Primary structures of the wild-type and mutant alleles encoding the phosphatidylglycerophosphate synthase of Escherichia coli

M Usui; H Sembongi; H Matsuzaki; K Matsumoto; I Shibuya

doi:10.1128/jb.176.11.3389-3392.1994

Primary structures of the wild-type and mutant alleles encoding the phosphatidylglycerophosphate synthase of Escherichia coli

J Bacteriol. 1994 Jun;176(11):3389-92. doi: 10.1128/jb.176.11.3389-3392.1994.

Authors

M Usui¹, H Sembongi, H Matsuzaki, K Matsumoto, I Shibuya

Affiliation

¹ Department of Biochemistry, Saitama University, Urawa, Japan.

Abstract

The nucleotide sequence of the Escherichia coli pgsA gene, encoding phosphatidylglycerophosphate synthase, is revised to code for an enzyme of 182 amino acid residues, instead of the 216 of a previous work (A. S. Gopalakrishnan, Y.-C. Chen, M. Temkin, and W. Dowhan, J. Biol. Chem. 261:1329-1338, 1986). The revised structure now explains the properties of the enzyme. Three pgsA mutants of different phenotypes were also analyzed: pgsA3, pgsA36, and pgsA10 have single-base replacements in codons 60 (Thr-->Pro), 1 (ATG-->ATA), and 92 (Thr-->Ile), respectively.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Alleles
Amino Acid Sequence
Base Sequence
Escherichia coli / enzymology
Escherichia coli / genetics*
Molecular Sequence Data
Mutation*
Recombinant Fusion Proteins
Sequence Analysis, DNA
Transferases (Other Substituted Phosphate Groups) / genetics*

Substances

Recombinant Fusion Proteins
Transferases (Other Substituted Phosphate Groups)
CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase