Literature DB >> 6390179

[How do ribosome binding sites recognize the functional state of tRNA?].

E M Makarov, V I Katunin, V B Odintsov, Iu P Semenkov, S V Kirillov.   

Abstract

The order of relative affinity of three different functional form of tRNA (aminoacyl-tRNA, peptidyl-tRNA and deacylated tRNAOH) was established for three sites of the ribosome. The affinity increases for A-site in consecutive order: tRNAOH less than AcPhe-tRNA less than aa-tRNA; for P-site with messenger RNA: AcPhe-tRNA less than aa-tRNA less than tRNAOH; without messenger RNA: aa-tRNA less than AcPhe-tRNA less than tRNAOH; for E-site: (AcPhe-tRNA, aa-tRNA) much less than much less than tRNAOH. The dependence of association constants versus magnesium concentration for all forms of tRNA conforms the equation: delta lg Ka/delta lg[Mg2+] = n. Number "n" varies in the range 1 to 8 depending on the site of adsorption the form of tRNA and the presence of mRNA. Such magnesium dependence of affinity of tRNAs shows that the electrostatic interactions play an important role in the recognition of functional forms of tRNA by ribosomal sites.

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Year:  1984        PMID: 6390179

Source DB:  PubMed          Journal:  Mol Biol (Mosk)        ISSN: 0026-8984


  1 in total

1.  The process of mRNA-tRNA translocation.

Authors:  Joachim Frank; Haixiao Gao; Jayati Sengupta; Ning Gao; Derek J Taylor
Journal:  Proc Natl Acad Sci U S A       Date:  2007-11-14       Impact factor: 11.205

  1 in total

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