AAA+ proteins: have engine, will work

@article{Hanson2005AAAPH,
  title={AAA+ proteins: have engine, will work},
  author={Phyllis I Hanson and Sidney W. Whiteheart},
  journal={Nature Reviews Molecular Cell Biology},
  year={2005},
  volume={6},
  pages={519-529}
}
The AAA+ (ATPases associated with various cellular activities) family is a large and functionally diverse group of enzymes that are able to induce conformational changes in a wide range of substrate proteins. The family's defining feature is a structurally conserved ATPase domain that assembles into oligomeric rings and undergoes conformational changes during cycles of nucleotide binding and hydrolysis. Here, we review the structural organization of AAA+ proteins, the conformational changes… 
View on Nature
ncbi.nlm.nih.gov
1,099 Citations
Highly Influential Citations
84
Background Citations
480
Methods Citations
21
Results Citations
7

1,099 Citations

Citation Type

Citation Type

Fundamental Characteristics of AAA+ Protein Family Structure and Function
TLDR
The major features of AAA+ protein structure and function are discussed with an emphasis on pivotal aspects elucidated with archaeal proteins.
Evolutionary relationships and structural mechanisms of AAA+ proteins.
TLDR
The critical features of theAAA+ domain are described, current knowledge of how this versatile element is incorporated into larger assemblies is summarized, and specific adaptations of the AAA+ fold are discussed that allow complex molecular manipulations to be carried out for a highly diverse set of macromolecular targets.
AAA+ ATPases: Achieving Diversity of Function with Conserved Machinery
TLDR
The features and motifs that partially define AAA+ domains are reviewed, the cellular activities mediated by selected AAA+ proteins are described and the recent work is discussed, suggesting that various AAA+ machines with very different activities employ a common core mechanism.
Using chemical inhibitors to probe AAA protein conformational dynamics and cellular functions.
Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes.
Marching to the beat of the ring: polypeptide translocation by AAA+ proteases.
From the common molecular basis of the AAA protein to various energy-dependent and -independent activities of AAA proteins.
TLDR
Functional analysis indicates that this conserved residue in AAA proteases is involved in threading unfolded polypeptides, and it has been found that some chimaeras are able to degrade casein in an ATP-independent manner.
Coupling AAA protein function to regulated gene expression.
Biochemical studies of the essential Clp protease in cyanobacteria and its associated adaptor proteins
TLDR
This thesis work has examined the structure and function of the mixed proteolytic core within the essential ClpCP3/R protease and its associated adapter proteins ClpS1 and ClpPS2 in the cyanobacterium Synechococcus elongatus.
AAA+ ATPases in Protein Degradation: Structures, Functions and Mechanisms
TLDR
These studies reveal three highly conserved patterns in the structure–function relationship of AAA+ ATPase hexamers that were observed in the human 26S proteasome, thus suggesting common dynamic models of mechanochemical coupling during force generation and substrate translocation.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 121 REFERENCES
AAA+ superfamily ATPases: common structure–diverse function
  • T. Ogura, A. Wilkinson
  • Biology, Chemistry
    Genes to cells : devoted to molecular & cellular mechanisms
  • 2001
TLDR
The AAA+ proteins represent a novel type of molecular chaperone and are versatile in their mode of action, which collectively seem to involve some form of disruption of molecular or macromolecular structure.
Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases.
Conformational changes of the multifunction p97 AAA ATPase during its ATPase cycle
TLDR
Three-dimensional maps show that the two AAA domains, D1 and D2, as well as the N-domains, experience conformational changes during ATP binding, ATP hydrolysis, Pi release and ADP release, and the movements that this and possibly other AAA ATPases can undergo during an ATPase cycle.
AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes.
TLDR
Whole-genome analysis indicates that this class of proteins is ancient and has undergone considerable functional divergence prior to the emergence of the major divisions of life.
Sculpting the Proteome with AAA+ Proteases and Disassembly Machines
Aaa Proteins
  • R. Vale
  • Biology, Chemistry
    The Journal of cell biology
  • 2000
AAA ATPases (those associated with various cellular activities) play important roles in numerous cellular activities including proteolysis, protein folding, membrane trafficking, cytoskeletal…
A link between sequence conservation and domain motion within the AAA+ family.
Chaperone-like activity of the AAA domain of the yeast Yme1 AAA protease
TLDR
It is shown that Yme1 senses the folding state of solvent-exposed domains and specifically degrades unfolded membrane proteins and suggests that the AAA domains of other AAA proteins may have a similar function.
AAA proteases of mitochondria: quality control of membrane proteins and regulatory functions during mitochondrial biogenesis.
TLDR
An ubiquitous and conserved proteolytic system regulates the stability of mitochondrial inner membrane proteins and exerts crucial functions during the biogenesis of mitochondria.
Nucleotide-dependent domain motions within rings of the RecA/AAA(+) superfamily.
  • Jimin Wang
  • Biology
    Journal of structural biology
  • 2004
...
1
2
3
4
5
...