tRNAn+1 + phosphate tRNAn + a nucleoside diphosphate
where tRNA-N is a product of transcription, and tRNA Nucleotidyltransferase catalyzes this cytidine-cytidine-adenosine (CCA) addition to form the tRNA-NCCA product.
Function
Protein synthesis takes place in cytosolic ribosomes, mitochondria (mitoribosomes), and in plants, the plastids (chloroplast ribosomes). Each of these compartments requires a complete set of functional tRNAs to carry out protein synthesis. The production of mature tRNAs requires processing and modification steps[1] such as the addition of a 3’-terminal cytidine-cytidine-adenosine (CCA). Since no plant tRNA genes encode this particular sequence, a tRNA nucleotidyltransferase must add this sequence post-transcriptionally and therefore is present in all three compartments.
In eukaryotes, multiple forms of tRNA nucleotidyltransferases are synthesized from a single gene and are distributed to different subcellular compartments in the cell. There are multiple in-frame start codons which allow for the production of variant forms of the enzyme containing different targeting information predominantly found in the N-terminal sequence of the protein (reference). In vivo experiments show that the N-terminal sequences are used as transit peptides for import into the mitochondria and plastids. Comparison studies using available tRNA nucleotidyltransferase sequences have identified a single gene coding for this enzyme in plants. Complementation studies in yeast using cDNA derived from Arabidopsis thaliana[2] or Lupinus albus genes[3] demonstrate the biological activity of these enzymes. The enzyme has also been shown to repair damaged or incomplete CCA sequences in yeast.[4]
^Hopper AK, Phizicky EM (January 2003). "tRNA transfers to the limelight". Genes Dev. 17 (2): 162–80. doi:10.1101/gad.1049103. PMID 12533506.
^Gu J (2000). Identification of proteins interacting with lupin and Arabidopsis tRNA nucleotidyltransferase (MSc). Concordia University, Canada. pp. 51–55.
^Shanmugam K, Hanic-Joyce PJ, Joyce PB (January 1996). "Purification and characterization of a tRNA nucleotidyltransferase from Lupinus albus and functional complementation of a yeast mutation by corresponding cDNA". Plant Mol. Biol. 30 (2): 281–95. doi:10.1007/bf00020114. PMID 8616252. S2CID 8120292.
^Rosset R, Monier R (November 1965). "[Instability of the terminal 3'-hydroxy sequence of transfer RNA in microorganisms. I. Turnover of terminal AMP in Saccharomyces cerevisiae]". Biochim. Biophys. Acta (in French). 108 (3): 376–84. doi:10.1016/0005-2787(65)90030-4. PMID 4286478.
Further reading
Cudny H, Deutscher MP (1988). "3' processing of tRNA precursors in ribonuclease-deficient Escherichia coli. Development and characterization of an in vitro processing system and evidence for a phosphate requirement". J. Biol. Chem. 263 (3): 1518–23. doi:10.1016/S0021-9258(19)57334-3. PMID 3275667.
Deutscher MP, Marshall GT, Cudny H (1988). "RNase PH: an Escherichia coli phosphate-dependent nuclease distinct from polynucleotide phosphorylase". Proc. Natl. Acad. Sci. U.S.A. 85 (13): 4710–14. Bibcode:1988PNAS...85.4710D. doi:10.1073/pnas.85.13.4710. PMC280505. PMID 2455297.
trna, nucleotidyltransferase, enzymology, enzyme, that, catalyzes, chemical, reactionrnase, hexamer, pseudomonas, aeruginosaidentifiersec, 56cas, 116412, 3databasesintenzintenz, viewbrendabrenda, entryexpasynicezyme, viewkeggkegg, entrymetacycmetabolic, pathwa. In enzymology a tRNA nucleotidyltransferase EC 2 7 7 56 is an enzyme that catalyzes the chemical reactiontRNA nucleotidyltransferaseRNase PH hexamer Pseudomonas aeruginosaIdentifiersEC no 2 7 7 56CAS no 116412 36 3DatabasesIntEnzIntEnz viewBRENDABRENDA entryExPASyNiceZyme viewKEGGKEGG entryMetaCycmetabolic pathwayPRIAMprofilePDB structuresRCSB PDB PDBe PDBsumGene OntologyAmiGO QuickGOSearchPMCarticlesPubMedarticlesNCBIproteins tRNAn 1 phosphate displaystyle rightleftharpoons tRNAn a nucleoside diphosphatewhere tRNA N is a product of transcription and tRNA Nucleotidyltransferase catalyzes this cytidine cytidine adenosine CCA addition to form the tRNA NCCA product Function EditProtein synthesis takes place in cytosolic ribosomes mitochondria mitoribosomes and in plants the plastids chloroplast ribosomes Each of these compartments requires a complete set of functional tRNAs to carry out protein synthesis The production of mature tRNAs requires processing and modification steps 1 such as the addition of a 3 terminal cytidine cytidine adenosine CCA Since no plant tRNA genes encode this particular sequence a tRNA nucleotidyltransferase must add this sequence post transcriptionally and therefore is present in all three compartments In eukaryotes multiple forms of tRNA nucleotidyltransferases are synthesized from a single gene and are distributed to different subcellular compartments in the cell There are multiple in frame start codons which allow for the production of variant forms of the enzyme containing different targeting information predominantly found in the N terminal sequence of the protein reference In vivo experiments show that the N terminal sequences are used as transit peptides for import into the mitochondria and plastids Comparison studies using available tRNA nucleotidyltransferase sequences have identified a single gene coding for this enzyme in plants Complementation studies in yeast using cDNA derived from Arabidopsis thaliana 2 or Lupinus albus genes 3 demonstrate the biological activity of these enzymes The enzyme has also been shown to repair damaged or incomplete CCA sequences in yeast 4 This enzyme belongs to the family of transferases specifically those transferring phosphorus containing nucleotide groups nucleotidyltransferases References Edit Hopper AK Phizicky EM January 2003 tRNA transfers to the limelight Genes Dev 17 2 162 80 doi 10 1101 gad 1049103 PMID 12533506 Gu J 2000 Identification of proteins interacting with lupin and Arabidopsis tRNA nucleotidyltransferase MSc Concordia University Canada pp 51 55 Shanmugam K Hanic Joyce PJ Joyce PB January 1996 Purification and characterization of a tRNA nucleotidyltransferase from Lupinus albus and functional complementation of a yeast mutation by corresponding cDNA Plant Mol Biol 30 2 281 95 doi 10 1007 bf00020114 PMID 8616252 S2CID 8120292 Rosset R Monier R November 1965 Instability of the terminal 3 hydroxy sequence of transfer RNA in microorganisms I Turnover of terminal AMP in Saccharomyces cerevisiae Biochim Biophys Acta in French 108 3 376 84 doi 10 1016 0005 2787 65 90030 4 PMID 4286478 Further reading EditCudny H Deutscher MP 1988 3 processing of tRNA precursors in ribonuclease deficient Escherichia coli Development and characterization of an in vitro processing system and evidence for a phosphate requirement J Biol Chem 263 3 1518 23 doi 10 1016 S0021 9258 19 57334 3 PMID 3275667 Deutscher MP Marshall GT Cudny H 1988 RNase PH an Escherichia coli phosphate dependent nuclease distinct from polynucleotide phosphorylase Proc Natl Acad Sci U S A 85 13 4710 14 Bibcode 1988PNAS 85 4710D doi 10 1073 pnas 85 13 4710 PMC 280505 PMID 2455297 Portal Biology This EC 2 7 enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title TRNA nucleotidyltransferase amp oldid 1045676623, wikipedia, wiki, book, books, library,
