Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function

ME Cheetham, AJ Caplan - Cell stress & chaperones, 1998 - ncbi.nlm.nih.gov
It is a general feature of molecular chaperones that they are highly conserved throughout
evolution. Prokaryotic and eukaryotic Hsp70 proteins, for example, are over 50% identical at …

[HTML][HTML] Mechanisms for regulation of Hsp70 function by Hsp40

CY Fan, S Lee, DM Cyr - Cell stress & chaperones, 2003 - ncbi.nlm.nih.gov
The Hsp70 family members play an essential role in cellular protein metabolism by acting as
polypeptide-binding and release factors that interact with nonnative regions of proteins at …

The Cauliflower Or Gene Encodes a DnaJ Cysteine-Rich Domain-Containing Protein That Mediates High Levels of β-Carotene Accumulation

S Lu, J Van Eck, X Zhou, AB Lopez… - The Plant …, 2006 - academic.oup.com
Despite recent progress in our understanding of carotenogenesis in plants, the mechanisms
that govern overall carotenoid accumulation remain largely unknown. The Orange (Or) gene …

[HTML][HTML] The Hdj‐2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis

GC Meacham, Z Lu, S King, E Sorscher… - The EMBO …, 1999 - embopress.org
The cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride ion channel
constructed from two membrane‐spanning domains (MSDs), two nucleotide‐binding …

Mechanisms of the Hsp70 chaperone system

JC Young - Biochemistry and cell biology, 2010 - cdnsciencepub.com
Molecular chaperones of the Hsp70 family have diverse functions in cells. They assist the
folding of newly synthesized and stress-denatured proteins, as well as the import of proteins …

Role of the J-domain in the cooperation of Hsp40 with Hsp70

MK Greene, K Maskos… - Proceedings of the …, 1998 - National Acad Sciences
The Escherichia coli Hsp40 DnaJ and Hsp70 DnaK cooperate in the binding of proteins at
intermediate stages of folding, assembly, and translocation across membranes. Binding of …

[HTML][HTML] Its substrate specificity characterizes the DnaJ co‐chaperone as a scanning factor for the DnaK chaperone

S Rüdiger, J Schneider‐Mergener, B Bukau - The EMBO journal, 2001 - embopress.org
The evolutionarily conserved DnaJ proteins are essential components of Hsp70 chaperone
systems. The DnaJ homologue of Escherichia coli associates with chaperone substrates …

The Arabidopsis Chaperone J3 Regulates the Plasma Membrane H+-ATPase through Interaction with the PKS5 Kinase

Y Yang, Y Qin, C Xie, F Zhao, J Zhao, D Liu… - The Plant …, 2010 - academic.oup.com
The plasma membrane H+-ATPase (PM H+-ATPase) plays an important role in the
regulation of ion and metabolite transport and is involved in physiological processes that …

The action of molecular chaperones in the early secretory pathway

SW Fewell, KJ Travers, JS Weissman… - Annual review of …, 2001 - annualreviews.org
▪ Abstract The endoplasmic reticulum (ER) serves as a way-station during the biogenesis of
nearly all secreted proteins, and associated with or housed within the ER are factors …

Heavy metal ions are potent inhibitors of protein folding

SK Sharma, P Goloubinoff, P Christen - Biochemical and biophysical …, 2008 - Elsevier
Environmental and occupational exposure to heavy metals such as cadmium, mercury and
lead results in severe health hazards including prenatal and developmental defects. The …