Are the tryptophanyl‐tRNA synthetase and the peptide‐chain‐release factor from higher eukaryotes one and the same protein?
- 3 March 1993
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 212 (2), 457-466
- https://doi.org/10.1111/j.1432-1033.1993.tb17682.x
Abstract
Recently, cDNA clones encoding the bovine (b) [M. Garret, B. Pajot, V. Trézéguet, J. Labouesse, M. Merle, J.-C. Gandar, J.-P. Benedetto, M.-L. Sallafranque, J. Alterio, M. Gueguen, C. Sarger, B. Labouesse and J. Bonnet (1991) Biochemistry 30, 7809-7817] and human (h) [L. Yu. Frolova, M. A. Sudomoina, A. Yu. Grigorieva, O. L. Zinovieva and L. L. Kisselev (1991) Gene 109, 291-296] tryptophanyl-tRNA synthetases (TrpRS) were sequenced; the deduced amino acid sequences exhibit typical structural features of class I aminoacyl-tRNA synthetases [G. Eriani, M. Delarue, O. Poch, J. Gangloff and D. Moras (1990) Nature 237, 203-206] and limited, although significant, similarity with bacterial TrpRS. Independently, it was shown that a major protein whose synthesis is stimulated in human cell cultures by interferon gamma [J. Fleckner, H. H. Rasmussen and J. Justesen (1991) Proc. Natl Acad. Sci. USA 88, 11,520-11,524], and interferons gamma or alpha [B. Y. Rubins, S. L. Anderson, L. Xing, R. J. Powell and W. P. Tate (1991) J. Biol. Chem. 226, 24,245-24,248], exhibits TrpRS activity and an amino acid sequence identical to that of hTrpRS. The amino acid sequences of bTrpRS and hTrpRS are highly similar and are surprisingly very similar to the amino acid sequence deduced from a cloned and sequenced cDNA reported to encode rabbit (r) peptide-chain-release factor (RF) [C. C. Lee, W. J. Craigen, D. M. Muzny, E. Harlow and C. T. Caskey (1990) Proc. Natl Acad. Sci. USA 87, 3508-3512]. This close similarity between mammalian TrpRS and cloned RF is unexpected given the distinct functional properties of these proteins. Consequently, the question arises as to whether the mammalian TrpRS and RF activities reside on identical or very similar polypeptides. Alternatively, one may assume that the cloned rabbit cDNA encodes a protein other than rRF. Several properties (immunochemical, biochemical and physico-chemical) of mammalian TrpRS and RF have been compared. rTrpRS and rRF have distinct thermostability behaviours, and dissimilar chromatographic profiles on phosphocellulose. Both the anti-bTrpRS polyclonal antibodies and the monoclonal antibody Am2 strongly inhibit the bTrpRS and hTrpRS aminoacylation activities, but not the rRF activity. In addition, neither bTrpRS nor hTrpRS exhibit RF activity.(ABSTRACT TRUNCATED AT 400 WORDS)Keywords
This publication has 47 references indexed in Scilit:
- Carbohydrates in mammalian tryptophanyl‐tRNA synthetaseFEBS Letters, 1992
- An interferon‐induced protein with release factor activity is a tryptophanyl‐tRNA synthetaseFEBS Letters, 1992
- Cloning and nucleotide sequence of the structural gene encoding for human tryptophanyl-tRNA synthetaseGene, 1991
- Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifsNature, 1990
- Stop making sense or Regulation at the level of termination in eukaryotic protein synthesisFEBS Letters, 1988
- Effects of the ligands of beef tryptophanyl-tRNA synthetase on the elementary steps of the tRNATrp aminoacylationBiochemistry, 1988
- Kinetic evidence for half-of-the-sites reactivity in tRNATrp aminoacylation by tryptophanyl-tRNA synthetase from beef pancreasBiochemistry, 1986
- Bovine Tryptophanyl‐tRNA SynthetaseEuropean Journal of Biochemistry, 1981
- Role of exposed cytosine residues in aminoacylation activity of tRNATrpFEBS Letters, 1981
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970