
Alterations in envelope structure of heptose-deficient mutants of Escherichia coli as revealed by freeze-etching.
Author(s) -
Manfred Bayer,
Jane Koplow,
Howard Goldfine
Publication year - 1975
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.72.12.5145
Subject(s) - cleavage (geology) , cell envelope , heptose , bacterial outer membrane , mutant , biophysics , membrane , inner membrane , chemistry , cell membrane , membrane protein , escherichia coli , biology , crystallography , biochemistry , paleontology , fracture (geology) , gene
The surface of freeze-etched E. coli strain GR467, a heptose-deficient ("deep rough") mutant derived from CR34, was studied by electron microscopy. The outer membrane of GR467 has an increased ratio of phospholipid to protein, mainly due to a decreased protein content. Freeze-etched CR34 showed structural features indistinguishable for wild-type E. coli, i.e., the primary cleavage occurring in the inner membrane with only minor appearance of cleavage within the outer membrane. In contrast to this, in mutant GR467 most of the freeze-cleavages had taken place along a new plane, presumably in a hydrophobic region of the outer membrane. In this cleavage plane numerous particles were seen. Often the cleavage extended over the entire exposed cell surface; occasionally only a few large plateaus were visible, around which the next deeper cleavage plane, that of the protoplasmic or inner membrane, was discernible. Two spontaneous revertants (R11 and R16) with protein and lipid A levels similar to wild-type cells showed mostly freeze fractures with wild-type characteristics, and only a few cells had retained fracturing properties of GR467. A partial revertant revealed intermediate characteristics. Thus, there appears to be a morphological correlation with the chemical data relating the amount of outer membrane protein with the heptose content of the lipopolysaccharide.