Molecular chaperones in cellular protein folding

BioEssays ◽  
1994 ◽  
Vol 16 (9) ◽  
pp. 689-692 ◽  
Author(s):  
J�rg Martin ◽  
F.-Ulrich Hartl
Keyword(s):  
Protein Folding ◽  
Molecular Chaperones ◽  
Cellular Protein

Principles of chaperone-mediated protein folding

1995 ◽  
Vol 348 (1323) ◽  
pp. 107-112 ◽  
Keyword(s):  
Protein Folding ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Cellular Protein ◽  
Chaperone Proteins ◽  
Shock Proteins ◽  
Polypeptide Chains

The recent discovery of molecular chaperones and their functions has changed dramatically our view of the processes underlying the folding of proteins in vivo . Rather than folding spontaneously, most newly synthesized polypeptide chains seem to acquire their native conformations in a reaction mediated by chaperone proteins. Different classes of molecular chaperones, such as the members of the Hsp70 and Hsp60 families of heat-shock proteins, cooperate in a coordinated pathway of cellular protein folding.

scholarly journals Teasing Apart the Role of the Ribosome and Molecular Chaperones in Cellular Protein Folding

2018 ◽  
Vol 114 (3) ◽  
pp. 414a
Author(s):  
Rayna M. Addabbo ◽  
Matthew D. Dalphin ◽  
Yue Liu ◽  
Miranda F. Mecha ◽  
Silvia Cavagnero
Keyword(s):  
Protein Folding ◽  
Molecular Chaperones ◽  
Cellular Protein

Molecular chaperones in cellular protein folding

Nature ◽  
1996 ◽  
Vol 381 (6583) ◽  
pp. 571-580 ◽  
Author(s):  
F. Ulrich Hartl
Keyword(s):  
Protein Folding ◽  
Molecular Chaperones ◽  
Cellular Protein

Insights into chaperonin function from studies on archaeal thermosomes

2011 ◽  
Vol 39 (1) ◽  
pp. 94-98 ◽  
Author(s):  
Peter Lund
Keyword(s):  
Cell Death ◽  
Protein Folding ◽  
Recent Work ◽  
Mechanism Of Action ◽  
Molecular Chaperones ◽  
Short Review ◽  
Living Cells ◽  
Living Organisms ◽  
Opening And Closing ◽  
Hydrolysis Of

It is now well understood that, although proteins fold spontaneously (in a thermodynamic sense), many nevertheless require the assistance of helpers called molecular chaperones to reach their correct and active folded state in living cells. This is because the pathways of protein folding are full of traps for the unwary: the forces that drive proteins into their folded states can also drive them into insoluble aggregates, and, particularly when cells are stressed, this can lead, without prevention or correction, to cell death. The chaperonins are a family of molecular chaperones, practically ubiquitous in all living organisms, which possess a remarkable structure and mechanism of action. They act as nanoboxes in which proteins can fold, isolated from their environment and from other partners with which they might, with potentially deleterious consequences, interact. The opening and closing of these boxes is timed by the binding and hydrolysis of ATP. The chaperonins which are found in bacteria are extremely well characterized, and, although those found in archaea (also known as thermosomes) and eukaryotes have received less attention, our understanding of these proteins is constantly improving. This short review will summarize what we know about chaperonin function in the cell from studies on the archaeal chaperonins, and show how recent work is improving our understanding of this essential class of molecular chaperones.

Sign in / Sign up

Export Citation Format

Share Document