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''' | ==Structure of the KOW1-Linker1 domain of Transcription Elongation Factor Spt5== | ||
<StructureSection load='4ytk' size='340' side='right' caption='[[4ytk]], [[Resolution|resolution]] 1.09Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4ytk]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YTK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YTK FirstGlance]. <br> | |||
</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=4ytk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ytk OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ytk RCSB], [http://www.ebi.ac.uk/pdbsum/4ytk PDBsum]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/SPT5_YEAST SPT5_YEAST]] The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene.<ref>PMID:12554661</ref> <ref>PMID:12556496</ref> <ref>PMID:15780939</ref> <ref>PMID:16172632</ref> <ref>PMID:9450930</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The eukaryotic Spt4-Spt5 heterodimer forms a higher-order complex with RNA polymerase II (and I) to regulate transcription elongation. Extensive genetic and functional data have revealed diverse roles of Spt4-Spt5 in coupling elongation with chromatin modification and RNA processing pathways. Mechanistic understanding of the diverse functions of Spt4-Spt5 is hampered by challenges in resolving the distribution of functions amongst its structural domains including the five KOW domains in Spt5 and a lack of their high-resolution structures. We present high-resolution crystallographic results demonstrating that distinct structures are formed by the first through third KOW domains (KOW1-Linker1 and KOW2-KOW3) of yeast Spt5. The structure reveals that KOW1-Linker1 (K1L1) displays a positively charged patch (PCP) on its surface, which binds nucleic acids in vitro as shown in biochemical assays and is important for in vivo function as shown in growth assays. Furthermore, assays in yeast show that the PCP carries a function that partially overlaps that of Spt4. A synthesis of our results with previous evidence suggests a model in which Spt4 and the K1L1 domain of Spt5 form functionally overlapping interactions with nucleic acids upstream of the transcription bubble, and this mechanism may endow robustness to processes associated with transcription elongation. | |||
Structures and functions of the multiple KOW domains of transcription elongation factor Spt5.,Meyer PA, Li S, Zhang M, Yamada K, Takagi Y, Hartzog GA, Fu J Mol Cell Biol. 2015 Jul 27. pii: MCB.00520-15. PMID:26217010<ref>PMID:26217010</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
[[Category: | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Fu, J]] | |||
[[Category: Hartzog, G A]] | |||
[[Category: Li, S]] | [[Category: Li, S]] | ||
[[Category: Meyer, P A]] | |||
[[Category: Takagi, Y]] | |||
[[Category: Yamada, K]] | [[Category: Yamada, K]] | ||
[[Category: Zhang, M]] | [[Category: Zhang, M]] | ||
[[Category: | [[Category: Elongation]] | ||
[[Category: | [[Category: Protein-dna interaction]] | ||
[[Category: Rna processing]] | |||
[[Category: Transcription]] | |||
Revision as of 17:31, 12 August 2015
Structure of the KOW1-Linker1 domain of Transcription Elongation Factor Spt5Structure of the KOW1-Linker1 domain of Transcription Elongation Factor Spt5
Structural highlights
Function[SPT5_YEAST] The SPT4-SPT5 complex mediates both activation and inhibition of transcription elongation, and plays a role in pre-mRNA processing. This complex seems to be important for the stability of the RNA polymerase II elongation machinery on the chromatin template but not for the inherent ability of this machinery to translocate down the gene.[1] [2] [3] [4] [5] Publication Abstract from PubMedThe eukaryotic Spt4-Spt5 heterodimer forms a higher-order complex with RNA polymerase II (and I) to regulate transcription elongation. Extensive genetic and functional data have revealed diverse roles of Spt4-Spt5 in coupling elongation with chromatin modification and RNA processing pathways. Mechanistic understanding of the diverse functions of Spt4-Spt5 is hampered by challenges in resolving the distribution of functions amongst its structural domains including the five KOW domains in Spt5 and a lack of their high-resolution structures. We present high-resolution crystallographic results demonstrating that distinct structures are formed by the first through third KOW domains (KOW1-Linker1 and KOW2-KOW3) of yeast Spt5. The structure reveals that KOW1-Linker1 (K1L1) displays a positively charged patch (PCP) on its surface, which binds nucleic acids in vitro as shown in biochemical assays and is important for in vivo function as shown in growth assays. Furthermore, assays in yeast show that the PCP carries a function that partially overlaps that of Spt4. A synthesis of our results with previous evidence suggests a model in which Spt4 and the K1L1 domain of Spt5 form functionally overlapping interactions with nucleic acids upstream of the transcription bubble, and this mechanism may endow robustness to processes associated with transcription elongation. Structures and functions of the multiple KOW domains of transcription elongation factor Spt5.,Meyer PA, Li S, Zhang M, Yamada K, Takagi Y, Hartzog GA, Fu J Mol Cell Biol. 2015 Jul 27. pii: MCB.00520-15. PMID:26217010[6] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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