5l3t

From Proteopedia

(Difference between revisions)

Revision as of 08:22, 10 October 2018

Structure of the Saccharomyces cerevisiae TREX-2 complex

Structural highlights

5l3t is a 6 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:	SAC3, LEP1, YDR159W, YD8358.13 (ATCC 18824), THP1, BUD29, YOL072W, O1140 (ATCC 18824), SEM1, DSH1, YDR363W-A (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SAC3_YEAST] Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket.^[1] ^[2] [SEM1_YEAST] Versatile protein that might stabilize multiple protein complexes involved in diverse pathways. Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis. Associates also with the TREX-2 complex that is required for transcription-coupled mRNA export, and the COP9 signalosome, which is involved in deneddylation.^[3] ^[4] [THP1_YEAST] Component of the SAC3-THP1 complex, which functions in transcription-coupled mRNA export from the nucleus to the cytoplasm. SAC3-THP1 functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. THP1 binds to RNA in vitro.^[5] ^[6] ^[7]

Publication Abstract from PubMed

Transcription-export complex 2 (TREX-2 complex) facilitates the localization of actively transcribing genes to the nuclear periphery and also functions to contribute to the generation of export-competent mRNPs through interactions with the general mRNA nuclear export factor Mex67:Mtr2. The TREX-2 complex is based on a Sac3 scaffold to which Thp1, Sem1, Cdc31, and Sus1 bind. TREX-2 can be subdivided into two modules: one, in which Thp1 and Sem1 bind to the Sac3M region (residues approximately 100-551), and the other in which Cdc31 and two Sus1 chains bind to the Sac3CID region (residues approximately 710-805). Complementary structural analyses using X-ray crystallography, electron microscopy, and small-angle X-ray scattering of the Saccharomyces cerevisiae TREX-2 complex, expressed using Baculovirus-infected Sf9 cells, have indicated that the TPR-like repeats of the Sac3M region extend considerably further towards the N-terminus than previously thought, and also indicate that this region and Sac3CID:Sus1:Cdc31 region of the S. cerevisiae complex are structurally independent. Although the density visible accounted for only approximately 100kDa, a 5.3A resolution cryo-EM reconstruction was obtained of the M-region of TREX-2 that showed an additional three putative alpha-helices extending towards the Sac3 N-terminus and these helices were also seen in a 4.9A resolution structure obtained by X-ray crystallography. SUMMARY STATEMENT: We describe the expression, purification and structural characterization of the S. cerevisiae TREX-2 complex and demonstrate that the Sac3 TPR-like repeats are more extensive than previously thought and that the M- and CID-regions do not appear to have a defined spatial orientation.

The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region.,Aibara S, Bai XC, Stewart M J Struct Biol. 2016 Jul 12. pii: S1047-8477(16)30148-4. doi:, 10.1016/j.jsb.2016.07.007. PMID:27422657^[8]

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

References

↑ Fischer T, Strasser K, Racz A, Rodriguez-Navarro S, Oppizzi M, Ihrig P, Lechner J, Hurt E. The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores. EMBO J. 2002 Nov 1;21(21):5843-52. PMID:12411502
↑ Gallardo M, Luna R, Erdjument-Bromage H, Tempst P, Aguilera A. Nab2p and the Thp1p-Sac3p complex functionally interact at the interface between transcription and mRNA metabolism. J Biol Chem. 2003 Jun 27;278(26):24225-32. Epub 2003 Apr 17. PMID:12702719 doi:http://dx.doi.org/10.1074/jbc.M302900200
↑ Faza MB, Kemmler S, Jimeno S, Gonzalez-Aguilera C, Aguilera A, Hurt E, Panse VG. Sem1 is a functional component of the nuclear pore complex-associated messenger RNA export machinery. J Cell Biol. 2009 Mar 23;184(6):833-46. doi: 10.1083/jcb.200810059. Epub 2009 Mar, 16. PMID:19289793 doi:http://dx.doi.org/10.1083/jcb.200810059
↑ Sone T, Saeki Y, Toh-e A, Yokosawa H. Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae. J Biol Chem. 2004 Jul 2;279(27):28807-16. Epub 2004 Apr 26. PMID:15117943 doi:http://dx.doi.org/10.1074/jbc.M403165200
↑ Gallardo M, Aguilera A. A new hyperrecombination mutation identifies a novel yeast gene, THP1, connecting transcription elongation with mitotic recombination. Genetics. 2001 Jan;157(1):79-89. PMID:11139493
↑ Fischer T, Strasser K, Racz A, Rodriguez-Navarro S, Oppizzi M, Ihrig P, Lechner J, Hurt E. The mRNA export machinery requires the novel Sac3p-Thp1p complex to dock at the nucleoplasmic entrance of the nuclear pores. EMBO J. 2002 Nov 1;21(21):5843-52. PMID:12411502
↑ Gallardo M, Luna R, Erdjument-Bromage H, Tempst P, Aguilera A. Nab2p and the Thp1p-Sac3p complex functionally interact at the interface between transcription and mRNA metabolism. J Biol Chem. 2003 Jun 27;278(26):24225-32. Epub 2003 Apr 17. PMID:12702719 doi:http://dx.doi.org/10.1074/jbc.M302900200
↑ Aibara S, Bai XC, Stewart M. The Sac3 TPR-like region in the Saccharomyces cerevisiae TREX-2 complex is more extensive but independent of the CID region. J Struct Biol. 2016 Jul 12. pii: S1047-8477(16)30148-4. doi:, 10.1016/j.jsb.2016.07.007. PMID:27422657 doi:http://dx.doi.org/10.1016/j.jsb.2016.07.007

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5l3t"

@@ Line 3: / Line 3: @@
 <StructureSection load='5l3t' size='340' side='right' caption='[[5l3t]], [[Resolution|resolution]] 4.93&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5l3t]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L3T FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5l3t]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5L3T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5L3T FirstGlance]. <br>
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SAC3, LEP1, YDR159W, YD8358.13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), THP1, BUD29, YOL072W, O1140 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), SEM1, DSH1, YDR363W-A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=5l3t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5l3t OCA], [http://pdbe.org/5l3t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5l3t RCSB], [http://www.ebi.ac.uk/pdbsum/5l3t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5l3t ProSAT]</span></td></tr>
 </table>
@@ Line 18: / Line 19: @@
 </div>
 <div class="pdbe-citations 5l3t" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Proteasome|Proteasome]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Atcc 18824]]
 [[Category: Aibara, S]]
 [[Category: Stewart, M]]

5l3t

From Proteopedia

Revision as of 08:22, 10 October 2018

Structure of the Saccharomyces cerevisiae TREX-2 complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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