Folding while bound to chaperones

Scott Horowitz; Philipp Koldewey; Frederick Stull; James Ca Bardwell

doi:10.1016/j.sbi.2017.06.009

Folding while bound to chaperones

Curr Opin Struct Biol. 2018 Feb:48:1-5. doi: 10.1016/j.sbi.2017.06.009. Epub 2017 Jul 19.

Authors

Scott Horowitz¹, Philipp Koldewey², Frederick Stull³, James Ca Bardwell⁴

Affiliations

¹ Department of Chemistry & Biochemistry and the Knoebel Institute for Healthy Aging, University of Denver, 2155 E. Wesley Avenue, Denver, CO 80208, USA. Electronic address: [email protected].
² Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N. University, Ann Arbor, MI 48109, USA.
³ Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N. University, Ann Arbor, MI 48109, USA; Howard Hughes Medical Institute, University of Michigan, 830 N. University, Ann Arbor, MI 48109, USA.
⁴ Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 N. University, Ann Arbor, MI 48109, USA; Howard Hughes Medical Institute, University of Michigan, 830 N. University, Ann Arbor, MI 48109, USA. Electronic address: [email protected].

Abstract

Chaperones are important in preventing protein aggregation and aiding protein folding. How chaperones aid protein folding remains a key question in understanding their mechanism. The possibility of proteins folding while bound to chaperones was reintroduced recently with the chaperone Spy, many years after the phenomenon was first reported with the chaperones GroEL and SecB. In this review, we discuss the salient features of folding while bound in the cases for which it has been observed and speculate about its biological importance and possible occurrence in other chaperones.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review

MeSH terms

Adenosine Triphosphate / chemistry*
Adenosine Triphosphate / metabolism
Bacterial Proteins / chemistry*
Bacterial Proteins / genetics
Bacterial Proteins / metabolism
Carrier Proteins / chemistry
Carrier Proteins / genetics
Carrier Proteins / metabolism
Chaperonin 10 / chemistry
Chaperonin 10 / genetics
Chaperonin 10 / metabolism
Chaperonin 60 / chemistry
Chaperonin 60 / genetics
Chaperonin 60 / metabolism
Escherichia coli / genetics
Escherichia coli / metabolism*
Escherichia coli Proteins / chemistry*
Escherichia coli Proteins / genetics
Escherichia coli Proteins / metabolism
Gene Expression
Kinetics
Models, Molecular
Molecular Chaperones / chemistry*
Molecular Chaperones / genetics
Molecular Chaperones / metabolism
Periplasmic Proteins / chemistry*
Periplasmic Proteins / genetics
Periplasmic Proteins / metabolism
Protein Binding
Protein Conformation
Protein Folding
Ribonucleases / chemistry
Ribonucleases / genetics
Ribonucleases / metabolism
Thermodynamics

Substances

Bacterial Proteins
Carrier Proteins
Chaperonin 10
Chaperonin 60
E colicin-binding immunity protein Im7, E coli
Escherichia coli Proteins
Molecular Chaperones
Periplasmic Proteins
SecB protein, Bacteria
Spy protein, E coli
Adenosine Triphosphate
Ribonucleases
Bacillus amyloliquefaciens ribonuclease

Abstract

Publication types

MeSH terms

Substances

Grants and funding