Regulation of the mdh‐sucCDABoperon in Rhizobium leguminosarum
In: FEMS Microbiology Letters, Jg. 176 (1999-07-01), Heft 1, S. 247-255
Online
serialPeriodical
Zugriff:
The malate dehydrogenase gene, mdh, from Rhizobium leguminosarumencodes a protein with a molecular weight of 33 590 that associates as a homotetramer. It is a lactate dehydrogenase‐like malate dehydrogenase that most closely resembles the protein from the colonial green alga Botryococcus braunii. Malate dehydrogenase from R. leguminosarumhas a Kmof 74 μM and a Vmaxof 822 μmol min−1mg−1protein for oxaloacetate, while the Kmfor malate is 3.6 mM and the Vmax62 μmol min−1mg−1protein. Downstream of mdhare sucCDAB, which encode succinyl‐CoA synthetase (sucCD) and the E1 and E2 components of the α‐ketoglutarate dehydrogenase complex (sucAB). Complementation and LacZ fusion analysis indicates that there is a common promoter for the mdh‐sucgenes. Mutation of downstream genes in the mdh‐sucoperon increases transcription 7‐fold from the mdhpromoter. The transcriptional coupling of mdhand sucCDABis likely to be important in the regulation of carbon and nitrogen metabolism in bacteroids.
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Regulation of the mdh‐sucCDABoperon in Rhizobium leguminosarum
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Autor/in / Beteiligte Person: | Poole, Philip ; Reid, Colm ; East, Alison K. ; Allaway, David ; Day, Michael ; Leonard, Mary |
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Zeitschrift: | FEMS Microbiology Letters, Jg. 176 (1999-07-01), Heft 1, S. 247-255 |
Veröffentlichung: | 1999 |
Medientyp: | serialPeriodical |
ISSN: | 0378-1097 (print) ; 1574-6968 (print) |
DOI: | 10.1111/j.1574-6968.1999.tb13669.x |
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