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Activity patterns of aminoacyl-tRNA synthetases, tRNA methylases, arginyltransferase and tubulin: tyrosine ligase during development and ageing of Caenorhabditis elegans.
Eur J Biochem ; 131(1): 231-4, 1983 Mar 01.
Article in En | MEDLINE | ID: mdl-6832143
ABSTRACT
As a step in the characterization of development and ageing in the nematode Caenorhabditis elegans, the activities of different groups of enzymes that supposedly exert modulating functions in and after protein synthesis have been determined. From embryonic (E), the four juvenile larval stages (L1-L4) and the gravid adult (A,A+), the selection of defined developmental stages extends to two different preparations of aged nematodes (S10, S12). Some aminoacyl-tRNA synthetase activities remain nearly unchanged in all stages up to the adult, some increase continuously during the larval stages and the remaining activities show stage-specific alterations. Upon ageing all activities except the one for tryptophan decrease sharply, tRNA methylase activities increase from E to L4, decrease from L4 to adult and to aged nematodes with only qualitative alterations in substrate specificity. The activity of tubulin tyrosine ligase exhibits a parallel pattern, while arginyltransferase activity has a plateau between L2 and L4. The results are consistent with the idea of a modulation of protein synthesis and other cellular processes by quantitative activity changes during development and ageing.
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Collection: 01-internacional Database: MEDLINE Main subject: Peptide Synthases / TRNA Methyltransferases / Caenorhabditis / Acyltransferases / Aminoacyltransferases / Amino Acyl-tRNA Synthetases Type of study: Qualitative_research Limits: Animals Language: En Journal: Eur J Biochem Year: 1983 Document type: Article
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Collection: 01-internacional Database: MEDLINE Main subject: Peptide Synthases / TRNA Methyltransferases / Caenorhabditis / Acyltransferases / Aminoacyltransferases / Amino Acyl-tRNA Synthetases Type of study: Qualitative_research Limits: Animals Language: En Journal: Eur J Biochem Year: 1983 Document type: Article