A novel peptidoglycan-associated lipoprotein found in the cell envelope of Pseudomonas aeruginosa and Escherichia coli.

Abstract:

:Protein H, one of the major outer membrane proteins Pseudomonas aeruginosa, shows an interesting interaction with the peptidoglycan layer of the cell. It is retained by peptidoglycan after extraction of the cell envelope with SDS solution at 35 degrees C. A protein of the same molecular weight (21,000) as protein H was found in the peptidoglycan-associated fraction of Escherichia coli K-12 prepared under the same conditions. This protein, designated here as protein 21K, was purified from the cell envelope of E. coli, and the properties of two proteins (protein H and protein 21K) were compared. By gas chromatographic analysis of purified protein 21K and protein H, it was found that both contained covalently linked fatty acid. In isotopic labeling experiments, [14C]palmitic acid and [2-3H]glycerol were incorported into both proteins H and 21K. These two proteins showed similar amino acid compositions, but no apparent correlation was found between protein 21K or protein H and Braun's lipoprotein. These results suggest that protein 21K of E. coli K-12 and protein H of P. aeruginosa PAO are a novel type of lipoprotein. All nine gram-negative bacteria tested, including enteric and non-enteric bacteria, contained a similar protein of apparent molecular weight 21,000 as a peptidoglycan-protein complex.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Mizuno T

doi

10.1093/oxfordjournals.jbchem.a132631

keywords:

subject

Has Abstract

pub_date

1979-10-01 00:00:00

pages

991-1000

issue

4

eissn

0021-924X

issn

1756-2651

journal_volume

86

pub_type

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