scholarly journals The C-terminal cysteine annulus participates in auto-chaperone function forSalmonellaphage P22 tailspike folding and assembly

Bacteriophage ◽  
2012 ◽  
Vol 2 (1) ◽  
pp. 36-49 ◽  
Author(s):  
Takumi Takata ◽  
Cameron Haase-Pettingell ◽  
Jonathan King
Keyword(s):  
Chaperone Function ◽  
P22 Tailspike

Chaperone Function in Androgen-Independent Prostate Cancer

2011 ◽  
Author(s):  
Bryce Paschal
Keyword(s):  
Prostate Cancer ◽  
Chaperone Function ◽  
Androgen Independent

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

scholarly journals Temperature-sensitive mutations and second-site suppressor substitutions affect folding of the P22 tailspike protein in vitro.

1993 ◽  
Vol 268 (27) ◽  
pp. 20071-20075
Author(s):  
A Mitraki ◽  
M Danner ◽  
J King ◽  
R Seckler
Keyword(s):  
Temperature Sensitive ◽  
P22 Tailspike ◽  
Tailspike Protein

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.

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