3UO2

Jac1 co-chaperone from Saccharomyces cerevisiae

3UO2 の概要

• エントリーDOI: 10.2210/pdb3uo2/pdb
• 分子名称: J-type co-chaperone JAC1, mitochondrial (2 entities in total)
• 機能のキーワード: structural genomics, psi-biology, midwest center for structural genomics, mcsg, co-chaperone, j-protein, iron sulfur cluster biogenesis, ssq1 hsp70 chaperone, isu proteins, chaperone
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Mitochondrion matrix : P53193
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41234.59

構造登録者

Osipiuk, J.,Mulligan, R.,Bigelow, L.,Marszalek, J.,Craig, E.A.,Dutkiewicz, R.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2011-11-16, 公開日: 2011-12-14, 最終更新日: 2023-09-13)

主引用文献

Ciesielski, S.J.,Schilke, B.A.,Osipiuk, J.,Bigelow, L.,Mulligan, R.,Majewska, J.,Joachimiak, A.,Marszalek, J.,Craig, E.A.,Dutkiewicz, R.
Interaction of j-protein co-chaperone jac1 with fe-s scaffold isu is indispensable in vivo and conserved in evolution.
J.Mol.Biol., 417:1-12, 2012

PubMed Abstract: The ubiquitous mitochondrial J-protein Jac1, called HscB in Escherichia coli, and its partner Hsp70 play a critical role in the transfer of Fe-S clusters from the scaffold protein Isu to recipient proteins. Biochemical results from eukaryotic and prokaryotic systems indicate that formation of the Jac1-Isu complex is important for both targeting of the Isu for Hsp70 binding and stimulation of Hsp70's ATPase activity. However, in apparent contradiction, we previously reported that an 8-fold decrease in Jac1's affinity for Isu1 is well tolerated in vivo, raising the question as to whether the Jac1:Isu interaction actually plays an important biological role. Here, we report the determination of the structure of Jac1 from Saccharomyces cerevisiae. Taking advantage of this information and recently published data from the homologous bacterial system, we determined that a total of eight surface-exposed residues play a role in Isu binding, as assessed by a set of biochemical assays. A variant having alanines substituted for these eight residues was unable to support growth of a jac1-Δ strain. However, replacement of three residues caused partial loss of function, resulting in a significant decrease in the Jac1:Isu1 interaction, a slow growth phenotype, and a reduction in the activity of Fe-S cluster-containing enzymes. Thus, we conclude that the Jac1:Isu1 interaction plays an indispensable role in the essential process of mitochondrial Fe-S cluster biogenesis.

PubMed: 22306468
DOI: 10.1016/j.jmb.2012.01.022

実験手法

X-RAY DIFFRACTION (2.13 Å)