Literature DB >> 351566

Interaction of Escherichia coli glutaminyl-tRNA synthesis with noncognate tRNA's.

T Seno, A Nakamura, S Fukuhara, K Iwata.   

Abstract

Several noncognate tRNA's from Escherichia coli were mischarged with glutamine by E. coli glutaminyl-tRNA synthetase if dimethylsulfoxide was present in the reaction mixture. Kinetic analysis of the mischarging revealed that dimethyl sulfoxide stimulated the misacylation by affecting the maximum velocity. Several noncognate tRNA's were shown to interact with glutaminyl-tRNA synthetase as measured by their ability to protect the enzyme against thermal inactivation or to replace cognate tRNA in stimulating glutamine-dependent ATP-PPi exchange reaction. These tRNA's, however, did not coincide with those which were mischargeable with glutamine.

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Year:  1978        PMID: 351566      PMCID: PMC342104          DOI: 10.1093/nar/5.5.1561

Source DB:  PubMed          Journal:  Nucleic Acids Res        ISSN: 0305-1048            Impact factor:   16.971


  13 in total

1.  GLUTAMYL AND GLUTAMINYL RIBONUCLEIC ACID SYNTHETASES OF ESCHERICHIA COLI W. SEPARATION, PROPERTIES, AND STIMULATION OF ADENOSINE TRIPHOSPHATE-PYROPHOSPHATE EXCHANGE BY ACCEPTOR RIBONUCLEIC ACID.

Authors:  J M RAVEL; S F WANG; C HEINEMEYER; W SHIVE
Journal:  J Biol Chem       Date:  1965-01       Impact factor: 5.157

2.  Structural organization of complexes of transfer RNAs with aminoacyl transfer RNA synthetases.

Authors:  A Rich; P R Schimmel
Journal:  Nucleic Acids Res       Date:  1977       Impact factor: 16.971

3.  A single mutational modification of a tryptophan-specific transfer RNA permits aminoacylation by glutamine and translation of the codon UAG.

Authors:  M Yaniv; W R Folk; P Berg; L Soll
Journal:  J Mol Biol       Date:  1974-06-25       Impact factor: 5.469

4.  Incorrect aminoacylatins catalysed by the phenylalanyl-and valyl-tRNA synthetases from yeast.

Authors:  D Kern; R Giegé; J P Ebel
Journal:  Eur J Biochem       Date:  1972-11-21

5.  Amino acid acceptor stem of E. coli suppressor tRNA tyr is a site of synthetase recognition.

Authors:  J E Celis; M L Hooper; J D Smith
Journal:  Nat New Biol       Date:  1973-08-29

6.  Involvement of the anticodon region of Escherichia coli tRNAGln and tRNAGlu in the specific interaction with cognate aminoacyl-tRNA synthetase. Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur deprivation.

Authors:  T Seno; P F Agris; D Söll
Journal:  Biochim Biophys Acta       Date:  1974-05-31

7.  Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. II. Interaction with intact glutamyl transfer ribonucleic acid.

Authors:  J Lapointe; D Söll
Journal:  J Biol Chem       Date:  1972-08-25       Impact factor: 5.157

8.  Glutamyl transfer ribonucleic acid synthetase of Escherichia coli. I. Purification and properties.

Authors:  J Lapointe; D Söll
Journal:  J Biol Chem       Date:  1972-08-25       Impact factor: 5.157

9.  Molecular weighr of Escherichia coli glutaminyl transfer ribonucleic acid synthetase, and isolation of its complex with glutamine transfer ribonucleic acid.

Authors:  W R Folk
Journal:  Biochemistry       Date:  1971-04-27       Impact factor: 3.162

10.  Binding of transfer RNA and arginine to the arginine transfer RNA synthetase of Escherichia coli.

Authors:  S K Mitra; K Chakraburtty; A H Mehler
Journal:  J Mol Biol       Date:  1970-04-14       Impact factor: 5.469

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