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Transfer RNA is an adaptor molecule composed of RNA, typically 76 to 90 nucleotides in length, that serves as the physical link between the mRNA and the amino acid sequence of proteins. Transfer RNA (tRNA) does this by carrying an amino acid to the protein synthesizing machinery of a cell called the ribosome. Complementation of a 3-nucleotide codon in a messenger RNA (mRNA) by a 3-nucleotide anticodon of the tRNA results in protein synthesis based on the mRNA code. As such, tRNAs are a necessary component of translation, the biological synthesis of new proteins in accordance with the genetic code.
An aminoacyl-tRNA synthetase, also called tRNA-ligase, is an enzyme that attaches the appropriate amino acid onto its corresponding tRNA. It does so by catalyzing the transesterification of a specific cognate amino acid or its precursor to one of all its compatible cognate tRNAs to form an aminoacyl-tRNA. In humans, the 20 different types of aa-tRNA are made by the 20 different aminoacyl-tRNA synthetases, one for each amino acid of the genetic code.
EF-Tu is a prokaryotic elongation factor responsible for catalyzing the binding of an aminoacyl-tRNA (aa-tRNA) to the ribosome. It is a G-protein, and facilitates the selection and binding of an aa-tRNA to the A-site of the ribosome. As a reflection of its crucial role in translation, EF-Tu is one of the most abundant and highly conserved proteins in prokaryotes. It is found in eukaryotic mitochondria as TUFM.
In enzymology, an arginine—tRNA ligase is an enzyme that catalyzes the chemical reaction
Aspartate—tRNAAsn ligase is an enzyme with systematic name L-aspartate:tRNAAsx ligase (AMP-forming). This enzyme catalyses the following chemical reaction
In enzymology, a glutamate—tRNAGln ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a glutamate—tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a glutamine—tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a phenylalanine—tRNA ligase is an enzyme that catalyzes the chemical reaction
In enzymology, a threonine-tRNA ligase is an enzyme that catalyzes the chemical reaction
Tyrosine—tRNA ligase, also known as tyrosyl-tRNA synthetase is an enzyme that is encoded by the gene YARS. Tyrosine—tRNA ligase catalyzes the chemical reaction
In enzymology, an amidase is an enzyme that catalyzes the hydrolysis of an amide:
Bifunctional aminoacyl-tRNA synthetase is an enzyme that in humans is encoded by the EPRS gene.
Glutaminyl-tRNA synthetase is an enzyme that in humans is encoded by the QARS gene.
Aminoacyl-tRNA synthetases, class II is a family of proteins. These proteins catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have a limited sequence homology.
EF-P is an essential protein that in bacteria stimulates the formation of the first peptide bonds in protein synthesis. Studies show that EF-P prevents ribosomes from stalling during the synthesis of proteins containing consecutive prolines. EF-P binds to a site located between the binding site for the peptidyl tRNA and the exiting tRNA. It spans both ribosomal subunits with its amino-terminal domain positioned adjacent to the aminoacyl acceptor stem and its carboxyl-terminal domain positioned next to the anticodon stem-loop of the P site-bound initiator tRNA. The EF-P protein shape and size is very similar to a tRNA and interacts with the ribosome via the exit “E” site on the 30S subunit and the peptidyl-transferase center (PTC) of the 50S subunit. EF-P is a translation aspect of an unknown function, therefore It probably functions indirectly by altering the affinity of the ribosome for aminoacyl-tRNA, thus increasing their reactivity as acceptors for peptidyl transferase.
In molecular biology, the protein domain WHEP-TRS refers to helix-turn-helix domains. They are found in variable numbers in glutamyl-prolyl tRNA synthetase (EPRS). This protein domain has an important function in protein–protein interactions between synthetases. WHEP domains exhibit high-affinity interactions with tRNA, indicating a putative evolutionary relationship to facilitate tRNA binding to fused synthetases, thereby enhancing catalytic efficiency.
The B3/B4 domain, is found in tRNA synthetase beta subunits, as well as in some non-tRNA synthetase proteins.
In molecular biology, Yce-I protein domain is a putative periplasmic protein. This entry represents the lipid-binding protein YceI from Escherichia coli and the polyisoprenoid-binding protein TTHA0802 from Thermus thermophilus. Its role is to help aid the biosynthesis of isoprenoid, an important molecule found in all living organisms.
Dino Moras, born on 23 November 1944, is a French biochemist, research director at the CNRS and co-director of the Institute of Genetics and Molecular and Cellular Biology (IGBMC) in Illkirch-Graffenstaden until 2010.
References
- ↑ Delarue M, Moras D, Poch O, Eriani G, Gangloff J (1990). "Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs". Nature. 347 (6289): 203–206. Bibcode:1990Natur.347..203E. doi:10.1038/347203a0. PMID 2203971. S2CID 4324290.
- ↑ Moras D, Konno M, Shimada A, Nureki O, Tateno M, Yokoyama S, Sugiura I, Ugaji-Yoshikawa Y, Kuwabara S, Lorber B, Giege R (2000). "The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules". Structure. 8 (2): 197–208. doi: 10.1016/S0969-2126(00)00095-2 . PMID 10673435.
- ↑ Perona JJ, Steitz TA, Rould MA (1993). "Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase". Biochemistry. 32 (34): 8758–8771. doi:10.1021/bi00085a006. PMID 8364025.
- ↑ Delarue M, Moras D (1993). "The aminoacyl-tRNA synthetase family: modules at work". BioEssays. 15 (10): 675–687. doi:10.1002/bies.950151007. PMID 8274143. S2CID 35612984.
- ↑ Schimmel P (1991). "Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code". Trends Biochem. Sci. 16 (1): 1–3. doi:10.1016/0968-0004(91)90002-D. PMID 2053131.
- ↑ Cusack S, Leberman R, Hartlein M (1991). "Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases". Nucleic Acids Res. 19 (13): 3489–3498. doi:10.1093/nar/19.13.3489. PMC 328370 . PMID 1852601.
- ↑ Bairoch A (2004). "List of aminoacyl-tRNA synthetases".
{{cite journal}}: Cite journal requires|journal=(help) - ↑ Soll D, Freist W, Gauss DH, Lapointe J (1997). "Glutamyl-tRNA sythetase". Biol. Chem. 378 (11): 1313–1329. doi:10.1515/bchm.1997.378.11.1299. PMID 9426192.
