Abstract:
:Expression of the dimethylsulfoxide respiratory (dor) operon of Rhodobacter is regulated by oxygen, light intensity and availability of substrate. Since dimethylsulfoxide reductase contains a pterin molybdenum cofactor, the role of molybdate in the regulation of dor operon expression was investigated. In this report we show that the molybdate-responsive transcriptional regulator, MopB, and molybdate are essential for maximal dimethylsulfoxide reductase activity and expression of a dorA::lacZ transcriptional fusion in Rhodobacter capsulatus. In contrast, mop genes are not required for the expression of the periplasmic nitrate reductase or xanthine dehydrogenase in R. capsulatus under conditions of molybdenum sufficiency. This is the first report demonstrating a clear functional difference between the ModE homologues MopB and MopA in this bacterium. The results suggest that MopA is primarily involved in the regulation of nitrogen fixation gene expression in response to molybdate while MopB has a role in nitrogen fixation and dimethylsulfoxide respiration.
journal_name
FEMS Microbiol Lettjournal_title
FEMS microbiology lettersauthors
Solomon PS,Shaw AL,Young MD,Leimkuhler S,Hanson GR,Klipp W,McEwan AGdoi
10.1111/j.1574-6968.2000.tb09287.xkeywords:
subject
Has Abstractpub_date
2000-09-15 00:00:00pages
203-8issue
2eissn
0378-1097issn
1574-6968pii
S0378-1097(00)00336-0journal_volume
190pub_type
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journal_title:FEMS microbiology letters
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