AAA+ proteins: diversity in function, similarity in structure.

@article{Snider2008AAAPD,
  title={AAA+ proteins: diversity in function, similarity in structure.},
  author={Jamie D. Snider and Walid A. Houry},
  journal={Biochemical Society transactions},
  year={2008},
  volume={36 Pt 1},
  pages={
          72-7
        }
}
The AAA+ (ATPases associated with various cellular activities) superfamily of proteins represents a distinct lineage of the larger class of P-loop NTPases. Members of this superfamily use the power of nucleotide binding and hydrolysis to direct molecular remodelling events. All AAA+ proteins share a common core architecture, which, through various sequence and structural modifications, has been adapted for use in a remarkably diverse range of functions. The following mini-review provides a… 
View on PubMed
biochemsoctrans.org
147 Citations
Highly Influential Citations
8
Background Citations
62
Methods Citations
1

Figures from this paper

147 Citations

Citation Type

Citation Type

The AAA+ superfamily of functionally diverse proteins
SummaryThe AAA+ superfamily is a large and functionally diverse superfamily of NTPases that are characterized by a conserved nucleotide-binding and catalytic module, the AAA+ module. Members are…
AAA proteins and the life process.
TLDR
The talks that are discussed herein and the corresponding papers that follow this introduction give a good overview of the current areas of research into these proteins.
Hsp78 (78 kDa Heat Shock Protein), a Representative AAA Family Member Found in the Mitochondrial Matrix of Saccharomyces cerevisiae
TLDR
Hsp104 and its homolog Hsp78 (78 kDa heat shock protein) are representatives of the Clp family in yeast and the possible existence of other homologs in metazoans is discussed.
Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes.
Assessing heterogeneity in oligomeric AAA+ machines
  • T. Sysoeva
  • Biology, Chemistry
    Cellular and Molecular Life Sciences
  • 2016
TLDR
The first part of this work will provide a broad overview of what arrangements of AAA+ subunits have been structurally observed focusing on diversity of ATPase oligomericEnsembles and heterogeneity within the ensembles.
Deviation of the typical AAA substrate-threading pore prevents fatal protein degradation in yeast Cdc48
TLDR
It is shown that artificial retrieval of this aromatic residue in Cdc48 is lethal, and essential features to support the threading mechanism are required to exhibit the lethal phenotype, meaning that the widely applicable threading model is less effective for wild-type CDC48.
Proteasomal AAA-ATPases: structure and function.
Comparison of the multiple oligomeric structures observed for the Rvb1 and Rvb2 proteins.
The Rvb1 and Rvb2 proteins are 2 members of the AAA+ family, involved in roles as diverse as chromatin remodeling, transcription, small nucleolar RNA maturation, cellular transformation, signaling of…
Formation of MgF3−-dependent complexes between an AAA+ ATPase and σ54
The ATPase of the phi29 DNA packaging motor is a member of the hexameric AAA+ superfamily
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 42 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.
Classification of AAA+ proteins.
Evolutionary history and higher order classification of AAA+ ATPases.
Phylogenetic analysis of AAA proteins.
Conserved arginine residues implicated in ATP hydrolysis, nucleotide-sensing, and inter-subunit interactions in AAA and AAA+ ATPases.
Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions.
Classification and evolution of P-loop GTPases and related ATPases.
TLDR
The distribution of nucleotide specificity among the proteins of the G TPase superclass indicates that the common ancestor of the entire superclass was a GTPase and that a secondary switch to ATPase activity has occurred on several independent occasions during evolution.
Evidence for an ancestral core structure in nucleotide-binding proteins with the type A motif.
Dissecting the Role of a Conserved Motif (the Second Region of Homology) in the AAA Family of ATPases
TLDR
Analysis of the data in the light of the crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein suggests a plausible mechanism of ATP hydrolysis by the AAA ATPases, which invokes an intermolecular catalytic role for the SRH.
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.
...
1
2
3
4
5
...