3oak

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Crystal structure of a Spn1 (Iws1)-Spt6 complexCrystal structure of a Spn1 (Iws1)-Spt6 complex

Structural highlights

3oak is a 4 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:IWS1, SPN1, YPR133C (ATCC 18824), SPT6, CRE2, SSN20, YGR116W, G6169 (ATCC 18824)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[IWS1_YEAST] Transcription factor involved in RNA polymerase II transcription regulation. May function in both SPT15/TBP post-recruitment and recruitment steps of transcription.[1] [2] [SPT6_YEAST] Plays a role in maintenance of chromatin structure during RNA polymerase II transcription elongation thereby repressing transcription initiation from cryptic promoters. Mediates the reassembly of nucleosomes onto the promoters of at least a selected set of genes during repression; the nucleosome reassembly is essential for transcriptional repression. Essential for viability.[3] [4] [5] [6]

Publication Abstract from PubMed

Eukaryotic transcription and mRNA processing depend upon the coordinated interactions of many proteins, including Spn1 and Spt6, which are conserved across eukaryotes, are essential for viability, and associate with each other in some of their biologically important contexts. Here we report crystal structures of the Spn1 core alone and in complex with the binding determinant of Spt6. Mutating interface residues greatly diminishes binding in vitro and causes strong phenotypes in vivo, including a defect in maintaining repressive chromatin. Overexpression of Spn1 partially suppresses the defects caused by an spt6 mutation affecting the Spn1 interface, indicating that the Spn1-Spt6 interaction is important for managing chromatin. Spt6 binds nucleosomes directly in vitro, and this interaction is blocked by Spn1, providing further mechanistic insight into the function of the interaction. These data thereby reveal the structural and biochemical bases of molecular interactions that function in the maintenance of chromatin structure.

Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding.,McDonald SM, Close D, Xin H, Formosa T, Hill CP Mol Cell. 2010 Dec 10;40(5):725-35. Epub 2010 Nov 25. PMID:21094070[7]

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

See Also

References

  1. ↑ Fischbeck JA, Kraemer SM, Stargell LA. SPN1, a conserved gene identified by suppression of a postrecruitment-defective yeast TATA-binding protein mutant. Genetics. 2002 Dec;162(4):1605-16. PMID:12524336
  2. ↑ Lindstrom DL, Squazzo SL, Muster N, Burckin TA, Wachter KC, Emigh CA, McCleery JA, Yates JR 3rd, Hartzog GA. Dual roles for Spt5 in pre-mRNA processing and transcription elongation revealed by identification of Spt5-associated proteins. Mol Cell Biol. 2003 Feb;23(4):1368-78. PMID:12556496
  3. ↑ Hartzog GA, Wada T, Handa H, Winston F. Evidence that Spt4, Spt5, and Spt6 control transcription elongation by RNA polymerase II in Saccharomyces cerevisiae. Genes Dev. 1998 Feb 1;12(3):357-69. PMID:9450930
  4. ↑ Kaplan CD, Laprade L, Winston F. Transcription elongation factors repress transcription initiation from cryptic sites. Science. 2003 Aug 22;301(5636):1096-9. PMID:12934008 doi:http://dx.doi.org/10.1126/science.1087374
  5. ↑ Kaplan CD, Holland MJ, Winston F. Interaction between transcription elongation factors and mRNA 3'-end formation at the Saccharomyces cerevisiae GAL10-GAL7 locus. J Biol Chem. 2005 Jan 14;280(2):913-22. Epub 2004 Nov 5. PMID:15531585 doi:http://dx.doi.org/10.1074/jbc.M411108200
  6. ↑ Adkins MW, Tyler JK. Transcriptional activators are dispensable for transcription in the absence of Spt6-mediated chromatin reassembly of promoter regions. Mol Cell. 2006 Feb 3;21(3):405-16. PMID:16455495 doi:http://dx.doi.org/S1097-2765(05)01852-6
  7. ↑ McDonald SM, Close D, Xin H, Formosa T, Hill CP. Structure and biological importance of the Spn1-Spt6 interaction, and its regulatory role in nucleosome binding. Mol Cell. 2010 Dec 10;40(5):725-35. Epub 2010 Nov 25. PMID:21094070 doi:10.1016/j.molcel.2010.11.014

3oak, resolution 2.15Å

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