|
Volume 272, Number 29,
Issue of July 18, 1997
pp. 17952-17960
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Identification of the Histidine Protein Kinase KinB in
Pseudomonas aeruginosa and Its Phosphorylation of the
Alginate Regulator AlgB
(Received for publication, February 24, 1997, and in revised form, April 30, 1997)
Sheng
Ma
,
Daniel J.
Wozniak
§
and
Dennis E.
Ohman
From the Department of Microbiology and Immunology,
University of Tennessee and the Veterans Administration Medical Center,
Memphis, Tennessee 38163 and the § Department of
Microbiology and Immunology, Bowman Gray School of Medicine at Wake
Forest University, Winston-Salem, North Carolina 27157-1064
The exopolysaccharide alginate is an important
virulence factor in chronic lung infections caused by the bacterium
Pseudomonas aeruginosa. Two positive activators for
alginate synthesis, algB and algR, are members
of a superfamily of response regulators of the two-component regulatory
system. AlgB belongs to the NtrC subfamily of response regulators and
is required for high-level production of alginate. In this study, an
open reading frame encoding a polypeptide of 66 kDa, designated
kinB, was identified immediately downstream of
algB. The sequence of KinB is homologous to the histidine
protein kinase members of two-component regulatory systems. Western
blot analysis of a P. aeruginosa strain carrying a
kinB-lacZ protein fusion and studies of
kinB-phoA fusions indicate that KinB localizes
to the inner membrane and has a NH2-terminal periplasmic domain. A KinB derivative containing the COOH terminus of KinB was
generated and purified. In the presence of [ -32P]ATP,
the purified COOH-terminal KinB protein was observed to undergo
progressive autophosphorylation in vitro. Moreover, the phosphoryl label of KinB could be rapidly transferred to purified AlgB.
Substitutions of the residues conserved among histidine protein kinases
abolished KinB autophosphorylation. These results provide evidence that
kinB encodes the AlgB cognate histidine protein kinase.

CiteULike Complore Connotea Del.icio.us Digg Reddit Technorati What's this?
This article has been cited by other articles:

|
 |

|
 |
 
F. H. Damron, J. Napper, M. A. Teter, and H. D. Yu
Lipotoxin F of Pseudomonas aeruginosa is an AlgU-dependent and alginate-independent outer membrane protein involved in resistance to oxidative stress and adhesion to A549 human lung epithelia
Microbiology,
April 1, 2009;
155(4):
1028 - 1038.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
F. H. Damron, D. Qiu, and H. D. Yu
The Pseudomonas aeruginosa Sensor Kinase KinB Negatively Controls Alginate Production through AlgW-Dependent MucA Proteolysis
J. Bacteriol.,
April 1, 2009;
191(7):
2285 - 2295.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
A. J. Leech, A. Sprinkle, L. Wood, D. J. Wozniak, and D. E. Ohman
The NtrC Family Regulator AlgB, Which Controls Alginate Biosynthesis in Mucoid Pseudomonas aeruginosa, Binds Directly to the algD Promoter
J. Bacteriol.,
January 15, 2008;
190(2):
581 - 589.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
J. B. Lyczak, C. L. Cannon, and G. B. Pier
Lung Infections Associated with Cystic Fibrosis
Clin. Microbiol. Rev.,
April 1, 2002;
15(2):
194 - 222.
[Abstract]
[Full Text]
[PDF]
|
 |
|

|
 |

|
 |
 
S. Ma, U. Selvaraj, D. E. Ohman, R. Quarless, D. J. Hassett, and D. J. Wozniak
Phosphorylation-Independent Activity of the Response Regulators AlgB and AlgR in Promoting Alginate Biosynthesis in Mucoid Pseudomonas aeruginosa
J. Bacteriol.,
February 15, 1998;
180(4):
956 - 968.
[Abstract]
[Full Text]
|
 |
|
Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.
|
Advertisement
Advertisement
|