Characteristics of the inhibition and metabolic inactivation of the yeast TRNA nucleotidyl transferase.
1. Yeast tRNA nucleotidyl transferase is inhibited by low molecular weight compounds present in cell-free extracts. The inhibition produced by the main component(s) is competitive with respect to ATP and is not prevented by metal chelating agents. The major component(s) has been partially purified. It is resistant to heat (90 degrees C, 5 min) and insensitive to digestion by alkaline phosphatase, snake venom phosphodiesterase and inorganic pyrophosphatase, indicating that it is not a nucleotide. 2. Besides the masking of the transferase activity in the crude extracts by the inhibitors, the enzyme is inactivated in nitrogen starved cells. The inactivation also occurs in yeast mutants lacking several proteases and is not prevented by inhibitors of yeast proteases. These results rule out extracellular proteolysis as the cause of inactivation and strength our previous observations on the metabolic inactivation of the transferase in response to nitrogen starvation.
Navarro
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MA
Instituto de Investigaciones Biomédicas del C.S.I.C. Facultad de Medicina, U.A.M., Madrid.
Heredia
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CF
D000255:Adenosine Triphosphate / Q000378:metabolism; D002474:Cell-Free System; D005656:Fungal Proteins / Q000037:antagonists & inhibitors*; D009584:Nitrogen / Q000378:metabolism; D012316:RNA Nucleotidyltransferases / Q000037:antagonists & inhibitors*; D012441:Saccharomyces cerevisiae / Q000201:enzymology*
D005656:Fungal Proteins; D000255:Adenosine Triphosphate; D012316:RNA Nucleotidyltransferases; C023198:tRNA nucleotidyltransferase; D009584:Nitrogen