Topographical distribution of penicillin-binding proteins in the Escherichia coli membrane.

Journal of Bacteriology
C E Buchanan

Abstract

The penicillin-binding proteins (PBPs) found in the membranes of Escherichia coli X925 minicells (primarily cell ends or septa) were compared with those found in rod-shaped cells (primarily sidewalls) in an effort to determine whether certain PBPs are unevenly distributed over the bacterial cell membrane. The seven major PBPs of E. coli were all present in minicell membranes. PBP 1B was altered in minicells, however, appearing as two bands on sodium dodecyl sulfate-polyacrylamide gels rather than the usual three. PBP 2, which is needed for longitudinal growth of the cell but not for septum formation, was significantly reduced in minicell membranes. This observation is consistent with the fact that minicells contain very little sidewall material and raises the possibility that the specialized function of PBP 2 may be determined or regulated by its uneven topographical distribution in the membrane. None of the PBPs appeared to be selectively enriched in minicell membranes.

Citations

Mar 1, 1984·European Journal of Biochemistry·A Rodríguez-TébarD Vázquez
May 10, 2001·Journal of Bacteriology·S R Lybarger, J R Maddock
Jun 26, 1999·Molecular Microbiology·I Fishov, C L Woldringh
Sep 1, 1982·Microbiological Reviews·N H Mendelson
Dec 1, 1987·Journal of Bacteriology·L C FerreiraU Schwarz
Jul 1, 1982·Journal of Bacteriology·C E Buchanan, M O Sowell

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