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Cardiolipin tightly associates with the SecYEG protein channel complex, whereupon it stabilizes the dimer, creates a high-affinity binding surface for the SecA ATPase, and stimulates ATP hydrolysis. In addition to the effects on the structure and function, the subcellular distribution of the complex is modified by the cardiolipin content of the membrane. Together, the results provide rare and comprehensive insights into the action of a phospholipid on an essential transport complex, which appears to be relevant to a broad range of energy-dependent reactions occurring at membranes.<\/jats:p>","DOI":"10.1073\/pnas.0914680107","type":"journal-article","created":{"date-parts":[[2010,5,17]],"date-time":"2010-05-17T22:13:23Z","timestamp":1274134403000},"page":"10044-10049","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":168,"title":["The action of cardiolipin on the bacterial translocon"],"prefix":"10.1073","volume":"107","author":[{"given":"Vicki A. 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