Regulation of Nitrogen Fixation in
            <i>Klebsiella pneumoniae</i>
            : Evidence for a Role of Glutamine Synthetase as a Regulator of Nitrogenase Synthesis

Streicher, Stanley L.; Shanmugam, K. T.; Ausubel, Frederick M.; Morandi, Carlo; Goldberg, Robert P.

doi:10.1128/jb.120.2.815-821.1974

Cited by 198 publications

(83 citation statements)

References 12 publications

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“…On examining possible ways in which glutamine synthetase regulates the synthesis of nitrogenase in Anabaena two factors may be noted. First, catalytically active glutamine synthetase does not appear to act as a positive control factor in switching on nitrogenase directly as proposed by Streicher et al (1974) ioi Klebsiella, since we have evidence hom Anabaena (Stewart and Rowell, 1975) and from symbiotic Nostoc cells (Stewart and Rowell, 1977) that nitrogenase activity remains high when glutamine synthetase activity is low or undetectable. Second, the most consistent correlations which we obtained between nitrogenase activity and various other parameters (Table 1) were inverse ones between nitrogenase activity and the intracellular pools of glutamine and of aspartate.…”

Section: Discussionmentioning

confidence: 77%

“…This alga shows low glutamate dehydrogenase activity even in ammonium-grown cultures (Stewart, Haystead and Dharmawardene, 1975) and alanine dehydrogenase, although active, is unlikely to be the primary route of ammonia-assimilation under nitrogen-fixing conditions (Rowell and Stewart, 1976). There is also evidence that in nitrogen-fixing heterotrophic bacteria, particularly Klebsiella pneumoniae, glutamine synthetase is involved in the regulation of nitrogenase synthesis, but exactly how is uncertain (see Streicher et al, 1974;Tubb, 1974;Shanmugam, Chan and Morandi, 1975;Shanmugam and Morandi, 1976). Here we consider the ways in which the glutamine synthetase of Anabaena cylindrica is regulated and examine the relationship in this alga between nitrogenase activity and glutamine synthetase activity.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

GLUTAMINE SYNTHETASE AND NITROGENASE ACTIVITY IN THE BLUE‐GREEN ALGA ANABAENA CYLINDRICA

Rowell¹,

Enticott²,

Stewart³

1977

New Phytologist

112

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Summary On adding NH4+ to nitrogen‐fixing cultures of Anabaena cylindrica, the glutamine pool of the intact filament increases within seconds. Nitrogenase activity and then glutamine synthetase activity decline. There are no changes in the activities of glutamate‐aspartate aminotrans‐ferase, or in the pools of alanine, glycine and aspartate during this period. Nitrogenase activity is usually inversely related to the size of the glutamine pool and shows little correlation with glutamine synthetase activity per se. There is no evidence of adenylylation or dead‐enylylation of glutamine synthetase (snake venom phosphodiesterase has no effect on activity, there is no serological homogeneity with the Escherichia coli enzyme which shows a covalent modification; the ratio of biosynthetic: transferase activity does not change markedly on the addition of NH4+ and the kinetics of decrease in glutamine synthetase activity are not consistent with adenylylation of the enzyme). Feed‐back inhibition occurs, with alanine and glycine being particularly effective inhibitors and with some inhibition occurring with AMP, carbamoyl phosphate and aspartate. Histidine, lysine, ornithine, citrulline and arginine were non‐inhibitory at the concentrations used. There is no evidence of inhibition of glutamine synthetase by glutamine. The addition of azaserine inhibits glutamine uptake by intact filaments and reduces the subsequent conversion of glutamine to glutamate within the filament by 77%. Such results are consistent with the operation of the glutamine synthetase‐glutamate synthase pathway in Anabaena cylindrica.

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Section: Discussionmentioning

confidence: 77%

Section: Introductionmentioning

confidence: 99%

GLUTAMINE SYNTHETASE AND NITROGENASE ACTIVITY IN THE BLUE‐GREEN ALGA ANABAENA CYLINDRICA

Rowell¹,

Enticott²,

Stewart³

1977

New Phytologist

112

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“…The first indication that the ntr system may also regulate synthesis of the NH~ carrier stems from the observation that a regulatory mutant of K. pneumoniae (strain KP5060 [59]) was unable to transport MA [35]. This mutant had been characterized before as defective in glutamine synthetase (Gin-), nitrogenase (Nif-) and histidine utilization (Hut).…”

Section: Regulation Of Carrier Synthesismentioning

confidence: 99%

Bacterial ammonium transport

Kleiner

1985

FEMS Microbiology Letters

259

175

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“…The exact mechanism of the protease repression remains to be elucidated. Recently, a novel control mechanism, the "glutamine synthetase-mediated" repression, was described for microbial enzymes responsible for the utilization of nitrogen sources (13,25). The enzyme synthesis subject to this control is characteristically repressed by NH4+.…”

Section: Discussionmentioning

confidence: 99%

Catabolite‐Like Repression of Extracellular Enzyme Production in Vibrio parahaemolyticus

Iuchi

Tanaka

1980

Microbiology and Immunology

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Production of extracellular amylase and protease in Vibrio parahaemolyticus was repressed by various carbohydrates present in the medium. In addition, the protease production was repressed very strongly by peptones or casamino acids. Cyclic adenosine 3', 5'-monophosphate (cyclic AMP) added exogenously could reverse the repression of amylase production, but not that of protease production irrespective of the "repressors" used. Mutants of V. parahaemolyticus, which resembled the reported cya (adenylate cyclase) and crp (cyclic AMP receptor protein) mutants of Escherichia coli and related organisms, were examined for the exoenzyme production. Amylase production in the mutants was defective, while their protease production was not defective, but rather accentuated as compared with that in the parental strain.These findings strongly suggest that amylase production is subject to catabolite repression mediated by cyclic AMP, whereas protease production is controlled by a repression mechanism which mimics in part, but may be distinct from catabolite repression.Many studies on the regulation of extracellular enzyme (exoenzyme) production in bacteria have been reported. Some of them including ours (27) were reviewed recently (6, 18). Exoenzyme production, whether it is constitutive or inducible, is generally subject to the catabolite or at least "catabolite-like" repression, i.e. the repression effected by various carbon and energy sources in the medium. It has been established (17) that catabolite repression in Escherichia coli and related organisms is mediated by cyclic adenosine 3', 5'-monophosphate (cyclic AMP; cAMP), which, in combination with cAMP receptor protein (CRP), positively controls the synthesis of various catabolite-repressible enzymes. The synthesis of such enzymes are, therefore, impaired in mutants lacking either adenylate cyclase [EC 4.6.1.1] (cya) or CRP (crp).Nevertheless, the question whether the "catabolite-like" repression of exoenzyme production is also mediated by cAMP still remains to be settled. We described previously (9) mutants of Vibrio parahaemolyticus which resembled the reported cya and crp mutants of other organisms (17). Since V. parahaemolyticus produces some

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Regulation of Nitrogen Fixation in Klebsiella pneumoniae : Evidence for a Role of Glutamine Synthetase as a Regulator of Nitrogenase Synthesis

Cited by 198 publications

References 12 publications

GLUTAMINE SYNTHETASE AND NITROGENASE ACTIVITY IN THE BLUE‐GREEN ALGA ANABAENA CYLINDRICA

GLUTAMINE SYNTHETASE AND NITROGENASE ACTIVITY IN THE BLUE‐GREEN ALGA ANABAENA CYLINDRICA

Bacterial ammonium transport

Catabolite‐Like Repression of Extracellular Enzyme Production in Vibrio parahaemolyticus

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