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  • 1
    Electronic Resource
    Electronic Resource
    Regulation of transcription initiation at the Escherichia coli nir operon promoter: a new mechanism to account for co-dependence on two transcription factors (1998)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 27 (1998), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Expression from the Escherichia coli nir promoter is co-dependent on Fnr (a transcription factor triggered by oxygen starvation) and on NarL or NarP (transcription factors triggered by nitrite and nitrate ions). Fnr binds to a single DNA site centred between basepairs 41 and 42 upstream from the nir transcript start, whereas NarL and NarP bind to a site upstream, centred between basepairs 69 and 70. A novel mechanism to account for co-dependence on Fnr and NarL/NarP is suggested from experiments in which the spacing between the DNA sites for Fnr and NarL/NarP was altered. DNA sequence elements located upstream of the NarL/NarP-binding site are the targets for two or more proteins that act to repress Fnr-dependent activation of the nir promoter. This inhibition is counteracted by NarL or NarP. The model has been corroborated by the effects of several deletions and single base substitutions in the nir promoter upstream sequences: these deletions and substitutions prevent the binding of the repressor proteins. One of these repressors has been identified as the Fis protein, that binds to a site located 135–149 bp upstream of the nir transcript start: the binding of Fis is suppressed by a single base substitution at position −146. The other repressor protein(s) have yet to be identified, but appear to bind downstream of the DNA site for Fis: binding is suppressed by a single base substitution at position −99.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1998.00699.x
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  • 2
    Electronic Resource
    Electronic Resource
    Identification of dipeptide repeats and a cell wall sorting signal in the fimbriae-associated adhesin, Fap1, of Streptococcus parasanguis (1999)
    Oxford BSL : Blackwell Science Ltd
    Molecular microbiology 34 (1999), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Fap1, a fimbriae-associated protein, is involved in fimbriae assembly and adhesion of Streptococcus parasanguis FW213 (Wu et al., 1998). In this study, the sequence of the fap1 gene was resolved using a primer island transposition system. Sequence analysis indicated that fap1 was composed of 7659 nucleotides. The predicted Fap1 protein contains an unusually long signal sequence (50 amino acid residues), a cell wall sorting signal and two repeat regions. Repeat regions I and II have a similar dipeptide composition (E/V/I)S, composed of 28 and 1000 repeats respectively. The two regions combined accounted for 80% of the Fap1 coding region. The experimental amino acid composition and isoelectric point (pI) of Fap1 were similar to that predicted from the deduced Fap1 protein. Results of Northern analyses revealed that the fap1 open reading frame (ORF) was transcribed as a 7.8 kb monocistronic message. Insertional inactivation at the 3′ end, downstream of the fap1 ORF, did not affect Fap1, fimbrial expression or bacterial adhesion. Insertional inactivation of fap1 immediately upstream of the repeat region II abolished expression of Fap1 and fimbriae, and was concurrent with a diminution in adhesion of FW213. Inactivation of the cell wall sorting signal of fap1 also eliminated long fimbrial formation and reduced the ability of FW213 to bind to SHA. Fap1 was no longer anchored on the cell surface. Large quantities of truncated Fap1 were found in the growth medium instead. These results suggest that the fap1 ORF alone is sufficient to support Fap1 expression and adhesion, and demonstrate that anchorage of Fap1 on the cell surface is required for long fimbriae formation. These data further document the role of long fimbriae in adhesion of S. parasanguis FW213 to SHA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2958.1999.01670.x
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  • 3
    Electronic Resource
    Electronic Resource
    Rapid and transient response of soil respiration to rain (2004)
    Oxford, UK : Blackwell Science Ltd
    Global change biology 10 (2004), S. 0 
    Details
    ISSN: 1365-2486
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Energy, Environment Protection, Nuclear Power Engineering , Geography
    Notes: The influence of rainstorm on soil respiration of a mixed forest in southern New England, USA was investigated with eddy covariance, rain simulation and laboratory incubation. Soil respiration is shown to respond rapidly and instantaneously to the onset of rain and return to the prerain rate shortly after the rain stops. The pulse-like flux, most likely caused by the decomposition of active carbon compounds in the litter layer, can amount to a loss of 0.18 t C ha−1 to the atmosphere in a single intensive storm, or 5–10% of the annual net ecosystem production of midlatitude forests. If precipitation becomes more variable in a future warmer world, the rain pulse should play an important part in the transient response of the ecosystem carbon balance to climate, particularly for ecosystems on ridge-tops with rapid water drainage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1529-8817.2003.00787.x
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  • 4
    Electronic Resource
    Electronic Resource
    Investigating the role of secA2 in secretion and glycosylation of a fimbrial adhesin in Streptococcus parasanguis FW213 (2004)
    Oxford, UK : Blackwell Science Ltd
    Molecular microbiology 53 (2004), S. 0 
    Details
    ISSN: 1365-2958
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Adhesion of Streptococcus parasanguis FW213, a primary colonizer, to the tooth surface is mediated mainly by peritrichous long fimbriae. The fimbrial structural unit, Fap1, is indispensable for fimbriae biogenesis, adhesion to an in vitro tooth model and biofilm formation. Mature Fap1 is a glycoprotein with an apparent molecular mass of 200 kDa. Glycosylated Fap1 is not present in some mutants screened from a transposon mutant library. Localization of the transposition sites revealed a gene determined to be secA2, which is distinct from the canonical secA gene. In FW213, glycosylated Fap1 was present in all the subcellular fractions including the cytoplasm. In VT1574, a non-polar mutant of secA2 generated by in frame deletion, Fap1 was not secreted. Glycosylated Fap1 was present in the membrane and cytoplasm of the mutant, although in greatly reduced amounts. Fap1 secretion and abundance were restored when VT1574 was complemented by a plasmid-borne secA2. The secretion defect of the secA2 mutation appears to be limited to a small group of proteins such as Fap1 and FimA. These data suggested that Fap1 secretion rather than glycosylation was the major effect of the deletion of secA2; however, this deletion also had an impact on Fap1 abundance. Two more secA2 mutants with different regions deleted were tested for their ability to secrete Fap1. One mutant was completely unable to secrete Fap1 while the other was able to secrete, but in a decreased amount. These data suggest that the region deleted in the latter mutant (nucleotides 2032–2337) is dispensable for Fap1 secretion.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1365-2958.2004.04116.x
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