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J Biol Chem, Vol. 274, Issue 24, 17290-17296, June 11, 1999
From the Department of Microbiology and Molecular Genetics,
University of Texas Medical School, Houston, Texas 77030
Photosynthesis gene expression in
Rhodobacter sphaeroides is controlled in part by the
two-component (Prr) regulatory system composed of a membrane-bound
sensor kinase (PrrB) and a response regulator (PrrA). Hydropathy
profile-based computer analysis predicted that the PrrB polypeptide
could contain six membrane-spanning domains at its amino terminus and a
hydrophilic, cytoplasmic carboxyl terminus. Both the localization and
the topology of the PrrB sensor kinase have been studied by generating
a series of gene fusions with the Escherichia coli
periplasmically localized alkaline phosphatase and the cytoplasmic
-galactosidase. Eighteen prrB-phoA and five prrB-lacZ fusions were constructed and expressed in both
E. coli and R. sphaeroides. Enzymatic activity
assays and immunoblot analyses were performed to identify and to
localize the different segments of PrrB in the membrane. The data
obtained in E. coli generally correlated with the data
obtained in R. sphaeroides and support the computer
predictions. On the basis of the theoretical model and the results
provided by these studies, a topological model for the membrane
localization of the PrrB polypeptide is proposed.
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