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- ********************************************************
- * Aminoacyl-transfer RNA synthetases class-I signature *
- ********************************************************
-
- Aminoacyl-tRNA synthetases (EC 6.1.1.-) [1] are a group of enzymes which
- activate amino acids and transfer them to specific tRNA molecules as the first
- step in protein biosynthesis. In prokaryotic organisms there are at least
- twenty different types of aminoacyl-tRNA synthetases, one for each different
- amino acid. In eukaryotes there are generally two aminoacyl-tRNA synthetases
- for each different amino acid: one cytosolic form and a mitochondrial form.
- While all these enzymes have a common function, they are widely diverse in
- terms of subunit size and of quaternary structure.
-
- A few years ago it was found [2] that several aminoacyl-tRNA synthetases share
- a region of similarity in their N-terminal section, in particular the
- consensus tetrapeptide His-Ile-Gly-His ('HIGH') is very well conserved. The
- 'HIGH' region has been shown [3] to be part of the adenylate binding site. The
- 'HIGH' signature has been found in the aminoacyl-tRNA synthetases specific for
- arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine,
- tyrosine, tryptophan, and valine. These aminoacyl-tRNA synthetases are
- referred to as class-I synthetases [4,5,6] and seem to share the same tertiary
- structure based on a Rossmann fold.
-
- -Consensus pattern: P-x(0,2)-[STAN]-x(2)-[LIVMFYP]-[HT]-[LIVMFYAC]-G-[HNTG]-
- [LIVMFYSTAC]
- -Sequences known to belong to this class detected by the pattern: ALL, except
- for Cys-tRNA ligases and three other sequences.
- -Other sequence(s) detected in SWISS-PROT: 52.
-
- -Note: in position 8 of the pattern His is present in all tRNA-synthetases of
- class-I except in some bacterial tryptophanyl-tRNA synthetases which have a
- Thr in that position.
-
- -Last update: June 1994 / Text revised.
-
- [ 1] Schimmel P.
- Annu. Rev. Biochem. 56:125-158(1987).
- [ 2] Webster T., Tsai H., Kula M., Mackie G.A., Schimmel P.
- Science 226:1315-1317(1984).
- [ 3] Brick P., Bhat T.N., Blow D.M.
- J. Mol. Biol. 208:83-98(1988).
- [ 4] Delarue M., Moras D.
- BioEssays 15:675-687(1993).
- [ 5] Schimmel P.
- Trends Biochem. Sci. 16:1-3(1991).
- [ 6] Nagel G.M., Doolittle R.F.
- Proc. Natl. Acad. Sci. U.S.A. 88:8121-8125(1991).
-