Size polymorphism and the structure of aminoacyl-tRNA synthetases - PubMed (original) (raw)
Comparative Study
. 1984 Dec;43(15):2987-90.
- PMID: 6389183
Comparative Study
Size polymorphism and the structure of aminoacyl-tRNA synthetases
P Schimmel et al. Fed Proc. 1984 Dec.
Abstract
Although aminoacyl-tRNA synthetases catalyze the same chemical reaction, the individual enzymes have a wide range of sizes. Proteolytic digestion has yielded active catalytic fragments of two synthetases. A set of gene deletions in a large synthetase has been used successfully in the creation of a variety of enzyme fragments that have been studied individually; a fragment with about half of the total polypeptide is sufficient to aminoacylate tRNA in vivo. The results suggest that size polymorphism is caused by fusion, to a core catalytic segment, of variable amounts of additional polypeptide sequences. These sequences may serve to impart additional functions. For example, in one case, a synthetase binds to its own gene promoter and regulates transcription.
Similar articles
- Glu-Q-tRNA(Asp) synthetase coded by the yadB gene, a new paralog of aminoacyl-tRNA synthetase that glutamylates tRNA(Asp) anticodon.
Blaise M, Becker HD, Lapointe J, Cambillau C, Giegé R, Kern D. Blaise M, et al. Biochimie. 2005 Sep-Oct;87(9-10):847-61. doi: 10.1016/j.biochi.2005.03.007. Epub 2005 Apr 8. Biochimie. 2005. PMID: 16164993 - Domain-domain communication for tRNA aminoacylation: the importance of covalent connectivity.
Zhang CM, Hou YM. Zhang CM, et al. Biochemistry. 2005 May 17;44(19):7240-9. doi: 10.1021/bi050285y. Biochemistry. 2005. PMID: 15882062 - [Comparative study of localization of tryptophanyl-tRNA-synthetase and components of high molecular weight aminoacyl-tRNA-synthetase complex in animal cells].
Ivanova IuL, Cherni NE, Popenko VI, Filonenko VV, Vartanian OG. Ivanova IuL, et al. Mol Biol (Mosk). 1993 May-Jun;27(3):666-84. Mol Biol (Mosk). 1993. PMID: 8316247 Russian. - The fidelity of the translation of the genetic code.
Sankaranarayanan R, Moras D. Sankaranarayanan R, et al. Acta Biochim Pol. 2001;48(2):323-35. Acta Biochim Pol. 2001. PMID: 11732604 Review. - Substrate selection by aminoacyl-tRNA synthetases.
Ibba M, Thomann HU, Hong KW, Sherman JM, Weygand-Durasevic I, Sever S, Stange-Thomann N, Praetorius M, Söll D. Ibba M, et al. Nucleic Acids Symp Ser. 1995;(33):40-2. Nucleic Acids Symp Ser. 1995. PMID: 8643392 Review.
Cited by
- Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryotic.
Dang CV, Dang CV. Dang CV, et al. Biochem J. 1986 Oct 15;239(2):249-55. doi: 10.1042/bj2390249. Biochem J. 1986. PMID: 3545179 Free PMC article. Review. No abstract available.