3t5v

From Proteopedia

(Difference between revisions)

Revision as of 16:44, 6 July 2022

Sac3:Thp1:Sem1 complex

Structural highlights

3t5v 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.
Gene:	LEP1, SAC3, YD8358.13, YDR159W (ATCC 18824), BUD29, O1140, THP1, YOL072W (ATCC 18824), DSH1, SEM1, 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

The conserved TREX-2 transcription-export complex integrates transcription and processing of many actively transcribed nascent mRNAs with the recruitment of export factors at nuclear pores and also contributes to transcriptional memory and genomic stability. We report the crystal structure of the Sac3-Thp1-Sem1 segment of Saccharomyces cerevisiae TREX-2 that interfaces with the gene expression machinery. Sac3-Thp1-Sem1 forms a previously uncharacterized PCI-domain complex characterized by the juxtaposition of Sac3 and Thp1 winged helix domains, forming a platform that mediates nucleic acid binding. Our structure-guided mutations support the idea that the Thp1-Sac3 interaction is an essential requirement for mRNA binding and for the coupling of transcription and processing to mRNP assembly and export. These results provide insight into how newly synthesized transcripts are efficiently transferred from TREX-2 to the principal mRNA export factor, and they reveal how Sem1 stabilizes PCI domain-containing proteins and promotes complex assembly.

Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex.,Ellisdon AM, Dimitrova L, Hurt E, Stewart M Nat Struct Mol Biol. 2012 Feb 19;19(3):328-36. doi: 10.1038/nsmb.2235. PMID:22343721^[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
↑ Ellisdon AM, Dimitrova L, Hurt E, Stewart M. Structural basis for the assembly and nucleic acid binding of the TREX-2 transcription-export complex. Nat Struct Mol Biol. 2012 Feb 19;19(3):328-36. doi: 10.1038/nsmb.2235. PMID:22343721 doi:10.1038/nsmb.2235

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/3t5v"

@@ Line 1: / Line 1: @@
 ==Sac3:Thp1:Sem1 complex==
-<StructureSection load='3t5v' size='340' side='right' caption='[[3t5v]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+<StructureSection load='3t5v' size='340' side='right'caption='[[3t5v]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3t5v]] 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=3T5V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T5V FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3t5v]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T5V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T5V FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LEP1, SAC3, YD8358.13, YDR159W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), BUD29, O1140, THP1, YOL072W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), DSH1, SEM1, YDR363W-A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LEP1, SAC3, YD8358.13, YDR159W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), BUD29, O1140, THP1, YOL072W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824]), DSH1, SEM1, YDR363W-A ([https://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=3t5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t5v OCA], [http://pdbe.org/3t5v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t5v RCSB], [http://www.ebi.ac.uk/pdbsum/3t5v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t5v 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=3t5v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t5v OCA], [https://pdbe.org/3t5v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t5v RCSB], [https://www.ebi.ac.uk/pdbsum/3t5v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t5v ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SAC3_YEAST 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.<ref>PMID:12411502</ref> <ref>PMID:12702719</ref>  [[http://www.uniprot.org/uniprot/SEM1_YEAST 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.<ref>PMID:19289793</ref> <ref>PMID:15117943</ref>  [[http://www.uniprot.org/uniprot/THP1_YEAST 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.<ref>PMID:11139493</ref> <ref>PMID:12411502</ref> <ref>PMID:12702719</ref>
+[[https://www.uniprot.org/uniprot/SAC3_YEAST 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.<ref>PMID:12411502</ref> <ref>PMID:12702719</ref>  [[https://www.uniprot.org/uniprot/SEM1_YEAST 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.<ref>PMID:19289793</ref> <ref>PMID:15117943</ref>  [[https://www.uniprot.org/uniprot/THP1_YEAST 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.<ref>PMID:11139493</ref> <ref>PMID:12411502</ref> <ref>PMID:12702719</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 20: / Line 20: @@
 ==See Also==
-*[[Proteasome|Proteasome]]
+*[[Proteasome 3D structures|Proteasome 3D structures]]
 == References ==
 <references/>
@@ Line 26: / Line 26: @@
 </StructureSection>
 [[Category: Atcc 18824]]
+[[Category: Large Structures]]
 [[Category: Ellisdon, A M]]
 [[Category: Stewart, M]]

3t5v

From Proteopedia

Revision as of 16:44, 6 July 2022

Sac3:Thp1:Sem1 complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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