Although bacteria have diverse membrane proteins, the function
of many of them remains unknown or uncertain even
in Escherichia coli. In this study, to investigate the function
of hypothetical membrane proteins, genome-wide analysis
of phenotypes of hypothetical membrane proteins was performed
under various envelope stresses. Several genes responsible
for adaptation to envelope stresses were identified.
Among them, deletion of YhcB, a conserved inner membrane
protein of unknown function, caused high sensitivities to various
envelope stresses and increased membrane permeability,
and caused growth defect under normal growth conditions.
Furthermore, yhcB deletion resulted in morphological
aberration, such as branched shape, and cell division defects,
such as filamentous growth and the generation of chromosome-
less cells. The analysis of antibiotic susceptibility
showed that the yhcB mutant was highly susceptible to various
anti-folate antibiotics. Notably, all phenotypes of the yhcB
mutant were completely or significantly restored by YhcB
without the transmembrane domain, indicating that the localization
of YhcB on the inner membrane is dispensable for its
function. Taken together, our results demonstrate that YhcB
is involved in cell morphology and cell division in a membrane
localization-independent manner.
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and in vitro, including production and secretion of tumor
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