scholarly journals ATPase Activity and Molecular Chaperone Function of the Stress70 Proteins

1996 ◽  
Vol 110 (2) ◽  
pp. 419-424 ◽  
Author(s):  
J. A. Miernyk ◽  
G. T. Hayman
Keyword(s):  
Atpase Activity ◽  
Molecular Chaperone ◽  
Chaperone Function

scholarly journals Inhibition of Simian Virus 40 replication by targeting the molecular chaperone function and ATPase activity of T antigen

2009 ◽  
Vol 141 (1) ◽  
pp. 71-80 ◽  
Author(s):  
Christine M. Wright ◽  
Sandlin P. Seguin ◽  
Sheara W. Fewell ◽  
Haijiang Zhang ◽  
Chandra Ishwad ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Molecular Chaperone ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
T Antigen ◽  
Chaperone Function

Molecular function of the prolyl cis/trans isomerase and metallochaperone SlyD

2013 ◽  
Vol 394 (8) ◽  
pp. 965-975 ◽  
Author(s):  
Michael Kovermann ◽  
Franz X. Schmid ◽  
Jochen Balbach
Keyword(s):  
Molecular Chaperone ◽  
Molecular Basis ◽  
Catalytic Efficiency ◽  
Enzyme Mechanism ◽  
Molecular Function ◽  
Twin Arginine Translocation ◽  
Chaperone Function ◽  
Nickel Binding ◽  
Biophysical Analysis ◽  
Optimal Function

Abstract SlyD is a bacterial two-domain protein that functions as a molecular chaperone, a prolyl cis/trans isomerase, and a nickel-binding protein. This review summarizes recent findings about the molecular enzyme mechanism of SlyD. The chaperone function located in one domain of SlyD is involved in twin-arginine translocation and increases the catalytic efficiency of the prolyl cis/trans isomerase domain in protein folding by two orders of magnitude. The C-terminal tail of SlyD binds Ni2+ ions and supplies them for the maturation of [NiFe] hydrogenases. A combined biochemical and biophysical analysis revealed the molecular basis of the delicate interplay of the different domains of SlyD for optimal function.

scholarly journals Specific Molecular Chaperone Interactions and an ATP-dependent Conformational Change Are Required during Posttranslational Protein Translocation into the Yeast ER

1998 ◽  
Vol 9 (12) ◽  
pp. 3533-3545 ◽  
Author(s):  
Amie J. McClellan ◽  
James B. Endres ◽  
Joseph P. Vogel ◽  
Debra Palazzi ◽  
Mark D. Rose ◽  
...  
Keyword(s):  
Atpase Activity ◽  
Conformational Change ◽  
Molecular Chaperone ◽  
Atp Hydrolysis ◽  
Protein Translocation ◽  
Wild Type ◽  
J Domain ◽  
Chaperone Interactions ◽  
Dependent Interaction ◽  
Er Membrane

The posttranslational translocation of proteins across the endoplasmic reticulum (ER) membrane in yeast requires ATP hydrolysis and the action of hsc70s (DnaK homologues) and DnaJ homologues in both the cytosol and ER lumen. Although the cytosolic hsc70 (Ssa1p) and the ER lumenal hsc70 (BiP) are homologous, they cannot substitute for one another, possibly because they interact with specific DnaJ homologues on each side of the ER membrane. To investigate this possibility, we purified Ssa1p, BiP, Ydj1p (a cytosolic DnaJ homologue), and a GST–63Jp fusion protein containing the lumenal DnaJ region of Sec63p. We observed that BiP, but not Ssa1p, is able to associate with GST–63Jp and that Ydj1p stimulates the ATPase activity of Ssa1p up to 10-fold but increases the ATPase activity of BiP by <2-fold. In addition, Ydj1p and ATP trigger the release of an unfolded polypeptide from Ssa1p but not from BiP. To understand further how BiP drives protein translocation, we purified four dominant lethal mutants of BiP. We discovered that each mutant is defective for ATP hydrolysis, fails to undergo an ATP-dependent conformational change, and cannot interact with GST–63Jp. Measurements of protein translocation into reconstituted proteoliposomes indicate that the mutants inhibit translocation even in the presence of wild-type BiP. We conclude that a conformation- and ATP-dependent interaction of BiP with the J domain of Sec63p is essential for protein translocation and that the specificity of hsc70 action is dictated by their DnaJ partners.

scholarly journals Thermotolerance and molecular chaperone function of an SGT1-like protein from the psychrophilic yeast, Glaciozyma antarctica

2016 ◽  
Vol 21 (4) ◽  
pp. 707-715 ◽  
Author(s):  
Nur Athirah Yusof ◽  
Noor Haza Fazlin Hashim ◽  
Travis Beddoe ◽  
Nor Muhammad Mahadi ◽  
Rosli Md Illias ◽  
...  
Keyword(s):  
Molecular Chaperone ◽  
Chaperone Function ◽  
Psychrophilic Yeast

scholarly journals Tamoxifen Enhances the Hsp90 Molecular Chaperone ATPase Activity

PLoS ONE ◽  
2010 ◽  
Vol 5 (4) ◽  
pp. e9934 ◽  
Author(s):  
Rongmin Zhao ◽  
Elisa Leung ◽  
Stefan Grüner ◽  
Matthieu Schapira ◽  
Walid A. Houry
Keyword(s):  
Atpase Activity ◽  
Molecular Chaperone

Goniothalamin enhances the ATPase activity of the molecular chaperone Hsp90 but inhibits its chaperone activity

2014 ◽  
Vol 157 (3) ◽  
pp. 161-168 ◽  
Author(s):  
Y. Yokoyama ◽  
A. Ohtaki ◽  
I. Jantan ◽  
M. Yohda ◽  
H. Nakamoto
Keyword(s):  
Atpase Activity ◽  
Molecular Chaperone ◽  
Chaperone Activity
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