Conformational Activation of the Yeast Phenylalanyl-tRNA Synthetase Catalytic Site Induced by TRNAPhe Interaction: Triggering of Adenosine or CpCpA Trinucleoside Diphosphate Aminoacylation Upon Binding of TRNAPhe Lacking These Residues

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1981 Mar 1

PMID 7015339

Citations 3

Authors

M Renaud

H Bacha

P Remy

J P Ebel

Affiliations

Soon will be listed here.

Abstract

Adenosine or CpCpA trinucleoside diphosphate can be aminoacylated by phenylalanyl-tRNA synthetase [L-phenylalanine:tRNAPhe ligase (AMP forming), EC 6.1.1.20] when the reaction takes place in the presence of tRNAPhe deprived of its 3' adenosine or pCpCpA terminus. This shows that, upon interaction with tRNA, a structural alteration of the enzyme's active site is achieved. This process may be a determining step in the specificity of the aminoacylation reaction.

Citing Articles

The early history of tRNA recognition by aminoacyl-tRNA synthetases.

Giege R J Biosci. 2007; 31(4):477-88.

PMID: 17206068 DOI: 10.1007/BF02705187.

Biosynthesis of Tetrapyrrole Pigment Precursors : Formation and Utilization of Glutamyl-tRNA for delta-Aminolevulinic Acid Synthesis by Isolated Enzyme Fractions from Chlorella Vulgaris.

Avissar Y, Beale S Plant Physiol. 1988; 88(3):879-86.

PMID: 16666399 PMC: 1055677. DOI: 10.1104/pp.88.3.879.

Anticodon-independent aminoacylation of an RNA minihelix with valine.

Frugier M, Florentz C, Giege R Proc Natl Acad Sci U S A. 1992; 89(9):3990-4.

PMID: 1570324 PMC: 525617. DOI: 10.1073/pnas.89.9.3990.

References

UZIEL M, KHYM J . Sequential degradation of nucleic acids. Degradation of Escherichia coli B phenylalanine transfer ribonucleic acid. Biochemistry. 1969; 8(8):3254-60. DOI: 10.1021/bi00836a018. View

Hanes C, ISHERWOOD F . Separation of the phosphoric esters on the filter paper chromatogram. Nature. 1949; 164(4183):1107-12, illust. DOI: 10.1038/1641107a0. View

Kern D, Giege R, Ebel J . Incorrect aminoacylatins catalysed by the phenylalanyl-and valyl-tRNA synthetases from yeast. Eur J Biochem. 1972; 31(1):148-55. DOI: 10.1111/j.1432-1033.1972.tb02513.x. View

Kim S, Suddath F, QUIGLEY G, McPherson A, Sussman J, Wang A . Three-dimensional tertiary structure of yeast phenylalanine transfer RNA. Science. 1974; 185(4149):435-40. DOI: 10.1126/science.185.4149.435. View

Robertus J, Ladner J, Finch J, Rhodes D, Brown R, Clark B . Structure of yeast phenylalanine tRNA at 3 A resolution. Nature. 1974; 250(467):546-51. DOI: 10.1038/250546a0. View

Rether B, Bonnet J, Ebel J . Studies on tRNA nucleotidyltransferase from baker's yeast. 1. Purification of the enzyme. Protection against thermal inactivation and inhibition by several substrates. Eur J Biochem. 1974; 50(1):281-8. DOI: 10.1111/j.1432-1033.1974.tb03896.x. View

Bonnet J, BEFORT N, BOLLACK C, Fasiolo F, Ebel J . Study of the role of the acceptor stem in the interactions between tRNAs and aminoacyl-tRNA synthetases. Nucleic Acids Res. 1975; 2(2):211-21. PMC: 342827. DOI: 10.1093/nar/2.2.211. View

Fasiolo F, Ebel J . Yeast phenylalanyl-tRNA synthetase. Stoichiometry of the phenylalanyl adenylate-enzyme complex and transfer of phenylalanine from this complex to tRNA-PHE. Eur J Biochem. 1974; 49(1):257-63. DOI: 10.1111/j.1432-1033.1974.tb03830.x. View

Fasiolo F, Boulanger Y, Ebel J . Modification of phenylalanyl-tRNA synthetase from baker's yeast by proteolytic cleavage and properties of the trypsin-modified enzyme. Eur J Biochem. 1975; 53(2):487-92. DOI: 10.1111/j.1432-1033.1975.tb04090.x. View

10.

Wubbeler W, Lossow C, FITTLER F, Zachau H . Amino-acid incorporation into tRNA fragments and into heterologous combinations of fragments. Eur J Biochem. 1975; 59(2):405-13. DOI: 10.1111/j.1432-1033.1975.tb02468.x. View

11.

Rigler R, Pachmann U, Hirsch R, Zachau H . On the interaction of seryl-tRNA synthetase with tRNA Ser. A contribution to the problem of synthetase-tRNA recognition. Eur J Biochem. 1976; 65(1):307-15. DOI: 10.1111/j.1432-1033.1976.tb10418.x. View

12.

Willick G, Kay C . Circular dichroism study of the interaction of glutamyl-tRNA synthetase with tRNAGlu2. Biochemistry. 1976; 15(19):4347-52. DOI: 10.1021/bi00664a032. View

13.

Krauss G, Riesner D, Maass G . Mechanism of discrimination between cognate and non-cognate tRNAs by phenylalanyl-tRNA synthetase from yeast. Eur J Biochem. 1976; 68(1):81-93. DOI: 10.1111/j.1432-1033.1976.tb10766.x. View

14.

Baltzinger M, Remy P . Yeast phenylalanyl--tRNA synthetase. Stimulation of the hydrolysis of enzyme bound aminoacyladenylate upon binding of tRNA. FEBS Lett. 1977; 79(1):117-20. DOI: 10.1016/0014-5793(77)80363-3. View

15.

Rich A, Schimmel P . Structural organization of complexes of transfer RNAs with aminoacyl transfer RNA synthetases. Nucleic Acids Res. 1977; 4(5):1649-65. PMC: 343779. DOI: 10.1093/nar/4.5.1649. View

16.

Fersht A, Gangloff J, DIRHEIMER G . Reaction pathway and rate-determining step in the aminoacylation of tRNAArg catalyzed by the arginyl-tRNA synthetase from yeast. Biochemistry. 1978; 17(18):3740-6. DOI: 10.1021/bi00611a011. View

17.

Fayat G, Hountondji C, Blanquet S . Methionyl-tRNA synthetase from Escherichia coli. Inactivation and labeling by periodate-treated initiator tRNA. Eur J Biochem. 1979; 96(1):87-92. DOI: 10.1111/j.1432-1033.1979.tb13016.x. View

18.

Zaccai G, Morin P, Jacrot B, Moras D, Thierry J, Giege R . Interactions of yeast valyl-tRNA synthetase with RNAs and conformational changes of the enzyme. J Mol Biol. 1979; 129(3):483-500. DOI: 10.1016/0022-2836(79)90508-4. View

19.

Favre A, Ballini J, Holler E . Phenylalanyl-tRNA synthetase induced conformational change of Escherichia coli tRNA phe. Biochemistry. 1979; 18(13):2887-95. DOI: 10.1021/bi00580a033. View

20.

Renaud M, Ehrlich R, Bonnet J, Remy P . Lack of correlation between affinity of the tRNA for the aminoacyl-tRNA synthetase and aminoacylation capacity as studied with modified tRNAPhe. Eur J Biochem. 1979; 100(1):157-64. DOI: 10.1111/j.1432-1033.1979.tb02044.x. View