Literature DB >> 1004617

[Corrective steps in amino acid activation for protein biosynthesis].

F von der Haar.   

Abstract

Activation of aminoacids for proteinbiosynthesis is not absolutely specific. With tRNA modified at the 3' end we were able to show, that valine misactivated by isoleucyl-tRNA synthetase is transferred to tRNA(I1e). Val-tRNA(I1e) is then hydrolyzed by the enzyme prior to release of the wrong product. For this hydrolysis the nonaccepting 3'OH of the 3'-terminal ribose is essential. The role of the 3'OH is to activate a water molecule which, in the case of valine, is inserted into the place normally occupied by the methyl group of isoleucine. Hence hydrolysis is specific for misactivated valine while the correct substrate, isoleucine, is protected by its additional methyl group.

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Year:  1976        PMID: 1004617     DOI: 10.1007/bf00596848

Source DB:  PubMed          Journal:  Naturwissenschaften        ISSN: 0028-1042


  12 in total

1.  Aminoacyl-tRNA synthetases from baker's yeast: reacting site of enzymatic aminoacylation is not uniform for all tRNAs.

Authors:  F Cramer; H Faulhammer; F von der Haar; M Sprinzl; H Sternbach
Journal:  FEBS Lett       Date:  1975-08-15       Impact factor: 4.124

2.  Isoleucyl-tRNA synthetase from baker's yeast: the 3'-hydroxyl group of the 3'-terminal ribose is essential for preventing misacylation of tRNAIle-C-C-A with misactivated valine.

Authors:  F von der Haar; F Cramer
Journal:  FEBS Lett       Date:  1975-08-15       Impact factor: 4.124

3.  On the role of soluble ribonucleic acid in coding for amino acids.

Authors:  F CHAPEVILLE; F LIPMANN; G VON EHRENSTEIN; B WEISBLUM; W J RAY; S BENZER
Journal:  Proc Natl Acad Sci U S A       Date:  1962-06-15       Impact factor: 11.205

4.  Factors determining the specificity of the tRNA aminoacylation reaction. Non-absolute specificity of tRNA-aminoacyl-tRNA synthetase recognition and particular importance of the maximal velocity.

Authors:  J P Ebel; R Giegé; J Bonnet; D Kern; N Befort; C Bollack; F Fasiolo; J Gangloff; G Dirheimer
Journal:  Biochimie       Date:  1973-05       Impact factor: 4.079

5.  Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity.

Authors:  J J Hopfield
Journal:  Proc Natl Acad Sci U S A       Date:  1974-10       Impact factor: 11.205

Review 6.  [Reaction steps of polypeptide synthesis on ribosomes. Mechanisms of protein synthesis, X].

Authors:  H Matthaei; G Sander; D Swan; T Kreuzer; H Caffier; A Parmeggiani
Journal:  Naturwissenschaften       Date:  1968-06

7.  Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase.

Authors:  A N Baldwin; P Berg
Journal:  J Biol Chem       Date:  1966-02-25       Impact factor: 5.157

8.  Phenylalanyl-tRNA synthetase from baker's yeast: role of 3'-terminal adenosine of tRNA-Phe in enzyme-substrate interaction studied with 3'-modified tRNA-Phe species.

Authors:  F Von Der Haar; E Gaertner
Journal:  Proc Natl Acad Sci U S A       Date:  1975-04       Impact factor: 11.205

9. 

Authors:  F Cramer; F v.d. Haar; E Schlimme
Journal:  FEBS Lett       Date:  1968-12       Impact factor: 4.124

10.  Chemically modified phenylalanine transfer ribonucleic acid from yeast. Synthesis and properties of tRNA Phe-C-Cs-A and the effect of adenosine 5'-O-(1-thiotriphosphate) on the activation of phenylalanine.

Authors:  E Schlimme; F von der Haar; F Eckstein; F Cramer
Journal:  Eur J Biochem       Date:  1970-06
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