aminoacyl tRNA

aminoacyl tRNA

[ə¦mē·nō¦as·əl ¦tē‚är‚en′ā]
(cell and molecular biology)
A molecular complex formed during protein synthesis by the linkage of a transfer ribonucleic acid molecule (tRNA) with its corresponding amino acid.
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
On the seventh day of hospitalization, the results of analysis of a blood sample taken on the day of admission showed that the patient had positive titers for autoantibodies against aminoacyl tRNA synthetase (ARS), including anti-Jo-1 antibodies.
Of these, the GARS gene located on chromosome 7p produces an aminoacyl tRNA synthetase responsible for charging the associated tRNAs and the first protein of its kind implicated in any inherited human disorder.
Discovered in 2003, this is the first example of an aminoacyl tRNA synthetase being implicated in any inherited human disorder, and so far 11 pathogenic missense GARS variants have been linked to not only dSMA-V but also Charcot-Marie-Tooth disease type 2D (CMT2D) [2].
One such family of enzymes is the aminoacyl tRNA synthetase, which is responsible for catalyzing the reaction that "charges" transfer-RNA with an amino acid.
"Aminoacyl tRNA synthetases are associated with - and we believe needed for - the building of organismal complexity, such as making tissues and organs in humans," Paul Schimmel from the Scripps Research Institute in California explained in a (http://www.scripps.edu/news/press/2016/20161209schimmel.html) statement released Friday.
However, Schimmel and his colleagues have now (http://www.pnas.org/content/early/2016/11/23/1617316113) discovered an aminoacyl tRNA synthetase called AlaRS that lacks any new decorations and can somehow still carry out its new role in humans without overhauling its basic architecture.
The RNA components of a ribosome are working like a ribozyme and play a central role, together with aminoacyl tRNA, in polypeptide formation, while the ribosomal proteins maintain the ribosomal structure and regulate the translational process.
In addition to ribosomal proteins, other proteins involved in translation, including peptidases (aminopeptidase C, aminopeptidase N, dipeptidase, peptidase T, proline dipeptidase, prolidase, and Xaa-Pro aminopeptidase), aminoacyl tRNA synthetases (arginyl-tRNA synthetase, isoleucyl-tRNA synthetase, phenylalanyl-tRNA synthetase beta chain, seryltRNA synthetase, threonyl-tRNA synthetase, and tyrosyltRNA synthetase), translation factors (elongation factors G, P, Ts, and Tu, translation initiation factor IF-1, and ribosome recycling factor), and proteins involved in modification (peptidyl-prolyl cis-trans isomerase), were identified in the proteomes from both growth phases.
Physiocrines are derived from aminoacyl tRNA synthetases, which have been known for decades to function intracellularly in protein synthesis.
Chapter 4 presents the two subclasses of aminoacyl tRNA synthetases and the significance of the genetic code assignments to each enzyme.
The top-half domain, sometimes referred to as a tRNA "minihelix," has been shown to provide the determinants necessary for specific charging by aminoacyl tRNA synthetases (14, 15); for interaction with elongation factor Tu (16); for 5[prime] processing by RNase P (17); and for distinguishing elongator from initiator tRNA (18).
Consequently I don't think that a full complement of aminoacyl tRNAs could be made by ribozymes.