A second Escherichia coli protein with CL synthase activity |
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| Authors: | Dagang Guo Burton E Tropp |
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| Institution: | 1. Queens College CUNY, Department of Chemistry and Biochemistry, 65-30 Kissena Boulevard, Flushing, NY 11367, USA;2. Ph.D. Program in Biochemistry, City University of New York, Queens College, Flushing, NY, USA |
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| Abstract: | The Escherichia coli open reading frame f413, which has the potential to code for a polypeptide homologous to cardiolipin (CL) synthase, has been cloned. Its polypeptide product has a molecular mass of 48 kDa, is membrane-bound, and catalyzes CL formation but does not hydrolyze CL. A comparison of the sequences predicted for the polypeptides encoded by f413 and cls indicates that the N-terminal residues specified by cls may be unnecessary for CL synthase activity. Construction of a truncated cls gene and characterization of its polypeptide product have confirmed this conclusion. |
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| Keywords: | Cardiolipin Cardiolipin synthase N-Terminal deletion |
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