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- W2169571454 abstract "ABSTRACT The photosynthetic bacterium Rhodobacter capsulatus has been shown to regulate its nitrogenase by covalent modification via the reversible ADP-ribosylation of Fe protein in response to darkness or the addition of external NH 4 + . Here we demonstrate the presence of ADP-ribosylated Fe protein under a variety of steady-state growth conditions. We examined the modification of Fe protein and nitrogenase activity under three different growth conditions that establish different levels of cellular nitrogen: batch growth with limiting NH 4 + , where the nitrogen status is externally controlled; batch growth on relatively poor nitrogen sources, where the nitrogen status is internally controlled by assimilatory processes; and continuous culture. When cultures were grown to stationary phase with different limiting concentrations of NH 4 + , the ADP-ribosylation state of Fe protein was found to correlate with cellular nitrogen status. Additionally, actively growing cultures (grown with N 2 or glutamate), which had an intermediate cellular nitrogen status, contained a portion of their Fe protein in the modified state. The correlation between cellular nitrogen status and ADP-ribosylation state was corroborated with continuous cultures grown under various degrees of nitrogen limitation. These results show that in R. capsulatus the modification system that ADP-ribosylates nitrogenase in the short term in response to abrupt changes in the environment is also capable of modifying nitrogenase in accordance with long-term cellular conditions." @default.
- W2169571454 created "2016-06-24" @default.
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- W2169571454 date "1999-04-01" @default.
- W2169571454 modified "2023-10-17" @default.
- W2169571454 title "The Presence of ADP-Ribosylated Fe Protein of Nitrogenase in <i>Rhodobacter capsulatus</i> Is Correlated with Cellular Nitrogen Status" @default.
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- W2169571454 doi "https://doi.org/10.1128/jb.181.7.1994-2000.1999" @default.
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