4YTK

Structure of the KOW1-Linker1 domain of Transcription Elongation Factor Spt5

4YTK の概要

• エントリーDOI: 10.2210/pdb4ytk/pdb
• 分子名称: Transcription elongation factor SPT5 (2 entities in total)
• 機能のキーワード: transcription, elongation, rna processing, protein-dna interaction.
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15423.50

構造登録者

Meyer, P.A.,Li, S.,Zhang, M.,Yamada, K.,Takagi, Y.,Hartzog, G.A.,Fu, J. (登録日: 2015-03-17, 公開日: 2015-08-12, 最終更新日: 2026-03-04)

主引用文献

Meyer, P.A.,Li, S.,Zhang, M.,Yamada, K.,Takagi, Y.,Hartzog, G.A.,Fu, J.
Structures and Functions of the Multiple KOW Domains of Transcription Elongation Factor Spt5.
Mol.Cell.Biol., 35:3354-3369, 2015

PubMed Abstract: 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. A mechanistic understanding of the diverse functions of Spt4-Spt5 is hampered by challenges in resolving the distribution of functions among 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 [K1L1] and KOW2-KOW3) of Saccharomyces cerevisiae Spt5. The structure reveals that 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 have shown that the PCP has a function that partially overlaps that of Spt4. 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 confer robustness on processes associated with transcription elongation.

PubMed: 26217010
DOI: 10.1128/MCB.00520-15

実験手法

X-RAY DIFFRACTION (1.0904 Å)