Genetic organization and sequence of the promoter-distal region of the tcp gene cluster of Vibrio cholerae

Ogierman, Monica A.; Zabihi, Susan; Mourtzios, Lefta; Manning, Paul A.

doi:10.1016/0378-1119(93)90589-u

Cited by 78 publications

(64 citation statements)

References 38 publications

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“…It is possible that these genes are part of an operon encoding the EPEC type IV fimbria biosynthetic machinery. One known type IV system, the Tcp gene cluster, contains more than 11 genes, with at least 9 of them belonging to the same transcriptional unit (37). The fact that the PstI-BamHI fragment can complement the pilD mutant in only one orientation suggests that expression of b.fP depends on a promoter from the vector (lacZ promoter in pDN19).…”

Section: Discussionmentioning

confidence: 99%

A plasmid-encoded prepilin peptidase gene from enteropathogenic Escherichia coli

1994

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Enteropathogenic Escherichia coli, a leading agent of infantile diarrhea worldwide, adheres to tissue culture cells in a pattern called "localized adherence." Localized adherence is associated with bundle-forming pili encoded by the plasmid bfpA gene, the product of which is homologous with the major structural subunit proteins of type IV fimbriae in other bacteria. Several of these proteins have been shown to be processed from a precursor by a specific prepilin peptidase. We cloned restriction fragments downstream of the bfpA gene into an E. coli-Pseudomonas aeruginosa shuttle vector and mobilized them into a P. aeruginosa prepilin peptidase (pilD) mutant. A plasmid containing a 1.3-kb PstI-BamHI fragment was able to complement the pilD mutation, as demonstrated by restoration of sensitivity to the pilus-specific bacteriophage PO4. The DNA sequence of this fragment revealed an open reading frame, designated bfpP, the predicted product of which is homologous to other prepilin peptidases, including TcpJ of Vibrio cholerae (30% identical amino acids), PulO of Klebsiella oxytoca (29%), and PilD of P. aeruginosa (28%). A bfpA::TnphoA mutant complemented with a bfpA-containing DNA fragment only partially processes the BfpA protein. When complemented with a larger fragment containing bfpP as well as bfpA, the mutant expresses the fully processed BfpA protein. P. aeruginosa PAK, but not a pilD mutant of PAK, expresses mature BfpA protein when the bfpA gene is mobilized into this strain. Thus, as in other type IV fimbria systems, enteropathogenic E. coli utilizes a specific prepilin peptidase to process the major subunit of the bundle-forming pilus. This prepilin petidase contains sequence and reciprocal functional homologies with the PilD protein of P. aeruginosa.

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Section: Discussionmentioning

confidence: 99%

A plasmid-encoded prepilin peptidase gene from enteropathogenic Escherichia coli

1994

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“…The PilB-like proteins vary both in length and in the degree of homology found in different parts of the molecule (for alignments see Whitchurch et al, 1991 ;Ogierman et al, 1993;Sandkvist et al, 1993). There are three subgroups that are closely related over their length: the secretion-specific proteins, PiIB/PiIF and PiIT/PiIU.…”

Section: Nucleotide-binding (Piib-like) Proteinsmentioning

confidence: 99%

Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein‐secretion apparatus: a general system for the formation of surface‐associated protein complexes

Hobbs

Mattick

1993

Molecular Microbiology

361

286

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Summary The Pseudomonas aeruginosa genes pilB‐D and pilQ are necessary for the assembly of type 4 fimbriae. Homologues of these genes and of the subunit (pilin) gene have been described in various different bacterial species, but not always in association with type 4 fimbrial biosynthesis and function. Pil‐like proteins are also involved in protein secretion, DNA transfer by conjugation and transformation, and morphogenesis of filamentous bacteriophages. It seems likely that the Pil homologues function in the processing and export of proteins resembling type 4 fimbrial sub‐units, and in their organization into fimbrial‐like structures. These may either be true type 4 fimbriae, or components of protein complexes which act in the transport of macromolecules (DNA or protein) into or out of the cell. Some PilB‐like and PilQ‐like proteins are apparently also involved in the assembly of non‐type 4 polymeric structures (filamentous phage virions and conjugative pili). The diverse studies summarized in this review are providing insight into an extensive infrastructural system which appears to be utilized in the formation of a variety of cell surface‐associated complexes.

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“…The gene encoding ToxT is located within the tcp gene cluster, between tcpF and tcpJ (Higgins et al, 1992;Kaufman et al, 1993;Ogierman et al, 1993). Just downstream of the gene for tcpF, there is a relatively strong transcriptional terminator (approximately 80% effective) (Higgins and DiRita, 1994).…”

Section: Introductionmentioning

confidence: 99%

“…In addition to genes in the tcpA operon, these studies disclosed two genes upstream of tcpA, tcpH (transcribed in the same direction as tcpA) and tcpI (divergently transcribed); the phenotypes of mutations in these genes suggested that TcpH was a positive regulator of the tcpA operon and TcpI was a negative regulator. Ogierman et al (1993) subsequently described an additional gene, tcpP, located between tcpI and tcpH and transcribed in the same direction as tcpH.…”

Section: Introductionmentioning

confidence: 99%

Phase variation in tcpH modulates expression of the ToxR regulon in Vibrio cholerae

Carroll

Tashima

Rogers

et al. 1997

Molecular Microbiology

124

126

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SummaryWe evaluated a spontaneous mutant of Vibrio cholerae, which was avirulent in an infant mouse and had reduced expression of cholera toxin and TcpA in response to environmental signals. The toxR, toxS and toxT genes in the mutant were normal, but transcription of toxT was absent. A plasmid expressing wild-type tcpP and tcpH complemented the mutant. The mutation resulted from a frameshift in a string of nine G residues within tcpH; similar slipped-strand mutations in tcpH arose at a frequency of 10 ¹4 during overnight growth and in the majority of colonies by the end of 5 days of growth in ToxR-inducing conditions. Transcription of tcpPH was regulated by temperature and pH independently of ToxR or ToxT. These results suggest that TcpH couples environmental signals (temperature and pH) to expression of the ToxR regulon, and provide a model for phase variation in the co-ordinate expression of cholera virulence factors.

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Genetic organization and sequence of the promoter-distal region of the tcp gene cluster of Vibrio cholerae

Cited by 78 publications

References 38 publications

A plasmid-encoded prepilin peptidase gene from enteropathogenic Escherichia coli

A plasmid-encoded prepilin peptidase gene from enteropathogenic Escherichia coli

Common components in the assembly of type 4 fimbriae, DNA transfer systems, filamentous phage and protein‐secretion apparatus: a general system for the formation of surface‐associated protein complexes

Phase variation in tcpH modulates expression of the ToxR regulon in Vibrio cholerae

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