Elsevier

Gene

Volume 140, Issue 1, 1994, Pages 25-31
Gene

Cloning and sequences of the structural (hupSLC) and accessory (hupDHI) genes for hydrogenase biosynthesis in Thiocapsa roseopersicina

https://doi.org/10.1016/0378-1119(94)90726-9Get rights and content

Abstract

The first molecular biology study on the purple sulfur photosynthetic bacterium Thiocapsa roseopersicina is reported, namely, the construction of cosmid libraries and isolation of a hydrogenase gene cluster by hybridization with hydrogenase structural genes from the purple non-sulfur bacterium, Rhodobacter capsulatus. The sequenced gene cluster contains six open reading frames, the products of which show significant degrees of identity (from 40 to 78%) with hydrogenase gene products necessary for biosynthesis of the group-I of [NiFe]hydrogenases. The structural hupSLC genes encode the small and large hydrogenase subunits and a hydrophobic protein shown to accept electrons from hydrogenase in R. capsulatus. They are followed downstream by three genes, hupDHI, which are similar to hydrogenase accessory genes found in other bacteria.

References (36)

  • B. Cauvin et al.

    The hydrogenase structural operon in Rhodobacter cupsulatus contains a third gene, hupM, necessary for the formation of a physiologically competent hydrogenase

    Mol. Microbiol.

    (1991)
  • A. Colbeau et al.

    Organisation of the genes necessary for hydrogenase expression in Rhodobacter capsulatus. Sequence analysis and identification of two regulatory mutants

    Mol. Microbiol.

    (1993)
  • F. Dross et al.

    The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes

    Eur. J. Biochem.

    (1992)
  • E. Hidalgo et al.

    Nucleotide sequence of the hydrogenase structural genes from Rhizobium leguminosarum

    Plant Mol. Biol.

    (1990)
  • E. Hidalgo et al.

    Nucleotide sequence and characterization of four additional genes of the hydrogenase structural operon from Rhizobium leguminosarum bv. viciae

    J. Bacteriol.

    (1992)
  • C. Kortlüke et al.

    A gene complex coding for the membrane-bound hydrogenase of Alcaligenes eutrophus H16

    J. Bacteriol.

    (1992)
  • K.L. Kovacs et al.

    Immunological relationships among hydrogenases

    J. Bacteriol.

    (1989)
  • M. Leclerc et al.

    Cloning an sequencing of the genes encoding the large and the small subunits of the H2 uptake hydrogenase (hup) of Rhodobacter capsulatus

    Mol. Gen. Genet.

    (1988)
    M. Leclerc et al.

    Cloning an sequencing of the genes encoding the large and the small subunits of the H2 uptake hydrogenase (hup) of Rhodobacter capsulatus

    Erratum

    (1989)
  • Cited by (40)

    • The HydS C-terminal domain of the Thiocapsa bogorovii HydSL hydrogenase is involved in membrane anchoring and electron transfer

      2021, Biochimica et Biophysica Acta - Bioenergetics
      Citation Excerpt :

      The purple sulfur bacterium Thiocapsa bogorovii BBS (previously named Thiocapsa roseopersicina) [ [2]; https://lpsn.dsmz.de/species/thiocapsa-bogorovii] contains at least five sets of structural genes and synthesizes at least four different hydrogenases, which have been shown to be regulated independently [3,4]. Genes of HupSLC hydrogenase were first discovered in T. bogorovii BBS [5]. This hydrogenase belongs to 1d subgroup.

    • Heterologous functionality and roles of conserved cysteine motifs of the [NiFe]-hydrogenase accessory protein, HupK/HoxV

      2014, International Journal of Hydrogen Energy
      Citation Excerpt :

      Nevertheless, variations in the general scheme can be anticipated, because T. roseopersicina expresses four hydrogenases associated with distinct metabolic functions [22]. In T. roseopersicina, few accessory genes were identified in the hydrogenase structural genes clusters (hupDHI, hoxW, hynH) [30,31], others (hypA, hypB, hypC1, hypC2, hypD, hypE, hypF, hynD and hupK) were scattered in the genome in several loci [26,27]. Analysis of ΔhupK mutant strains disclosed that HupK protein was important for the formation of the functionally active membrane-bound hydrogenases (HynSL and HupSL), but not for the biosynthesis of the soluble enzymes (Hox1, Hox2) [27].

    • Relationship between PHA and hydrogen metabolism in the purple sulfur phototrophic bacterium Thiocapsa roseopersicina BBS

      2012, International Journal of Hydrogen Energy
      Citation Excerpt :

      Our model organism, Thiocapsa roseopersicina BBS is a photosynthetic purple sulfur bacterium (PSB) which can be propagated photochemolitoautotrophically on reduced sulfur compounds and simple organic substrates such as acetate, succinate, pyruvate, glucose, etc. It contains four active [NiFe] hydrogenases: two of them are membrane-associated (HupSL, HynSL) [18,19], and Hox1 [20] and the recently described Hox2 [21] are soluble hydrogenases. This microbe is able to fix molecular nitrogen in the absence of alternative nitrogen sources.

    • Specificity and selectivity of HypC chaperonins and endopeptidases in the molecular assembly machinery of [NiFe] hydrogenases of Thiocapsa roseopersicina

      2010, International Journal of Hydrogen Energy
      Citation Excerpt :

      The phototrophic purple sulfur bacterium, Thiocapsa roseopersicina BBS can grow under various environmental conditions, it is cultivated usually phototrophically under anaerobic conditions in laboratory. The wild-type strain (BBS) harbours at least three functional [NiFe] hydrogenases (HupSL, HynSL, HoxEFUYH) [20–23] and a silent regulatory hydrogenase (HupTUV) [24]. The basic principles of [NiFe] hydrogenase maturation are expected to be valid for the hydrogenases of T. roseopersicina, as these ancient enzymes are well-conserved.

    • A novel approach for biohydrogen production

      2006, International Journal of Hydrogen Energy
    • Novel approaches to exploit microbial hydrogen metabolism

      2004, Biohydrogen III: Renewable Energy System by Biological Solar Energy Conversion
    View all citing articles on Scopus

    Permanent address: Institute of Biophysics, Biological Research Centre, Hungarian Academy of Sciences P.O. Box 521, Szeged 6701, Hungary. Tel. (36-62) 433-465.

    View full text