2013
ε subunit of Bacillus subtilis F1-ATPase relieves MgADP inhibition.
PloS one
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- Volume
- 8
- Number
- 8
- First page
- e73888
- Last page
- Language
- English
- Publishing type
- Research paper (scientific journal)
- DOI
- 10.1371/journal.pone.0073888
- Publisher
- Public Library of Science
MgADP inhibition, which is considered as a part of the regulatory system of ATP synthase, is a well-known process common to all F1-ATPases, a soluble component of ATP synthase. The entrapment of inhibitory MgADP at catalytic sites terminates catalysis. Regulation by the ε subunit is a common mechanism among F1-ATPases from bacteria and plants. The relationship between these two forms of regulatory mechanisms is obscure because it is difficult to distinguish which is active at a particular moment. Here, using F1-ATPase from Bacillus subtilis (BF1), which is strongly affected by MgADP inhibition, we can distinguish MgADP inhibition from regulation by the ε subunit. The ε subunit did not inhibit but activated BF1. We conclude that the ε subunit relieves BF1 from MgADP inhibition.
- Link information
- ID information
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- DOI : 10.1371/journal.pone.0073888
- ISSN : 1932-6203
- Pubmed ID : 23967352
- Pubmed Central ID : PMC3742539
- SCOPUS ID : 84881492336