Transcriptional analysis of the Aeromonas salmonicida S-layer protein gene vapA

Chu, Shijian; Gustafson, Corinne E.; Feutrier, J; Cavaignac, Sonia M.; Trust, Trevor J.

doi:10.1128/jb.175.24.7968-7975.1993

Cited by 29 publications

(22 citation statements)

References 49 publications

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“…The half-life of the S-protein mRNAs has only been determined for three species, Caulobacter crescentus (10 to 15 min; Fisher et al, 1988), A. salmonicida (22 min;Chu et al, 1993), and L. acidophilus (15 min;Boot et al, 1996a). Secondary-structure formation in the long, untranslated leader sequences, found for many S-protein mRNAs (Table 1) …”

Section: Expression Of S-protein Genesmentioning

confidence: 99%

Expression, secretion and antigenic variation of bacterial S‐layer proteins

Boot

Pouwels

1996

Molecular Microbiology

119

108

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SummaryThe function of the S-layer, a regularly arranged structure on the outside of numerous bacteria, appears to be different for bacteria living in different environments. Almost no similarity exists between the primary sequences of S-proteins, although their amino acid composition is comparable. S-protein production is directed by single or multiple promoters in front of the S-protein gene, yielding stable mRNAs. Most bacteria secrete S-proteins via the general secretory pathway (GSP). Translocation of S-protein across the outer membrane of Gram-negative bacteria sometimes occurs by S-protein-specific branches of the GSP. O-polysaccharide side-chains of the lipopolysaccharide component of the cell wall of Gramnegative bacteria appear to function as receptors for attachment of the S-layer. Silent S-protein genes have been found in Campylo-bacter fetus and Lactobacillus acidophilus. These silent genes are placed in the expression site in a fraction of the bacterial population via inversion of a chromosomal segment.

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Section: Expression Of S-protein Genesmentioning

confidence: 99%

Expression, secretion and antigenic variation of bacterial S‐layer proteins

Boot

Pouwels

1996

Molecular Microbiology

119

108

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“…1, Spots 1 -5, 37 and 38). It has been estimated that in order to cover its entire surface with the VapA protein, A. salmonicida needs to synthesize approximately 5000 copies of the VapA protein per second (Chu et al 1993). The precise nature of the multiple isoelectropherotypes of the VapA protein in A. salmonicida has not been elucidated.…”

Section: Discussionmentioning

confidence: 99%

Identification of the major outer membrane proteins of Aeromonas salmonicida

Ebanks¹,

Goguen²,

McKinnon³

et al. 2005

Dis. Aquat. Org.

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Aeromonas salmonicida subsp. salmonicida is a Gram-negative bacterium that is the etiological agent of furunculosis, a serious infectious disease of salmonids. Aeromonas spp. are ubiquitous waterborne bacteria responsible for a wide spectrum of diseases among aquatic organisms and humans. Bacterial outer membrane proteins (OMPs) play a significant role in virulence as they comprise the outermost surface in contact with host cells and immune defense factors. To identify the major OMPs of A. salmonicida a proteomic analysis was undertaken using a carbonate OMP-enrichment protocol. The enriched OMP-extracts were separated by 2-dimensional electrophoresis (2-DE) and the spots identified using liquid chromatography/mass spectrometry/mass spectrometry (LC/MS/MS) via an electrospray ionization source. In total, 76 unique proteins were identified from the 125 spots observed on the 2-D gel. The surface layer (S-layer) VapA protein dominated the A. salmonicida OMP 2-D profile, accounting for 60% of the protein on the 2-D gels. Among the other outer membrane proteins identified were at least 10 porins and various receptors involved in nutrient acquisition. Also identified in the carbonate insoluble fraction were phosphoglycerate kinase, enolase and others that lacked classical export sorting signals. The putative association of these proteins with the cell surface might provide new insights concerning the biological and pathogenic roles of these molecules in A. salmonicida infection. This work represents the first systematic attempt to characterize the cell surface of A. salmonicida.

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“…Thus, similar translational regulatory mechanisms could also exist for these genes. In addition to this function, these 5ЈUTR of the S-layer protein mRNAs could also be implicated in the stability of their transcripts (Fisher et al, 1988;Chu et al, 1993;, as has been demonstrated for the E. coli OmpA mRNA (Melefors and Gabian, 1988). These two mechanisms would help to explain the fast regeneration of the S-layer observed under some experimental conditions (Lortal et al, 1992;Firtel et al, 1995).…”

Section: јUtr Mrna Binding By Slpa and Translational Autoregulationmentioning

confidence: 97%

Surface proteins and a novel transcription factor regulate the expression of the S‐layer gene in Thermus thermophilus HB8

Fernández-Herrero

Olabarría

Berenguer

1997

Molecular Microbiology

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SummaryWe have identified proteins that control the expression of slpA, the gene encoding the crystalline surface layer of Thermus thermophilus HB8. We cloned three genes from T. thermophilus that specifically repressed the expression of the slpA promoter in Escherichia coli. The proteins encoded by two of them (Rep6 and Rep29) bound in vitro to the slpA promoter, while that from the third (Rep54) bound specifically to the 5Ј-untranslated region (5ЈUTR) of the slpA mRNA. Rep6 protein was identified as a C-fragment from a Thermus cytoplasmic basic protein of 28 kDa, whose coding gene, slrA (for S-layer regulator), was characterized. Surprisingly, Rep29 was identified as a C-fragment of SlpM, an S-layerlike protein that is overexpressed in slpA mutants. Insertional inactivation of slrA and slpM demonstrated their in vivo function in the control of slpA transcription: SlrA acts as a repressor, and SlpM as an activator. Even more surprising was the identification of Rep54, the 5ЈUTR mRNA-binding protein, as a C-terminal fragment of the SlpA protein. This result, in addition to further in vivo evidence presented here, supports the existence of a translational autoregulation in slpA expression. The physiological meaning of overlapping transcriptional and translational controls of S-layer expression, and its relationships with other systems, are discussed.

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Transcriptional analysis of the Aeromonas salmonicida S-layer protein gene vapA

Cited by 29 publications

References 49 publications

Expression, secretion and antigenic variation of bacterial S‐layer proteins

Expression, secretion and antigenic variation of bacterial S‐layer proteins

Identification of the major outer membrane proteins of Aeromonas salmonicida

Surface proteins and a novel transcription factor regulate the expression of the S‐layer gene in Thermus thermophilus HB8

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