Mechanisms of mitochondrial iron-sulfur protein biogenesis
R Lill, SA Freibert - Annual review of biochemistry, 2020 - annualreviews.org
Mitochondria are essential in most eukaryotes and are involved in numerous biological
functions including ATP production, cofactor biosyntheses, apoptosis, lipid synthesis, and …
functions including ATP production, cofactor biosyntheses, apoptosis, lipid synthesis, and …
J-domain protein chaperone circuits in proteostasis and disease
The J-domain proteins (JDP) form the largest protein family among cellular chaperones. In
cooperation with the Hsp70 chaperone system, these co-chaperones orchestrate a plethora …
cooperation with the Hsp70 chaperone system, these co-chaperones orchestrate a plethora …
Function, evolution, and structure of J-domain proteins
Hsp70 chaperone systems are very versatile machines present in nearly all living organisms
and in nearly all intracellular compartments. They function in many fundamental processes …
and in nearly all intracellular compartments. They function in many fundamental processes …
From the discovery to molecular understanding of cellular iron-sulfur protein biogenesis
R Lill - Biological chemistry, 2020 - degruyter.com
Protein cofactors often are the business ends of proteins, and are either synthesized inside
cells or are taken up from the nutrition. A cofactor that strictly needs to be synthesized by …
cells or are taken up from the nutrition. A cofactor that strictly needs to be synthesized by …
Mechanism of iron–sulfur cluster assembly: In the intimacy of iron and sulfur encounter
B Srour, S Gervason, B Monfort, B D'Autréaux - Inorganics, 2020 - mdpi.com
Iron–sulfur (Fe–S) clusters are protein cofactors of a multitude of enzymes performing
essential biological functions. Specialized multi-protein machineries present in all types of …
essential biological functions. Specialized multi-protein machineries present in all types of …
[HTML][HTML] Multivalent protein–protein interactions are pivotal regulators of eukaryotic Hsp70 complexes
OT Johnson, JE Gestwicki - Cell Stress and Chaperones, 2022 - Elsevier
Abstract Heat shock protein 70 (Hsp70) is a molecular chaperone and central regulator of
protein homeostasis (proteostasis). Paramount to this role is Hsp70's binding to client …
protein homeostasis (proteostasis). Paramount to this role is Hsp70's binding to client …
Interaction of client—the scaffold on which FeS clusters are build—with J-domain protein Hsc20 and its evolving Hsp70 partners
J Marszalek, EA Craig - Frontiers in Molecular Biosciences, 2022 - frontiersin.org
In cells molecular chaperone systems consisting of Hsp70 and its obligatory J-domain
protein (JDP) co-chaperones transiently interact with a myriad of client proteins—with JDPs …
protein (JDP) co-chaperones transiently interact with a myriad of client proteins—with JDPs …
Chaperone function in Fe–S protein biogenesis: Three possible scenarios.
Among the six known iron‑sulfur (Fesingle bondS) cluster biogenesis machineries that
function across all domains of life only one involves a molecular chaperone system. This …
function across all domains of life only one involves a molecular chaperone system. This …
Molecular chaperones involved in mitochondrial iron–sulfur protein biogenesis
R Dutkiewicz, M Nowak - JBIC Journal of Biological Inorganic Chemistry, 2018 - Springer
Iron–sulfur (FeS) clusters are prosthetic groups critical for the function of many proteins in all
domains of life. FeS proteins function in processes ranging from oxidative phosphorylation …
domains of life. FeS proteins function in processes ranging from oxidative phosphorylation …
Two-step mechanism of J-domain action in driving Hsp70 function
B Tomiczek, W Delewski, L Nierzwicki… - PLoS computational …, 2020 - journals.plos.org
J-domain proteins (JDPs), obligatory Hsp70 cochaperones, play critical roles in protein
homeostasis. They promote key allosteric transitions that stabilize Hsp70 interaction with …
homeostasis. They promote key allosteric transitions that stabilize Hsp70 interaction with …