Bacterial RF3 Senses Chaperone Function in Co-Translational Folding

2020 ◽  
Author(s):  
Liang Zhao ◽  
Marie-Pierre Castanié-Cornet ◽  
Sneha Kumar ◽  
Pierre Genevaux ◽  
Manajit Hayer-Hartl ◽  
...  
Keyword(s):  
Chaperone Function

Bacterial RF3 senses chaperone function in co-translational folding

2021 ◽  
Author(s):  
Liang Zhao ◽  
Marie-Pierre Castanié-Cornet ◽  
Sneha Kumar ◽  
Pierre Genevaux ◽  
Manajit Hayer-Hartl ◽  
...  
Keyword(s):  
Chaperone Function

scholarly journals Chaperone Function of Hgh1 in the Biogenesis of Eukaryotic Elongation Factor 2

2019 ◽  
Vol 74 (1) ◽  
pp. 88-100.e9 ◽  
Author(s):  
Leonie Mönkemeyer ◽  
Courtney L. Klaips ◽  
David Balchin ◽  
Roman Körner ◽  
F. Ulrich Hartl ◽  
...  
Keyword(s):  
Elongation Factor ◽  
Chaperone Function ◽  
Elongation Factor 2 ◽  
Eukaryotic Elongation Factor 2 ◽  
Eukaryotic Elongation Factor

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.

Paradoxical Effects of Substitution and Deletion Mutation of Arg56 on the Structure and Chaperone Function of Human αB-Crystallin†

Biochemistry ◽  
2007 ◽  
Vol 46 (5) ◽  
pp. 1117-1127 ◽  
Author(s):  
Ashis Biswas ◽  
Jeffery Goshe ◽  
Antonia Miller ◽  
Puttur Santhoshkumar ◽  
Carol Luckey ◽  
...  
Keyword(s):  
Deletion Mutation ◽  
Chaperone Function ◽  
Paradoxical Effects ◽  
Αb Crystallin

scholarly journals A Chaperone Function of NO CATALASE ACTIVITY1 Is Required to Maintain Catalase Activity and for Multiple Stress Responses in Arabidopsis

2015 ◽  
Vol 27 (3) ◽  
pp. 908-925 ◽  
Author(s):  
Jing Li ◽  
Juntao Liu ◽  
Guoqiang Wang ◽  
Joon-Yung Cha ◽  
Guannan Li ◽  
...  
Keyword(s):  
Stress Responses ◽  
Catalase Activity ◽  
Multiple Stress ◽  
Chaperone Function
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