Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 283, Issue 20, Pages 13745-13752Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M709632200
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Funding
- Biotechnology and Biological Sciences Research Council Funding Source: Medline
- Wellcome Trust Funding Source: Medline
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p97, an essential chaperone in endoplasmic reticulum-associated degradation and organelle biogenesis, contains two AAA domains (D1 and D2) and assembles as a stable hexamer. We present a quantitative analysis of nucleotide binding to both D1 and D2 domains of p97, the first detailed study of nucleotide binding to both AAA domains for this type of AAA+ ATPase. We report that adenosine 5'-O-(thiotriphosphate) (ATP gamma S) binds with similar affinity to D1 and D2, but ADP binds with higher affinity to D1 than D2, offering an explanation for the higher ATPase activity in D2. Stoichiometric measurements suggest that although both ADP and ATP gamma S can saturate all 6 nucleotide binding sites in D1, only 3-4 of the 6 D2 sites can bind ATP gamma S simultaneously. ATP gamma S binding triggers a downstream cooperative conformational change of at least three monomers, which involves conserved arginine fingers and is necessary for ATP hydrolysis.
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