In vitro proof of direct regulation of glutamine synthetase by GlnK proteins in the extreme halophilic archaeon Haloferax mediterranei

2011 ◽  
Vol 39 (1) ◽  
pp. 259-262 ◽  
Author(s):  
Laia Pedro-Roig ◽  
Mónica Camacho ◽  
María José Bonete

Haloferax mediterranei is an extreme halophilic micro-organism belonging to the Archaea domain that was isolated from the Santa Pola solar salterns (Alicante, Spain) in 1983. The biochemistry of the proteins involved in nitrogen metabolism is being studied, but the knowledge of their regulation is very scarce at present. The PII superfamily is constituted by major regulators of nitrogen metabolism, which are widespread in prokaryotic and eukaryotic organisms. These trimeric proteins (12 kDa per subunit) have in Escherichia coli long been known to regulate GS (glutamine synthetase) activity via its adenylyltransferase/adenylyl-removing enzyme and, more recently, to be able to interact directly with this enzyme in methanogenic archaea. We have tested the possible role of PII proteins in the regulation of ammonium assimilation in our model organism and the results clearly indicate that the direct influence of GS by PII proteins can also take place in halophilic archaea, starting with the comprehension of nitrogen regulation in those organisms.

2003 ◽  
Vol 133 (1) ◽  
pp. 253-262 ◽  
Author(s):  
Judith Harrison ◽  
Marie-Anne Pou de Crescenzo ◽  
Olivier Sené ◽  
Bertrand Hirel

2009 ◽  
Vol 192 (5) ◽  
pp. 1463-1466 ◽  
Author(s):  
Pedro Filipe Teixeira ◽  
He Wang ◽  
Stefan Nordlund

ABSTRACT Nitrogen fixation and ammonium assimilation in Rhodospirillum rubrum are regulated in response to changes in light availability, and we show that the response in terms of glutamine synthetase activity and PII modification is dependent on the nitrogen source used for growth, N2 or glutamate, although both lead to nitrogenase derepression.


1970 ◽  
Vol 119 (2) ◽  
pp. 145-156 ◽  
Author(s):  
Khalid Iqbal ◽  
J. H. Ottaway

1. Glutamine synthetase activity has been determined in extracts of rat cardiac and skeletal muscle and kidney, after treatment to ensure that the rate of synthesis was proportional to time of incubation and to amount of extract added. The activity was measured by two methods, with hydroxylamine as substrate. 2. No activity was detected in rat heart extract by either method. The activity in skeletal muscle was of the order of 20μmol of glutamylhydroxamate synthesized/h per g of tissue under optimum conditions. The activity in kidney extracts was 180μmol/h per g of tissue when measured as ferric hydroxamate. 3. The activity in both skeletal-muscle and kidney extracts was inhibited by Pi. The inhibition is competitive for the muscle enzyme, with a Ki of 12mm. For the kidney enzyme the inhibition is non-competitive, and less marked. Possible enzyme mechanisms that would lead to these types of inhibition are discussed. 4. Several observations are reported that suggest that the enzymes from muscle and kidney are not identical. 5. Growth hormone, either in vivo or in vitro, did not affect the measured glutamine synthetase activity of tissue extracts.


Sign in / Sign up

Export Citation Format

Share Document