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PMID: 19000817 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Core structure of the yeast spt4-spt5 complex: a conserved module for regulation of transcription elongation.

Structure (London, England : 1993) ·Vol. 16 ·No. 11 ·2008-11-12 ·Pages 1649-58

Guo M, Xu F, Yamada J, Egelhofer T, Gao Y, Hartzog GA, Teng M, Niu L

Abstract

The Spt4-Spt5 complex is an essential RNA polymerase II elongation factor found in all eukaryotes and important for gene regulation. We report here the crystal structure of Saccharomyces cerevisiae Spt4 bound to the NGN domain of Spt5. This structure reveals that Spt4-Spt5 binding is governed by an acid-dipole interaction between Spt5 and Spt4. Mutations that disrupt this interaction disrupt the complex. Residues forming this pivotal interaction are conserved in the archaeal homologs of Spt4 and Spt5, which we show also form a complex. Even though bacteria lack a Spt4 homolog, the NGN domains of Spt5 and its bacterial homologs are structurally similar. Spt4 is located at a position that may help to maintain the functional conformation of the following KOW domains in Spt5. This structural and evolutionary perspective of the Spt4-Spt5 complex and its homologs suggest that it is an ancient, core component of the transcription elongation machinery.

MeSH Terms
Amino Acid Sequence Archaea/genetics Archaeal Proteins/chemistry,genetics Chromosomal Proteins, Non-Histone/chemistry,genetics Conserved Sequence Crystallography, X-Ray Models, Molecular Molecular Sequence Data Nuclear Proteins/chemistry,genetics Protein Binding Protein Conformation Saccharomyces cerevisiae/genetics Saccharomyces cerevisiae Proteins/chemistry,genetics Sequence Alignment Transcription, Genetic Transcriptional Elongation Factors/chemistry,genetics
Chemicals
Archaeal Proteins Chromosomal Proteins, Non-Histone Nuclear Proteins SPT4 protein, S cerevisiae Saccharomyces cerevisiae Proteins Transcriptional Elongation Factors SPT5 transcriptional elongation factor
Authors & Affiliations
8 authors, click to expand affiliations / ORCID
Guo Min
Hefei National Laboratory for Physical Sciences at Microscale and Key Laboratory of Structural Biology, School of Life Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230027, China.
Xu Fei
Yamada Jena
Egelhofer Thea
Gao Yongxiang
Hartzog Grant A
Teng Maikun
Niu Liwen
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Article Info
Journal
Structure (London, England : 1993)
Abbr.
Structure
ISSN
0969-2126
DOI
10.1016/j.str.2008.08.013
Published
2008-11-12
Pages
1649-58
Language
English
Region
United States
NLM ID
101087697
PMCID
PMC2743916
Subset
IM
Grants
NIGMS NIH HHS · R01 GM060479 · United States
NIGMS NIH HHS · R01 GM060479-09 · United States
NIGMS NIH HHS · GM060479 · United States
Databases
PDB
2EXU
External Links
PubMed source DOI: 10.1016/j.str.2008.08.013 PMC Full Text View journal details
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