Wyniki wyszukiwania dla: SSQ1

• Iron–Sulfur Cluster Biogenesis Chaperones: Evidence for Emergence of Mutational Robustness of a Highly Specific Protein–Protein Interaction

  Publikacja

  • W. Delewski
  • B. Paterkiewicz
  • M. Manicki
  • B. Schilke
  • B. Tomiczek
  • S. Ciesielski
  • Ł. Nierzwicki
  • J. Czub
  • R. Dutkiewicz
  • E. Craig
  • J. Marszalek

  - MOLECULAR BIOLOGY AND EVOLUTION - Rok 2016

  Biogenesis of iron–sulfur clusters (FeS) is a highly conserved process involving Hsp70 and J-protein chaperones. However, Hsp70 specialization differs among species. In most eukaryotes, including Schizosaccharomyces pombe, FeS biogenesis involves interaction between the J-protein Jac1 and the multifunctional Hsp70 Ssc1. But, in Saccharomyces cerevisiae and closely related species, Jac1 interacts with the specialized Hsp70 Ssq1,...

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• Analysis of Reconstituted Tripartite Complex Supports Avidity-based Recruitment of Hsp70 by Substrate Bound J-domain Protein

  Publikacja

  • M. Jelen
  • I. Grochowina
  • A. Grabinska-Rogala
  • S. Ciesielski
  • K. Dabrowska
  • B. Tomiczek
  • Ł. Nierzwicki
  • W. Delewski
  • B. Schilke
  • J. Czub... i 4 innych

  - JOURNAL OF MOLECULAR BIOLOGY - Rok 2023

  Hsp70 are ubiquitous, versatile molecular chaperones that cyclically interact with substrate protein(s). The initial step requires synergistic interaction of a substrate and a J-domain protein (JDP) cochaperone, via its J-domain, with Hsp70 to stimulate hydrolysis of its bound ATP. This hydrolysis drives conformational changes in Hsp70 that stabilize substrate binding. However, because of the transient nature of substrate and JDP...

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