5VSO

NMR structure of Ydj1 J-domain, a cytosolic Hsp40 from Saccharomyces cerevisiae

5VSO の概要

• エントリーDOI: 10.2210/pdb5vso/pdb
• NMR情報: BMRB: 30293
• 分子名称: Yeast dnaJ protein 1 (1 entity in total)
• 機能のキーワード: j-domain, j-protein, dnaj, chaperone
• 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: 8521.57

構造登録者

Ciesielski, S.J.,Tonelli, M.,Lee, W.,Cornilescu, G.,Markley, J.L.,Schilke, B.A.,Ziegelhoffer, T.,Craig, E.A. (登録日: 2017-05-12, 公開日: 2017-11-01, 最終更新日: 2024-05-15)

主引用文献

Schilke, B.A.,Ciesielski, S.J.,Ziegelhoffer, T.,Kamiya, E.,Tonelli, M.,Lee, W.,Cornilescu, G.,Hines, J.K.,Markley, J.L.,Craig, E.A.
Broadening the functionality of a J-protein/Hsp70 molecular chaperone system.
PLoS Genet., 13:e1007084-e1007084, 2017

PubMed Abstract: By binding to a multitude of polypeptide substrates, Hsp70-based molecular chaperone systems perform a range of cellular functions. All J-protein co-chaperones play the essential role, via action of their J-domains, of stimulating the ATPase activity of Hsp70, thereby stabilizing its interaction with substrate. In addition, J-proteins drive the functional diversity of Hsp70 chaperone systems through action of regions outside their J-domains. Targeting to specific locations within a cellular compartment and binding of specific substrates for delivery to Hsp70 have been identified as modes of J-protein specialization. To better understand J-protein specialization, we concentrated on Saccharomyces cerevisiae SIS1, which encodes an essential J-protein of the cytosol/nucleus. We selected suppressors that allowed cells lacking SIS1 to form colonies. Substitutions changing single residues in Ydj1, a J-protein, which, like Sis1, partners with Hsp70 Ssa1, were isolated. These gain-of-function substitutions were located at the end of the J-domain, suggesting that suppression was connected to interaction with its partner Hsp70, rather than substrate binding or subcellular localization. Reasoning that, if YDJ1 suppressors affect Ssa1 function, substitutions in Hsp70 itself might also be able to overcome the cellular requirement for Sis1, we carried out a selection for SSA1 suppressor mutations. Suppressing substitutions were isolated that altered sites in Ssa1 affecting the cycle of substrate interaction. Together, our results point to a third, additional means by which J-proteins can drive Hsp70's ability to function in a wide range of cellular processes-modulating the Hsp70-substrate interaction cycle.

PubMed: 29084221
DOI: 10.1371/journal.pgen.1007084

実験手法

SOLUTION NMR