A second Escherichia coli protein with CL synthase activity

被引：46
作者：
Guo, DG
Tropp, BE [1 ]
机构：
[1] CUNY Queens Coll, PhD Program Biochem, Flushing, NY 11367 USA
[2] CUNY Queens Coll, Dept Chem & Biochem, Flushing, NY 11367 USA
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 2000年 / 1483卷 / 02期
关键词：
cardiolipin; cardiolipin synthase; cls; f413; N-terminal deletion;
D O I：
10.1016/S1388-1981(99)00193-6
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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. (C) 2000 Elsevier Science B.V. All rights reserved.
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收藏
页码：263 / 274
页数：12
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