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Cloning and nucleotide sequence of the pst A gene of Wolinella succinogenes polysulphide reductase
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Titel: |
Cloning and nucleotide sequence of the pst A gene of Wolinella succinogenes polysulphide reductase |
In: | European Journal of Biochemistry, 206, 1992, 2, S. 503-510 |
veröffentlicht: |
Wiley
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Umfang: | 503-510 |
ISSN: |
1432-1033 0014-2956 |
DOI: | 10.1111/j.1432-1033.1992.tb16953.x |
Zusammenfassung: | <jats:p>The polysulphide reductase (formerly sulphur reductase) of <jats:italic>Wolinella succinogenes</jats:italic> is a component of the phosphorylative electron transport system with polysulphid as the terminal acceptor. Using an antiserum raised against the major subunit (PsrA, 85 kDa) of the enzyme, the corresponding gene (<jats:italic>psr A</jats:italic>) was cloned from a λ‐gene bank. The N‐terminal amino acid sequence of PsrA mapped within the <jats:italic>psr A</jats:italic> gene product, which also contained an apparent signal peptide. Downstream of the <jats:italic>Psr A</jats:italic> gene two more open reading frames (<jats:italic>psrB</jats:italic> and <jats:italic>psrC</jats:italic>) were found. the three genes may form a transcriptional unit with the transcription start site in front of <jats:italic>psr A</jats:italic>. The three genes were present only once on the genome. PsrA is a hydrophilic protein homologous to the largest subunits of six prokaryotic molybdoenzymes. PsrB is predicted to be hydrophilic, to contain ferredoxin‐like cysteine clusters and to be homologous to the smaller hydrophilic subunits of four molybdoenzymes. PsrC is predicted to be a hydrophobic protein that could possibly serve as the membrane anchor of the enzyme.</jats:p> |
Format: | E-Article |
Quelle: | Wiley (CrossRef) |
Sprache: | Englisch |