Open AccessTwo different genes and gene products for the large subunit of ribulose‐1,5‐bisphosphate carboxylase/oxygenase (RuBisCOase) in Nitrobacter hamburgensis
Author(s) -
Harris Stephanie,
Ebert Axel,
Schütze Eva,
Diercks Maren,
Bock E.,
Shively J.M.
Publication year - 1988
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.1574-6968.1988.tb02728.x
Subject(s) - ribulose 1,5 bisphosphate , biology , oxygenase , ribulose , biochemistry , plasmid , microbiology and biotechnology , gene , protein subunit , enzyme , phycobiliprotein , rhodobacter , gel electrophoresis , pyruvate carboxylase , restriction enzyme , specificity factor , rubisco , genetics , promoter , bacteria , cyanobacteria , gene expression , mutant
Heterologous DNA hybridization using a ribulose‐ 1,5‐biphosphate carboxylase/oxygenase (RuBisCOase) large subunit gene ( rbc L) probe from Anacystis nidulans revealed the presence of two rbc L in Nitrobacter hamburgensis . One gene is located on a plasmid, the other on the chromosome. The genes appear to be very similar since both hybridized strongly to the A. nidulans probe. However, restriction endonuclease digestions revealed differences. Two different RuBisCOase enzymes were isolated from N. hamburgensis. The M r of the native enzymes were 520 000 and 480 000. Sodium dodecyl sulfate‐polycrylamide gel electrophoresis (SDS‐PAGE) revealed the presence of both LSU and small subunits (SSU) for both enzymes. The M r were 53 000 and 16 000, and 49 000 and 13 500, respectively. A hexadecameric structure is suggested for both enzymes.