Regulation of the Aminoacyl‐tRNA Synthetase Complex of Rat Liver by Phosphorylation/Dephosphorylation in vitro and in vivo
10.1111/j.1432-1033.1982.tb07020.x
Crossref journal-article
Wiley
European Journal of Biochemistry (311)
Abstract

Incubation of liver extracts with MgATP led to complete inactivation of the aminoacyl‐tRNA synthetase complex provided that sodium fluoride was included. If sodium fluoride was omitted no inactivation was observed. The arginyl‐tRNA and isoleucyl‐tRNA synthetases were inactivated more slowly than the leucyl‐tRNA, lysyl‐tRNA and methionyl‐tRNA synthetases. Gel filtration on Sepharose 4B separated the aminoacyl‐tRNA synthetase complex (Ve/Vo= 1.2) from an inactivating factor that required MgATP (Ve/Vo= 2.8).The inactivated aminoacyl‐tRNA synthetase complex was eluted from Sepharose‐4B at the same position as the activated complex, and was resolved from a reactivating factor that required Mg2+ and was inhibited by sodium fluoride (Ve/Vo= 2.5). The arginyi‐tRNA and isoleucyl‐tRNA synthetases were reactivated more rapidly than the leucyl‐tRNA, lysyl‐tRNA and methionyl‐tRNA synthetases.The aminoacyl‐tRNA synthetase complex could also be reactivated using highly purified preparations of either protein phosphatase 1 or protein phosphatase 2A. Inhibitor 2, a specific inhibitor of protein phosphatase 1, prevented reactivation of the complex by protein phosphatase 1, but not by protein phosphatase 2A. The relative rates of reactivation of the different activities of the complex by either protein phosphatase 1 or protein phosphatase 2A were very similar to those observed with the reactivating factor.The aminoacyl‐tRNA synthetase complex was largely in the activated state in livers of normally fed rats, but overnight starvation produced substantial conversion to the inactivated form of the complex. Incubation of hepatocytes from normally fed rats with glucagon and isobutylmethylxanthine for 20 min also caused a substantial decrease in the activation state from approximately 80% to approximately 30%. Conversely, when hepatocytes prepared from starved rats were incubated with insulin for 30 min, almost complete reactivation of the complex was achieved.The results indicate that the aminoacyl‐tRNA synthetase complex is regulated by a phosphorylation dephosphorylation mechanism in vitro and in vivo. The effects of hormones on the activation state of the complex are discussed in the light of the observation that the inactivating factor is not cyclic‐AMP‐dependent protein kinase.

Bibliography

DAMUNI, Z., CAUDWELL, F. B., & COHEN, P. (1982). Regulation of the Aminoacyl‐tRNA Synthetase Complex of Rat Liver by Phosphorylation/Dephosphorylation in vitro and in vivo. European Journal of Biochemistry, 129(1), 57–65. Portico.

Authors 3
  1. Zahi DAMUNI (first)
  2. F. Barry CAUDWELL (additional)
  3. Philip COHEN (additional)
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Dates
Type When
Created 20 years, 5 months ago (March 3, 2005, 5:20 p.m.)
Deposited 1 year, 9 months ago (Nov. 22, 2023, 8:08 p.m.)
Indexed 4 months, 4 weeks ago (April 3, 2025, 8:34 p.m.)
Issued 42 years, 9 months ago (Dec. 1, 1982)
Published 42 years, 9 months ago (Dec. 1, 1982)
Published Online 20 years, 5 months ago (March 3, 2005)
Published Print 42 years, 9 months ago (Dec. 1, 1982)
Funders 0

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@article{DAMUNI_1982, title={Regulation of the Aminoacyl‐tRNA Synthetase Complex of Rat Liver by Phosphorylation/Dephosphorylation in vitro and in vivo}, volume={129}, ISSN={1432-1033}, url={http://dx.doi.org/10.1111/j.1432-1033.1982.tb07020.x}, DOI={10.1111/j.1432-1033.1982.tb07020.x}, number={1}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={DAMUNI, Zahi and CAUDWELL, F. Barry and COHEN, Philip}, year={1982}, month=dec, pages={57–65} }