Yeast proteinase yscB inactivates the leucyl tRNA synthetase in extracts of Saccharomyces cerevisiae.
The aminoacyl-tRNA synthetases are inactivated in extracts of Saccharomyces cerevisiae preferentially to other yeast enzymes and the rate of inactivation greatly increases in extracts of nitrogen-starved cells. The intensity of inactivation varies for the different synthetases. Under conditions in which more than 80 per cent of the leucyl and isoleucyl-tRNA synthetases are inactivated, the activities of the synthetases for serine and arginine remain unchanged and the synthetases for other amino acids are inactivated to different extents. We have analyzed the characteristics of inactivation of the leucyl-tRNA synthetase, and identified the inactivating agent as the yeast proteinase yscB by the following criteria: co-induction of both activities by nitrogen starvation; same pattern of sensitivity to yeast proteinase inhibitors; co-purification through a procedure designed to purify the proteinase yscB and lack of inactivating activity in extracts of a nitrogen-starved yeast mutant lacking proteinase yscB.
Larrinoa
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IF
Instituto de Investigaciones Biomédicas del CSIC, Facultad de Medicina de la UAM, Madrid, Spain.
Heredia
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CF
D007935:Leucine-tRNA Ligase / Q000037:antagonists & inhibitors / Q000378:metabolism*; D009154:Mutation; D009584:Nitrogen / Q000502:physiology; D011480:Protease Inhibitors / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins
D007935:Leucine-tRNA Ligase; D009584:Nitrogen; D011480:Protease Inhibitors; D012697:Serine Endopeptidases; C023302:yeast proteinase B; D029701:Saccharomyces cerevisiae Proteins