Comparison of Nitrogenase Regulation in A. Brasilense, A. Lipoferum, and A. Amazonense

1985 ◽  
pp. 116-126 ◽  
Author(s):  
A. Hartmann ◽  
H.-A. Fu ◽  
S.-D. Song ◽  
R. H. Burris
Keyword(s):  
Nitrogenase Regulation

Cyanobacterial ammonium transport, ammonium assimilation, and nitrogenase regulation

1987 ◽  
Vol 21 (3) ◽  
pp. 447-455 ◽  
Author(s):  
Nigel W. Kerby ◽  
Peter Rowell ◽  
William D. P. Stewart
Keyword(s):  
Ammonium Assimilation ◽  
Ammonium Transport ◽  
Nitrogenase Regulation

scholarly journals Lars Hällbom; Nitrogenase regulation and ultrastructure of heterocystous cyanobacteria; free living and in lichen symbiosis.

Rangifer ◽  
1982 ◽  
Vol 2 (1) ◽  
pp. 52
Author(s):  
Sven Skjenneberg
Keyword(s):  
Font Size ◽  
Free Living ◽  
Heterocystous Cyanobacteria ◽  
Nitrogenase Regulation ◽  
Lichen Symbiosis

<span style="font-family: Arial Unicode MS,Arial Unicode MS; font-size: xx-small;"><span style="font-family: Arial Unicode MS,Arial Unicode MS; font-size: xx-small;"><p align="justify">Doktoravhandling forsvart i Botanisk auditorium, Uppsala Universitet 19. mai 1982. (Inst. for fysiologisk botanik, Uppsala Universitet).</p></span></span>

scholarly journals Ammonia-Induced Formation of an AmtB-GlnK Complex Is Not Sufficient for Nitrogenase Regulation in the Photosynthetic Bacterium Rhodobacter capsulatus

2007 ◽  
Vol 190 (5) ◽  
pp. 1588-1594 ◽  
Author(s):  
Pier-Luc Tremblay ◽  
Patrick C. Hallenbeck
Keyword(s):  
Rhodobacter Capsulatus ◽  
Mutational Analysis ◽  
Nitrogenase Activity ◽  
Photosynthetic Bacterium ◽  
The Other ◽  
Amino Acid Residues ◽  
Adp Ribosylation ◽  
Nitrogenase Regulation ◽  
Ammonia Transport ◽  
First Time

ABSTRACT A series of Rhodobacter capsulatus AmtB variants were created and assessed for effects on ammonia transport, formation of AmtB-GlnK complexes, and regulation of nitrogenase activity and NifH ADP-ribosylation. Confirming previous reports, H193 and H342 were essential for ammonia transport and the replacement of aspartate 185 with glutamate reduced ammonia transport. Several amino acid residues, F131, D334, and D335, predicted to be critical for AmtB activity, are shown here for the first time by mutational analysis to be essential for transport. Alterations of the C-terminal tail reduced methylamine transport, prevented AmtB-GlnK complex formation, and abolished nitrogenase switch-off and NifH ADP-ribosylation. On the other hand, D185E, with a reduced level of transport, was capable of forming an ammonium-induced complex with GlnK and regulating nitrogenase. This reinforces the notions that ammonia transport is not sufficient for nitrogenase regulation and that formation of an AmtB-GlnK complex is necessary for these processes. However, some transport-incompetent AmtB variants, i.e., F131A, H193A, and H342A, form ammonium-induced complexes with GlnK but fail to properly regulate nitrogenase. These results show that formation of an AmtB-GlnK complex is insufficient in itself for nitrogenase regulation and suggest that partial ammonia transport or occupation of the pore by ammonia is essential for this function.

scholarly journals In Vivo Nitrogenase Regulation by Ammonium and Methylamine and the Effect of MSX on Ammonium Transport in Anabaena flos-aquae

1984 ◽  
Vol 74 (3) ◽  
pp. 701-704 ◽  
Author(s):  
David H. Turpin ◽  
Scott A. Edie ◽  
David T. Canvin
Keyword(s):  
Ammonium Transport ◽  
Nitrogenase Regulation

scholarly journals NH4+ ASSIMILATION AND NITROGENASE REGULATION IN THE LICHEN PELTIGERA APHTHOSA WILLD

1980 ◽  
Vol 85 (4) ◽  
pp. 545-555 ◽  
Author(s):  
A. N. RAI ◽  
P. ROWELL ◽  
W. D. P. STEWART
Keyword(s):  
Nitrogenase Regulation

Involvement of the ammonium transporter AmtB in nitrogenase regulation and ammonium excretion in Pseudomonas stutzeri A1501

2012 ◽  
Vol 163 (5) ◽  
pp. 332-339 ◽  
Author(s):  
Tao Zhang ◽  
Yongliang Yan ◽  
Sheng He ◽  
Shuzhen Ping ◽  
Khandakar Mohiul Alam ◽  
...  
Keyword(s):  
Pseudomonas Stutzeri ◽  
Ammonium Transporter ◽  
Ammonium Excretion ◽  
Nitrogenase Regulation

scholarly journals Comparing Short-Term Effects of Ammonia and Methylamine on Nitrogenase Activity in Anabaena variabilis (ATCC 29413)

1987 ◽  
Vol 42 (7-8) ◽  
pp. 902-906 ◽  
Author(s):  
Sabine Reich ◽  
Helmar Almon ◽  
Peter Böger
Keyword(s):  
Protein Synthesis ◽  
Light Intensity ◽  
Nitrogenase Activity ◽  
Anabaena Variabilis ◽  
Short Term ◽  
Heterocystous Cyanobacterium ◽  
Nitrogenase Regulation ◽  
Methyl Amine ◽  
Cyanobacterium Anabaena ◽  
Nitrogenase Inhibition

Cyanobacterium . Anabaena variabilis, Nitrogenase Regulation, Ammonia, Methylamine Using the heterocystous cyanobacterium A nabaena variabilis (ATCC 29413) in an alkaline environment its nitrogenase activity is rapidly inhibited by ammonia and methylamine. Nitro­genase inhibition by ammonia is probably caused by a mechanism comparable to the switch-off effect, which has been described for several species of the Rhodospirillaceae, whereas methyl-amine-induced inhibition is caused by an uncoupling effect only. Evidence for these different effects is obtained by comparing nitrogenase activity in cell-free extracts of filaments pretreated by ammonia or methylamine. In addition, ammonia-dependent nitrogenase inhibition is shown to be dependent on protein synthesis and on light intensity.

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