scholarly journals The Hsp70 Chaperone Ssq1p Is Dispensable for Iron-Sulfur Cluster Formation on the Scaffold Protein Isu1p

2006 ◽  
Vol 281 (12) ◽  
pp. 7801-7808 ◽  
Author(s):  
Rafal Dutkiewicz ◽  
Jaroslaw Marszalek ◽  
Brenda Schilke ◽  
Elizabeth A. Craig ◽  
Roland Lill ◽  
...  
Keyword(s):  
Cluster Formation ◽  
Scaffold Protein ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Hsp70 Chaperone

Regulation of Iron-Sulfur Cluster Formation in Plastids

2012 ◽  
pp. 135-144
Author(s):  
Karl Ravet ◽  
Douglas Van Hoewyk ◽  
Marinus Pilon
Keyword(s):  
Cluster Formation ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur

scholarly journals Biochemical Convergence of Mitochondrial Hsp70 System Specialized in Iron–Sulfur Cluster Biogenesis

2020 ◽  
Vol 21 (9) ◽  
pp. 3326 ◽  
Author(s):  
Malgorzata Kleczewska ◽  
Aneta Grabinska ◽  
Marcin Jelen ◽  
Milena Stolarska ◽  
Brenda Schilke ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Biochemical Properties ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur ◽  
Hsp70 Chaperone ◽  
J Domain ◽  
Domain Protein ◽  
Mitochondrial Hsp70 ◽  
Practical Implications

Mitochondria play a central role in the biogenesis of iron–sulfur cluster(s) (FeS), protein cofactors needed for many cellular activities. After assembly on scaffold protein Isu, the cluster is transferred onto a recipient apo-protein. Transfer requires Isu interaction with an Hsp70 chaperone system that includes a dedicated J-domain protein co-chaperone (Hsc20). Hsc20 stimulates Hsp70′s ATPase activity, thus stabilizing the critical Isu–Hsp70 interaction. While most eukaryotes utilize a multifunctional mitochondrial (mt)Hsp70, yeast employ another Hsp70 (Ssq1), a product of mtHsp70 gene duplication. Ssq1 became specialized in FeS biogenesis, recapitulating the process in bacteria, where specialized Hsp70 HscA cooperates exclusively with an ortholog of Hsc20. While it is well established that Ssq1 and HscA converged functionally for FeS transfer, whether these two Hsp70s possess similar biochemical properties was not known. Here, we show that overall HscA and Ssq1 biochemical properties are very similar, despite subtle differences being apparent - the ATPase activity of HscA is stimulated to a somewhat higher levels by Isu and Hsc20, while Ssq1 has a higher affinity for Isu and for Hsc20. HscA/Ssq1 are a unique example of biochemical convergence of distantly related Hsp70s, with practical implications, crossover experimental results can be combined, facilitating understanding of the FeS transfer process.

scholarly journals Anatomy of an iron-sulfur cluster scaffold protein: Understanding the determinants of [2Fe–2S] cluster stability on IscU

2015 ◽  
Vol 1853 (6) ◽  
pp. 1448-1456 ◽  
Author(s):  
Miquel Adrover ◽  
Barry D. Howes ◽  
Clara Iannuzzi ◽  
Giulietta Smulevich ◽  
Annalisa Pastore
Keyword(s):  
Scaffold Protein ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Cluster Stability ◽  
Iron Sulfur

scholarly journals The Role of CyaY in Iron Sulfur Cluster Assembly on the E. coli IscU Scaffold Protein

PLoS ONE ◽  
2011 ◽  
Vol 6 (7) ◽  
pp. e21992 ◽  
Author(s):  
Clara Iannuzzi ◽  
Salvatore Adinolfi ◽  
Barry D. Howes ◽  
Ricardo Garcia-Serres ◽  
Martin Clémancey ◽  
...  
Keyword(s):  
Scaffold Protein ◽  
Cluster Assembly ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
E Coli ◽  
Iron Sulfur

Methylene insertion into an Fe2S2 cluster: formation of a thiolate-bridged diiron complex containing an Fe–CH2–S moiety

2018 ◽  
Vol 54 (93) ◽  
pp. 13119-13122 ◽  
Author(s):  
Linan Su ◽  
Dawei Yang ◽  
Yixin Zhang ◽  
Baomin Wang ◽  
Jingping Qu
Keyword(s):  
Cluster Formation ◽  
Iron Sulfur Cluster ◽  
Sulfur Cluster ◽  
Iron Sulfur

Cleavage of both C−Cl bonds in CH2Cl2 by a reduced iron–sulfur cluster induced unexpected methylene insertion into the Fe–S bond.

Sign in / Sign up

Export Citation Format

Share Document