Open AccessMolecular biology studies of the uptake hydrogenase of Rhodobacter capsulatus and Rhodocyclus gelatinosus
Author(s) -
Richaud P.,
Vignais P.M.,
Colbeau A.,
Uffen R.L.,
Cauvin B.
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb04946.x
Subject(s) - hydrogenase , operon , rhodobacter , biochemistry , bacteria , structural gene , biology , open reading frame , gene , azotobacter chroococcum , nitrogenase , protein subunit , bradyrhizobium japonicum , enzyme , peptide sequence , genetics , nitrogen fixation , escherichia coli , rhizobiaceae , symbiosis , mutant
In the photosynthetic bacteria, as in other N 2 ‐fixing bacteria, two main enzymes are involved in H 2 metabolism: nitrogenase, which catalyses the photoproduction of H 2 , and a membrane‐bound (NiFe) hydrogenase, which functions as an H 2 ‐uptake enzyme. The structural genes for Rhodobacter capsulatus and Rhodocyclus gelatinosus uptake hydrogenases were isolated and sequenced. They present the same organization, with the gene encoding the small subunit ( hupS ) (molecular masses 34.2 and 34.6 kDa, respectively) preceding the gene encoding the large one ( hupL ) (molecular masses 65.8 and 68.5 kDa, respectively). The two hupSL genes apparently belong to the same operon. The deduced protein sequences of the small and of the large subunits share nearly 80% and maximally 70% identity, respectively, with their counterparts in uptake hydrogenases found in N 2 ‐fixing bacteria. However, unlike in Bradyrhizobium japonicum, R. gelatinosus or Azotobacter chroococcum , another open reading frame (ORFX) was found downstream and contiguous to the R. capsulatus hupSL whose transcription seemed to depend on the same hup promoter as hupSL . ORFX contained 786 nucleotides capable of encoding a hydrophobic polypeptide of 262 amino acids (30.2 kDa).