The effect of hemin, adenosine 3',5'-monophosphate and phosphorylated sugars on Met-tRNAfMet deacylase activity in rabbit reticulocyte lysates.
The effect of hemin, phosphorylated sugars, adenosine 3',5'-monophosphate (cyclic AMP) and a number of purines on a specific initiator tRNA deacylase activity in rabbit reticulocytes has been investigated. In the concentration range established to be optimal for maximal stimulation of translation (5.5-30.0 microM), hemin produces a 20-82% inhibition of Met-tRNAfMet deacylation. In contrast, all phosphorylated sugars tested, with the exception of fructose 1,6-diphosphate, are without effect. High concentrations of cyclic AMP (2-4 mM) also significantly inhibit the deacylase activity. The role of hemin and Met-tRNAfMet deacylase in the control of peptide initiation are discussed.
D000217:Acyltransferases / Q000037:antagonists & inhibitors* / Q000097:blood; D019881:Aminoacyltransferases; D000818:Animals; D000242:Cyclic AMP / Q000494:pharmacology*; D005635:Fructosediphosphates / Q000494:pharmacology; D006418:Heme / Q000031:analogs & derivatives*; D006427:Hemin / Q000494:pharmacology*; D066298:In Vitro Techniques; D009239:N-Formylmethionine / Q000037:antagonists & inhibitors / Q000097:blood; D009711:Nucleotides / Q000494:pharmacology; D010442:Peptide Chain Initiation, Translational / Q000187:drug effects; D014176:Protein Biosynthesis / Q000187:drug effects; D012346:RNA, Transfer, Amino Acyl / Q000037:antagonists & inhibitors / Q000097:blood; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism; D013403:Sugar Phosphates / Q000494:pharmacology*
D005635:Fructosediphosphates; D009711:Nucleotides; D012346:RNA, Transfer, Amino Acyl; D013403:Sugar Phosphates; D009239:N-Formylmethionine; D006418:Heme; D006427:Hemin; D000242:Cyclic AMP; D000217:Acyltransferases; D019881:Aminoacyltransferases; C021560:methionyl-tRNA-Met-f deacylase