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Journal of Bacteriology, September 2001, p. 5001-5007, Vol. 183, No. 17
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.17.5001-5007.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Proteolysis of the Caulobacter McpA
Chemoreceptor Is Cell Cycle Regulated by a ClpX-Dependent
Pathway
Jeng-Wen
Tsai and
M. R. K.
Alley*
Department of Biochemistry, Imperial College
of Science, Technology and Medicine, London SW7 2AY, United Kingdom
Received 1 November 2000/Accepted 8 June 2001
Proteolysis is involved in cell differentiation and the progression
through the cell cycle in Caulobacter crescentus. We
have constitutively expressed the transmembrane chemoreceptor McpA from
a multicopy plasmid to demonstrate that McpA degradation is modulated
during the cell cycle. The level of McpA protein starts to decrease
only when the swarmer cells differentiate into stalked cells. The
reduction in McpA protein levels is maintained until the stalked cells
develop into predivisional cells, at which point the level returns to
that observed in swarmer cells. The cell-cycle-regulated degradation of
McpA does not require the last 12 C-terminal amino acids, but it does
require three amino acids (AAL) located 15 residues away from the C
terminus. The ClpXP protease is essential in C.
crescentus for viability, and thus, we tested McpA
degradation in xylose conditional mutants. The effect on McpA
degradation occurred within two generations from the start of ClpX
depletion. The conditional mutants' growth rate was only slightly
affected, suggesting that ClpX is directly involved in McpA proteolysis.
*
Corresponding author. Mailing address: Department of
Biochemistry, Imperial College of Science, Technology and Medicine,
London SW7 2AY, United Kingdom. Phone: 44-20-75945304. Fax:
44-20-75945207. E-mail: d.alley{at}ic.ac.uk.
Journal of Bacteriology, September 2001, p. 5001-5007, Vol. 183, No. 17
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.17.5001-5007.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
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