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Journal of Bacteriology, November 1998, p. 5932-5946, Vol. 180, No. 22
Department of Biological Sciences, University
at Albany, Albany, New York 12222
Received 28 April 1998/Accepted 9 September 1998
The small DNA binding protein Fis is involved in several different
biological processes in Escherichia coli. It has been shown to stimulate DNA inversion reactions mediated by the Hin family of
recombinases, stimulate integration and excision of phage
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Identification and Characterization of the
fis Operon in Enteric Bacteria
genome,
regulate the transcription of several different genes including those
of stable RNA operons, and regulate the initiation of DNA replication
at oriC. fis has also been isolated from Salmonella typhimurium, and the genomic sequence of Haemophilus
influenzae reveals its presence in this bacteria. This work
extends the characterization of fis to other organisms.
Very similar fis operon structures were identified in the
enteric bacteria Klebsiella pneumoniae, Serratia
marcescens, Erwinia carotovora, and
Proteus vulgaris but not in several nonenteric bacteria. We
found that the deduced amino acid sequences for Fis are 100% identical
in K. pneumoniae, S. marcescens,
E. coli, and S. typhimurium and 96 to
98% identical when E. carotovora and P. vulgaris Fis are considered. The deduced amino acid sequence for
H. influenzae Fis is about 80% identical and 90%
similar to Fis in enteric bacteria. However, in spite of these
similarities, the E. carotovora, P. vulgaris, and H. influenzae Fis proteins are not
functionally identical. An open reading frame (ORF1) preceding
fis in E. coli is also found in all these
bacteria, and their deduced amino acid sequences are also very similar.
The sequence preceding ORF1 in the enteric bacteria showed a very
strong similarity to the E. coli fis P region from
53 to +27 and the region around
116 containing an ihf
binding site. Both
-galactosidase assays and primer extension assays
showed that these regions function as promoters in vivo and are subject
to growth phase-dependent regulation. However, their promoter strengths
vary, as do their responses to Fis autoregulation and integration host
factor stimulation.
*
Corresponding author. Mailing address: Department of
Biological Sciences, 1400 Washington Ave., University at Albany,
Albany, NY 12222. Phone: (518) 442-4333. Fax: (518) 442-4767. E-mail: osuna{at}cnsunix.albany.edu.
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