The Role of AAA+ Proteins in Protein Repair and Degradation

226.8K

views

66

authors

22

articles

Editorial

02 October 2018

Editorial: The Role of AAA+ Proteins in Protein Repair and Degradation

James Shorter

and

Walid A. Houry

12,763 views

18 citations

Editors

2

University of Toronto

University of Pennsylvania

Impact

Fetching...

About

ATPases Associated with diverse cellular Activities (AAA+) is a superfamily of proteins that carry out a large variety of functions essential to cell physiology, including control of protein homeostasis, DNA replication, recombination, chromatin remodeling, ribosomal RNA processing, molecular targeting, organelle biogenesis, and membrane fusion. Members of this superfamily are defined by the presence of what is termed the AAA+ domain containing the canonical Walker A and B motifs required for ATP binding and hydrolysis. They typically form hexameric complexes and act as motors to remodel other proteins, DNA/RNA, or multicomponent complexes. Indeed, many chaperones and ATP-dependent proteases are or have subunits that belong to this superfamily.

There has been substantial progress in identifying the structure and mechanism of function of a large number of AAA+ proteins. In this series, a detailed structural and biochemical view is provided of several AAA+ chaperones and proteases, namely: ClpXP, ClpAPS, ClpB and Hsp104, FtsH, 19S proteasome, Lon, p97, Pex1/6, CbbQ, torsin, and NSF.

Contributors are encouraged to submit perspectives, reviews, and original research articles.

ATPases Associated with diverse cellular Activities (AAA+) is a superfamily of proteins that carry out a large variety of functions essential to cell physiology, including control of protein homeostasis, DNA replication, recombination, chromatin remodeling, ribosomal RNA processing, molecular targeting, organelle biogenesis, and membrane fusion. Members of this superfamily are defined by the presence of what is termed the AAA+ domain containing the canonical Walker A and B motifs required for ATP binding and hydrolysis. They typically form hexameric complexes and act as motors to remodel other proteins, DNA/RNA, or multicomponent complexes. Indeed, many chaperones and ATP-dependent proteases are or have subunits that belong to this superfamily.

There has been substantial progress in identifying the structure and mechanism of function of a large number of AAA+ proteins. In this series, a detailed structural and biochemical view is provided of several AAA+ chaperones and proteases, namely: ClpXP, ClpAPS, ClpB and Hsp104, FtsH, 19S proteasome, Lon, p97, Pex1/6, CbbQ, torsin, and NSF.

Contributors are encouraged to submit perspectives, reviews, and original research articles.

Download ebook

Share

Editors

University of Toronto

University of Pennsylvania

Impact

226,783 Total views

157,350 Article views

63,858 Article downloads

5,575 Topic views

Published In

Journal Thumbnail

Frontiers in Molecular Biosciences

Structural Biology, Protein Folding, Misfolding and Degradation

Journal Thumbnail

Frontiers in Cell and Developmental Biology

Structural Biology

About Frontiers Research Topics

With their unique mixes of varied contributions from Original Research to Review Articles, Research Topics unify the most influential researchers, the latest key findings and historical advances in a hot research area! Find out more on how to host your own Frontiers Research Topic or contribute to one as an author.

Suggest a topic