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Journal of Bacteriology, March 1999, p. 1537-1543, Vol. 181, No. 5
Department of Microbiology, University of
Guelph, Guelph, Ontario, Canada N1G 2W1
Received 9 September 1998/Accepted 9 December 1998
ProP is an osmoregulatory compatible solute transporter in
Escherichia coli K-12. Mutation
proQ220::Tn5 decreased the rate constant for and the extent of ProP activation by an osmotic upshift but did not alter proP transcription or the ProP protein
level. Allele proQ220::Tn5 was
isolated, and the proQ sequence was determined. Locus
proQ is upstream from prc (tsp) at
41.2 centisomes on the genetic map. The
proQ220::Tn5 and prc
phenotypes were different, however. Gene proQ is predicted
to encode a 232-amino-acid, basic, hydrophilic protein (molecular mass,
25,876 Da; calculated isoelectric point, 9.66; 32% D, E, R, or K;
54.5% polar amino acids). The insertion of PCR-amplified
proQ into vector pBAD24 produced a plasmid containing the
wild-type proQ open reading frame, the expression of which
yielded a soluble protein with an apparent molecular mass of 30 kDa.
Antibodies raised against the overexpressed ProQ protein detected
cross-reactive material in proQ+ bacteria but
not in proQ220::Tn5 bacteria. ProQ
may be a structural element that influences the osmotic activation of
ProP at a posttranslational level.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Protein ProQ Influences Osmotic Activation of
Compatible Solute Transporter ProP in Escherichia coli
K-12

and
*
Corresponding author. Mailing address: Department
of Microbiology, University of Guelph, Guelph, ON N1G 2W1, Canada.
Phone: (519) 824-4120, ext. 3866. Fax: (519) 837-1802. E-mail:
jwood{at}uoguelph.ca.
Present address: Institut für Mikrobiologie und
Biotechnologie, Universität Bonn, Bonn D53115, Germany.
Present address: 331 Breezewood Crescent, Waterloo, ON N2L 5K4, Canada.
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