003 Sep;12(3):711-21. PMID:14527416
  4. ↑ Abruzzi KC, Lacadie S, Rosbash M. Biochemical analysis of TREX complex recruitment to intronless and intron-containing yeast genes. EMBO J. 2004 Jul 7;23(13):2620-31. Epub 2004 Jun 10. PMID:15192704 doi:http://dx.doi.org/10.1038/sj.emboj.7600261

7luv, resolution 3.70Å

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