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Journal of Bacteriology, July 2000, p. 3673-3680, Vol. 182, No. 13
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
ComP, a Pilin-Like Protein Essential for Natural
Competence in Acinetobacter sp. Strain BD413: Regulation,
Modification, and Cellular Localization
Dirk
Porstendörfer,
Olivia
Gohl,
Frank
Mayer, and
Beate
Averhoff*
Institut für Mikrobiologie und Genetik,
Georg-August-Universität Göttingen, D-37077
Göttingen, Germany
Received 5 January 2000/Accepted 7 April 2000
We recently identified a pilin-like competence factor, ComP, which
is essential for natural transformation of the gram-negative soil
bacterium Acinetobacter sp. strain BD413. Here we
demonstrate that transcription and synthesis of the pilin-like
competence factor ComP are maximal in the late stationary growth phase,
whereas competence is induced immediately after inoculation of a
stationary-phase culture into fresh medium. Western blot analyses
revealed three forms of ComP, one with an apparent molecular mass of 15 kDa, which correlates with the molecular mass deduced from the DNA sequence, one 20-kDa form, which was found to be glycosylated, and one
23-kDa form. The glycosylation of ComP was not required for its
function in DNA binding and uptake. The 20-kDa form was present in the
cytoplasmic membrane, the periplasm, and the outer membrane, whereas
the 23-kDa form was located in the outer membrane and might be due to a
further modification. Immunological data suggest that ComP is not a
subunit of the pilus structures. Possible functions of ComP in the DNA
transformation machinery of Acinetobacter sp. strain BD413
are discussed.
*
Corresponding author. Mailing address: Institut
für Mikrobiologie und Genetik, Georg-August-Universität,
Grisebachstrasse 8, D-37077 Göttingen, Germany. Phone:
49-551-394041. Fax: 49-551-393793. E-mail:
BAVERHO{at}gwdg.de.
Journal of Bacteriology, July 2000, p. 3673-3680, Vol. 182, No. 13
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
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