Effect of AmtB homologues on the post-translational regulation of nitrogenase activity in response to ammonium and energy signals in Rhodospirillum rubrum.
The AmtB protein transports uncharged NH(3) into the cell, but it also interacts with the nitrogen regulatory protein P(II), which in turn regulates a variety of proteins involved in nitrogen fixation and utilization. Three P(II) homologues, GlnB, GlnK and GlnJ, have been identified in the photosynthetic bacterium Rhodospirillum rubrum, and they have roles in at least four overlapping and distinct functions, one of which is the post-translational regulation of nitrogenase activity. In R. rubrum, nitrogenase activity is tightly regulated in response to addition or energy depletion (shift to darkness), and this regulation is catalysed by the post-translational regulatory system encoded by draTG. Two amtB homologues, amtB(1) and amtB(2), have been identified in R. rubrum, and they are linked with glnJ and glnK, respectively. Mutants lacking AmtB(1) are defective in their response to both addition and darkness, while mutants lacking AmtB(2) show little effect on the regulation of nitrogenase activity. These responses to darkness and appear to involve different signal transduction pathways, and the poor response to darkness does not seem to be an indirect result of perturbation of internal pools of nitrogen. It is also shown that AmtB(1) is necessary to sequester detectable amounts GlnJ to the cell membrane. These results suggest that some element of the AmtB(1)-P(II) regulatory system senses energy deprivation and a consistent model for the integration of nitrogen, carbon and energy signals by P(II) is proposed. Other results demonstrate a degree of specificity in interaction of AmtB(1) with the different P(II) homologues in R. rubrum. Such interaction specificity might be important in explaining the way in which P(II) proteins regulate processes involved in nitrogen acquisition and utilization.
Zhang
Yaoping
Y
Department of Bacteriology and the Center for the Study of Nitrogen Fixation, University of Wisconsin-Madison, Madison, WI 53706, USA.
Wolfe
David M
DM
Department of Bacteriology and the Center for the Study of Nitrogen Fixation, University of Wisconsin-Madison, Madison, WI 53706, USA.
Pohlmann
Edward L
EL
Department of Bacteriology and the Center for the Study of Nitrogen Fixation, University of Wisconsin-Madison, Madison, WI 53706, USA.
Conrad
Mary C
MC
Department of Bacteriology and the Center for the Study of Nitrogen Fixation, University of Wisconsin-Madison, Madison, WI 53706, USA.
Roberts
Gary P
GP
Department of Bacteriology and the Center for the Study of Nitrogen Fixation, University of Wisconsin-Madison, Madison, WI 53706, USA.
D036002:ADP Ribose Transferases / Q000502:physiology; D000255:Adenosine Triphosphate / Q000502:physiology; D001426:Bacterial Proteins / Q000502:physiology*; D027682:Cation Transport Proteins / Q000502:physiology*; D005973:Glutamine / Q000378:metabolism; D008717:Methionine Sulfoximine / Q000494:pharmacology; D009591:Nitrogenase / Q000378:metabolism*; D051922:PII Nitrogen Regulatory Proteins / Q000502:physiology; D011499:Protein Processing, Post-Translational; D000644:Quaternary Ammonium Compounds / Q000494:pharmacology*; D012247:Rhodospirillum rubrum / Q000201:enzymology*
D001426:Bacterial Proteins; D027682:Cation Transport Proteins; C439048:GlnJ protein, Rhodospirillum rubrum; D051922:PII Nitrogen Regulatory Proteins; D000644:Quaternary Ammonium Compounds; D005973:Glutamine; D008717:Methionine Sulfoximine; C404143:PIID regulatory protein, Bacteria; D000255:Adenosine Triphosphate; D009591:Nitrogenase; D036002:ADP Ribose Transferases; C057637:dinitrogenase reductase ADP-ribosyltransferase