Project Details

Description

Cell division is one of the most fundamental events for self-reproduction
of living organisms together with DNA-replication. However, it consists of
a very complex system, which is coordinated with DNA replication, membrane
biogenesis and various other cellular activities. Study of cell division
and membrane proteins has broad implications for understanding not only the
processes of normal growth of cells, but also those resulting in
uncontrolled growth such as found in cancer. Our long term goal is to solve the molecular mechanism of cell
division--precise sequence of events leading to cell division. However,
because of its complexity, we will still concentrate our efforts to
investigate individual key events such as the molecular mechanism of
regulation of gene expression, and biosynthesis and assembly of membrane
proteins in the present application. In particular, we will further explore a novel regulatory mechanism of gene
expression by means of a small RNA molecule, mRNA interfering complementory
RNA (micRNA), which was recently found in our laboratory. We will attempt
to elucidate the precise molecular mechanism of the mic regulation and at
the same time to apply this new concept to artificially regulate a specific
gene in Escherichia coli as well as in yeast. This novel method to
regulate a specific gene will provide a new, exciting approach for the
study of many essential genes of unknown functions including those required
for cell division. We will also continue to investigate the molecular
regulatory mechanism of gene expression of the major outer membrane
proteins, OmpA, ompC, and ompF. Second, we will continue to apply oligonucleotide-directed site-specific
mutagenesis to the prolipoprotein signal peptide to elucidate the exact
structural requirement of the signal peptide for protein secretion across
the membrane. Third, we will explore to find components required for protein secretion
(a) by characterizing the lepA gene product, which is known to be
cosynthesized with signal peptidase I and (b) by isolating and
characterizing the initial secretory complex formed in the cytoplasm in the
case of some mutant prolipoproteins. Fourth, we will attempt to clone the gene for the new lipoproteins found in
E. coli as well as the lipoprotein gene of Pseudomonas aeruginosa.
StatusFinished
Effective start/end date1/1/7512/31/04

Funding

  • National Institutes of Health
  • National Institutes of Health
  • National Institutes of Health
  • National Institutes of Health: $500,330.00
  • National Institutes of Health
  • National Institutes of Health
  • National Institutes of Health: $266,626.00
  • National Institutes of Health: $477,057.00
  • National Institutes of Health: $334,596.00
  • National Institutes of Health: $504,802.00
  • National Institutes of Health
  • National Institutes of Health: $406,510.00
  • National Institutes of Health: $383,263.00
  • National Institutes of Health
  • National Institutes of Health
  • National Institutes of Health: $502,949.00
  • National Institutes of Health: $488,696.00
  • National Institutes of Health
  • National Institutes of Health

ASJC

  • Medicine(all)
  • Biochemistry, Genetics and Molecular Biology(all)

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