Two-step mechanism of J-domain action in driving Hsp70 function.

Autor: Bartlomiej Tomiczek, Wojciech Delewski, Lukasz Nierzwicki, Milena Stolarska, Igor Grochowina, Brenda Schilke, Rafal Dutkiewicz, Marta A Uzarska, Szymon J Ciesielski, Jacek Czub, Elizabeth A Craig, Jaroslaw Marszalek

Publikováno v: PLoS Computational Biology, Vol 16, Iss 6, p e1007913 (2020)

J-domain proteins (JDPs), obligatory Hsp70 cochaperones, play critical roles in protein homeostasis. They promote key allosteric transitions that stabilize Hsp70 interaction with substrate polypeptides upon hydrolysis of its bound ATP. Although a rec

Externí odkaz: https://doaj.org/article/6137714d2eb446d5ac4f961e7b40983d

Iron Insertion at the Assembly Site of the ISCU Scaffold Protein Is a Conserved Process Initiating Fe–S Cluster Biosynthesis

Autor: Batoul Srour, Sylvain Gervason, Maren Hellen Hoock, Beata Monfort, Kristian Want, Djabir Larkem, Nadine Trabelsi, Gautier Landrot, Andrea Zitolo, Emiliano Fonda, Emilien Etienne, Guillaume Gerbaud, Christina Sophia Müller, Jonathan Oltmanns, Jesse B. Gordon, Vishal Yadav, Malgorzata Kleczewska, Marcin Jelen, Michel B. Toledano, Rafal Dutkiewicz, David P. Goldberg, Volker Schünemann, Bruno Guigliarelli, Bénédicte Burlat, Christina Sizun, Benoit D’Autréaux

Publikováno v: Journal of the American Chemical Society
Journal of the American Chemical Society, 2022, 144 (38), pp.17496-17515. ⟨10.1021/jacs.2c06338⟩

International audience; Iron−sulfur (Fe−S) clusters are prosthetic groups of proteins biosynthesized on scaffold proteins by highly conserved multi-protein machineries. Biosynthesis of Fe−S clusters into the ISCU scaffold protein is initiated b

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09f1e62412505c0e54f958b4c5b661c5
https://doi.org/10.1021/jacs.2c06338

Defining a novel domain that provides an essential contribution to site-specific interaction of Rep protein with DNA

Autor: Igor Konieczny, Urszula Walkow, Rafal Dutkiewicz, Jacek Czub, Miłosz Wieczór, María Moreno-del Álamo, Bartlomiej Tomiczek, Janusz M. Bujnicki, Igor Grochowina, Katarzyna Bury, Katarzyna Wegrzyn, Elzbieta Zabrocka, Rafael Giraldo, Urszula Uciechowska

Publikováno v: Nucleic Acids Research
Digital.CSIC. Repositorio Institucional del CSIC
instname

15 p.-6 fig.
An essential feature of replication initiation proteins is their ability to bind to DNA. In this work, we describe a new domain that contributes to a replication initiator sequence-specific interaction with DNA. Applying biochemical

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bd6bbab2070c07a0eec72feb2dcfe21c
https://pubmed.ncbi.nlm.nih.gov/33660784

CLPB (caseinolytic peptidase B homolog), the first mitochondrial protein refoldase associated with human disease

Autor: Saskia B. Wortmann, Dagmara Mróz, Katarzyna Bury, Rafal Dutkiewicz, Katarzyna Zawieracz, Tomasz Szablewski, Szymon Ziętkiewicz, Ron A. Wevers, Hubert Wyszkowski

Publikováno v: Biochimica et Biophysica Acta-General Subjects, 1864, 4
Biochimica et Biophysica Acta-General Subjects, 1864
Biochim. Biophys. Acta-Gen. Subj. 1864:129512 (2020)

Contains fulltext : 219662.pdf (Publisher’s version ) (Open Access)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::37500df57523d3f320082c2509268a0c
https://pubmed.ncbi.nlm.nih.gov/31917998

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

Autor: Mateusz Manicki, Brenda Schilke, Lukasz Nierzwicki, Jaroslaw Marszalek, Bartlomiej Tomiczek, Wojciech Delewski, Bogumiła Paterkiewicz, Rafal Dutkiewicz, Szymon J. Ciesielski, Elizabeth A. Craig, Jacek Czub

Publikováno v: Molecular Biology and Evolution. 33:643-656

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 int

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4ca4c396f7a60e558504b11e919bb59
https://doi.org/10.1093/molbev/msv254