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(Received for publication, August 8,
1995; and in revised form, August 28, 1995) The pilA gene of Neisseria gonorrhoeae encodes
the response regulator of a two-component regulatory system that
controls pilin gene expression. Examination of the primary sequence of
PilA indicates that the protein contains at least two functional
domains. The N-terminal region has a proposed helix-turn-helix motif
thought to be involved in DNA binding. This region also contains the
residues that are presumed to form the acidic pocket involved in
phosphorylation by PilB, the sensor kinase of the system. The C
terminus of the protein has extensive homology to the G (GTP-binding)
domains of the eukaryotic signal recognition particle (SRP) 54-kDa
protein and the
Volume 270,
Number 44,
Issue of November 3, 1995 pp. 26045-26048
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
subunit of the SRP receptor, or docking protein.
This homology also extends to similar regions of the bacterial SRP
homologs Ffh and FtsY. Here, we demonstrate that purified PilA has
significant GTPase activity, and that this activity has an absolute
requirement for MgCl
and is sensitive to KCl and low pH. We
also show that PilA has a strict specificity for GTP, and that GTP
hydrolysis follows first order kinetics, with a maximum velocity (V
) of 1900 pmol of P
produced per
min per mg of protein and a K for GTP of
9.6 µM at 37 °C.
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