Conformational change of the γ subunit regulates the ATP hydrolysis activity of cyanobacterial ATP synthase

Sunamura, Ei-Ichiro; Konno, Haruyoshi; Imashimizu, Mari; Mochimaru, Mari; Hisabori, Toru

doi:10.1016/j.bbabio.2012.06.076

Biochimica et Biophysica Acta (BBA) - Bioenergetics

2012

DOI: 10.1016/j.bbabio.2012.06.076

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Conformational change of the γ subunit regulates the ATP hydrolysis activity of cyanobacterial ATP synthase

Ei-Ichiro Sunamura

Haruyoshi Konno

Mari Imashimizu

et al.

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“…In the case of cyanobacterial and chloroplast ATP synthase, the γ subunit has a unique 30-40 amino acid sequence in this globular domain. In the previous study, we prepared the mutant α 3 β 3 γ complex of cyanobacterial ATP synthase whose inserted sequence was deleted [2,3]. Although the insertion is far from catalytic sites, the mutant complex shows a remarkable increase in ATP hydrolysis activity.…”

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confidence: 99%

IF1 (mitochondrial FoF1 inhibitor protein); from single molecule to knock-out mouse

Suzuki

Fujikawa

Nakamura

et al. 2012

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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complex, has a hexagonal arrangement consisting of an α 3 β 3 ring and the γ subunit [1]. The γ subunit is a central shaft of this motor enzyme and has a coiled-coil structure of N-and C-terminal α-helices and a globular domain. In the case of cyanobacterial and chloroplast ATP synthase, the γ subunit has a unique 30-40 amino acid sequence in this globular domain. In the previous study, we prepared the mutant α 3 β 3 γ complex of cyanobacterial ATP synthase whose inserted sequence was deleted [2,3]. Although the insertion is far from catalytic sites, the mutant complex shows a remarkable increase in ATP hydrolysis activity. We revealed that this activation was caused by a reduced tendency to lapse into ADP inhibition. Based on this study, we postulated that deletion of the insertion induces a conformational change of the γ subunit that results in a change of the activity. To prove the hypothesis, we prepared a mutant complex which can lock the possible conformational change by a disulfide bond formation. Consequently, the obtained mutant showed a significant change in ATP hydrolysis activity by the disulfide bond formation. Highly active locked complex was insensitive to LDAO, suggesting that the complex is resistant to ADP inhibition. In addition, the lock of conformational change affected ε inhibition. These results strongly suggest that the conformational change in the γ subunit can regulates the activity by changing both ADP inhibition and ε inhibition, which are thought to be regulatory mechanisms to prevent a wasteful ATP hydrolysis.

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mentioning

confidence: 99%

IF1 (mitochondrial FoF1 inhibitor protein); from single molecule to knock-out mouse

Suzuki

Fujikawa

Nakamura

et al. 2012

Biochimica et Biophysica Acta (BBA) - Bioenergetics

View full text Add to dashboard Cite

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Conformational change of the γ subunit regulates the ATP hydrolysis activity of cyanobacterial ATP synthase

Cited by 1 publication

References 3 publications

IF1 (mitochondrial FoF1 inhibitor protein); from single molecule to knock-out mouse

IF1 (mitochondrial FoF1 inhibitor protein); from single molecule to knock-out mouse

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