Open AccessAmino acid sequence for the peptide extension on the prolipoprotein of the Escherichia coli outer membrane.
Author(s) -
Sumiko Inouye,
Sansan Wang,
Jun Sekizawa,
Simon Halegoua,
Masayori Inouye
Publication year - 1977
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.74.3.1004
Subject(s) - peptide sequence , amino acid , biochemistry , bacterial outer membrane , escherichia coli , biology , peptide , messenger rna , sequence (biology) , chemistry , gene
The messenger RNA for the lipoprotein of the E. coli outer membrane was found to code for a putative precursor, prolipoprotein, which has 20 additional amino acid residues extending from the amino terminus of the lipoprotein. Using the prolipoprotein synthesized in an E. coli cell-free system directed by purified messenger RNA for the lipoprotein, the complete amino acid sequence of the amino-terminal precursor region was determined to be as follows: (formula: see text). It was also found that the prolipoprotein that accumulates in toluene-treated cells has the same sequence. The significance of the amino acid sequence is discussed in terms of the mechanism of biosynthesis and assembly of the lipoprotein in the E. coli outer membrane.