Characterization of the cycHJKL genes involved in cytochrome c biogenesis and symbiotic nitrogen fixation in Rhizobium leguminosarum

Delgado, M.-J., Yeoman, K.H., Wu, G., Vargas, C., Davies, A.E., Poole, R.K., Johnston, Andy and Downie, J.A. (1995) Characterization of the cycHJKL genes involved in cytochrome c biogenesis and symbiotic nitrogen fixation in Rhizobium leguminosarum. Journal of Bacteriology, 177 (17). pp. 4927-4934. ISSN 0021-9193

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Abstract

Mutants of Rhizobium leguminosarum bv. viciae unable to respire via the cytochrome aa pathway were identified by the inability to oxidize N,N'- dimethyl-p-phenylenediamine. Two mutants which were complemented by cosmid pIJ1942 from an R. leguminosarum clone bank were identified. Although pea nodules induced by these mutants contained many bacteroids, no symbiotic nitrogen fixation was detected. Heme staining of cellular proteins revealed that all cytochrome c-type heme proteins were absent. These mutants lacked spectroscopically detectable cytochrome c, but cytochromes aa and d were present, the latter at a higher than-normal level. DNA sequence analysis of complementing plasmids revealed four apparently cotranscribed open reading frames (cycH, cycJ, cycK, and cycL). CycH, CycJ, CycK and CycL are homologous to Bradyrhizobium japonicum and Rhizobium meliloti proteins thought to be involved in the attachment of heme to cytochrome c apoproteins; CycK and CycL are also homologous to the Rhodobacter capsulatus cell and cd2 gene products and the Escherichia coli nrfE and nrfF gene products involved in the assembly of c-type cytochromes. The absence of cytochrome c heme proteins in these R. leguminosarum mutants is consistent with the view that the cycHJKL operon could be involved in the attachment of heme to apocytochrome c.

Item Type: Article
Faculty \ School:
Faculty of Science > School of Biological Sciences
UEA Research Groups: Faculty of Science > Research Groups > Molecular Microbiology
Faculty of Social Sciences > Research Groups > Research in Mathematics Education
Related URLs:
Depositing User: Pure Connector
Date Deposited: 26 Nov 2013 12:48
Last Modified: 02 Aug 2023 00:08
URI: https://ueaeprints.uea.ac.uk/id/eprint/44561
DOI: 10.1128/jb.177.17.4927-4934.1995

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