Map of genes for carotenoid and bacteriochlorophyll biosynthesis in Rhodopseudomonas capsulata

Yen, Huei-Che; Marrs, Barry L.

doi:10.1128/jb.126.2.619-629.1976

Cited by 277 publications

(78 citation statements)

References 13 publications

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“…The R. capsulatus strains used in the study are described in Table 1, SB1003 is a spontaneous rifampicin-resistant strain and is used as the wild type in this study (Yen and Marrs, 1976). J61 Braddock.…”

Section: Bacterial Strains and Plasmidsmentioning

confidence: 99%

Analysis of the promoters and upstream sequences of nifA1 aud nifA2 in Rhodobacter capsulatus; activation requires ntrC but not rpoN

Foster‐Hartnett

Kranz

1992

Molecular Microbiology

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Transcription of Rhodobacter capsulatus genes encoding the nitrogenase polypeptides (nifHDK) is repressed by fixed nitrogen and oxygen. R. capsulatus nifA1 and nifA2 encode identical NIFA proteins that activate transcription of nifHDK and other nif genes. In this study, we report that nifA1-lacZ and nifA2-lacZ fusions are repressed in the presence of NH3 and activated to similar levels under nitrogen-deficient conditions. This nitrogen-controlled activation was dependent on R. capsulatus ntrC (which encodes a transcriptional activator) but not rpoN (which encodes an RNA polymerase sigma factor). We have used primer extension analyses of nifA1, nifA2 and nifH and deletion analyses of nifA1 and nifA2 upstream regions to define likely promoters and cis upstream activation sequences required for nitrogen control of these genes. Primer extension mapping confirmed that ntrC but not rpoN is required for nifA1 and nifA2 activation, and that nifA1 and nifA2 do not possess typical RPON-activated promoters.

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Section: Bacterial Strains and Plasmidsmentioning

confidence: 99%

Analysis of the promoters and upstream sequences of nifA1 aud nifA2 in Rhodobacter capsulatus; activation requires ntrC but not rpoN

Foster‐Hartnett

Kranz

1992

Molecular Microbiology

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“…In order to determine the reading frame of the hemA gene we sequenced the gene from both the wild-type strain SB1003 [8] and the hemA mutant AJB529 [9] (Fig. 1).…”

Section: Sequence Analysis Of the Hema Genementioning

confidence: 99%

Use of a lacZ fusion to study transcriptional regulation of the Rhodobacter capsulatus hemA gene

Wright

1991

FEMS Microbiology Letters

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An EcoRI fragment containing the Rhodobacter capsulatus hemA promoter has been cloned into a lacZ translational fusion vector. The resulting plasmid produced a hemA-lacZ fusion protein with a molecular mass of 147,000. Expression of the hemA-lacZ fusion, as measured by production of beta-galactosidase, was regulated 2- to 3-fold by oxygen tension. The unexpectedly small change in beta-galactosidase levels suggests that transcriptional regulation of the hemA gene is not the major factor in oxygen-mediated control of porphyrin synthesis.

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“…The wild-type chromosomal copy of the atp2 operon was deleted by taking advantage of the so-called GTA, bacteriophage-like particles produced by Rb. capsulatus [33] as described previously [26]. GTA particles are produced by Rb.…”

Section: Subunit a Mutagenesismentioning

confidence: 99%

A point mutation in the ATP synthase of Rhodobacter capsulatus results in differential contributions of ΔpH and Δφ in driving the ATP synthesis reaction

Turina

Melandri

2002

European Journal of Biochemistry

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The interface between the c-subunit oligomer and the a subunit in the F 0 sector of the ATP synthase is believed to form the core of the rotating motor powered by the protonic flow. Besides the essential cAsp61 and aArg210 residues (Escherichia coli numbering), a few other residues at this interface, although nonessential, show a high degree of conservation, among these aGlu219. The homologous residue aGlu210 in the ATP synthase of the photosynthetic bacterium Rhodobacter capsulatus has been substituted by a lysine. Inner membranes prepared from the mutant strain showed approximately half of the ATP synthesis activity when driven both by light and by acid-base transitions. As estimated with the ACMA assay, proton pumping rates in the inner membranes were also reduced to a similar extent in the mutant. The most striking impairment of ATP synthesis in the mutant, a decrease as low as 12 times as compared to the wild-type, was observed in the absence of a transmembrane electrical membrane potential (Du) at low transmembrane pH difference (DpH). Therefore, the mutation seems to affect both the mechanism responsible for coupling F 1 with proton translocation by F 0 , and the mechanism determining the relative contribution of DpH and Du in driving ATP synthesis.

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Map of genes for carotenoid and bacteriochlorophyll biosynthesis in Rhodopseudomonas capsulata

Cited by 277 publications

References 13 publications

Analysis of the promoters and upstream sequences of nifA1 aud nifA2 in Rhodobacter capsulatus; activation requires ntrC but not rpoN

Analysis of the promoters and upstream sequences of nifA1 aud nifA2 in Rhodobacter capsulatus; activation requires ntrC but not rpoN

Use of a lacZ fusion to study transcriptional regulation of the Rhodobacter capsulatus hemA gene

A point mutation in the ATP synthase of Rhodobacter capsulatus results in differential contributions of ΔpH and Δφ in driving the ATP synthesis reaction

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