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Biochim Biophys Acta. 2000 Jan 17;1483(2):263-74.

A second Escherichia coli protein with CL synthase activity.

Author information

1
Queens College CUNY, Department of Chemistry and Biochemistry, 65-30 Kissena Boulevard, Flushing, NY 11367, USA.

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.

PMID:
10634942
DOI:
10.1016/s1388-1981(99)00193-6
[Indexed for MEDLINE]

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