A second Escherichia coli protein with CL synthase activity.
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.
Guo
D
D
Queens College CUNY, Department of Chemistry and Biochemistry, 65-30 Kissena Boulevard, Flushing, NY 11367, USA.
Tropp
B E
BE
D002308:Cardiolipins / Q000378:metabolism; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics*; D015870:Gene Expression; D005798:Genes, Bacterial; D007700:Kinetics; D008565:Membrane Proteins; D009154:Mutation; D010739:Phospholipase D / Q000378:metabolism; D010957:Plasmids; D013696:Temperature; D017855:Transferases (Other Substituted Phosphate Groups) / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism
D002308:Cardiolipins; D008565:Membrane Proteins; D017855:Transferases (Other Substituted Phosphate Groups); C100091:cardiolipin synthetase; D010739:Phospholipase D