TRNA nucleotidyltransferase

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tRNA nucleotidyltransferase
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RNase PH hexamer, Pseudomonas aeruginosa
Identifiers
EC no. 2.7.7.56
CAS no. 116412-36-3
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In enzymology, a tRNA nucleotidyltransferase (EC 2.7.7.56) is an enzyme that catalyzes the chemical reaction

Contents

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]

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases).

Related Research Articles

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<span class="mw-page-title-main">Transfer-messenger RNA</span>

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<span class="mw-page-title-main">Directionality (molecular biology)</span> End-to-end chemical orientation of a single strand of nucleic acid

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Phosphoribosylformylglycinamidine cyclo-ligase is the fifth enzyme in the de novo synthesis of purine nucleotides. It catalyzes the reaction to form 5-aminoimidazole ribotide (AIR) from formylglycinamidine-ribonucleotide FGAM. This reaction closes the ring and produces a 5-membered imidazole ring of the purine nucleus (AIR):

Elongation factor 4 (EF-4) is an elongation factor that is thought to back-translocate on the ribosome during the translation of RNA to proteins. It is found near-universally in bacteria and in eukaryotic endosymbiotic organelles including the mitochondria and the plastid. Responsible for proofreading during protein synthesis, EF-4 is a recent addition to the nomenclature of bacterial elongation factors.

<span class="mw-page-title-main">5S ribosomal RNA</span> RNA component of the large subunit of the ribosome

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<span class="mw-page-title-main">Signal recognition particle RNA</span>

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<span class="mw-page-title-main">Polynucleotide adenylyltransferase</span>

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CCA tRNA nucleotidyltransferase is an enzyme with systematic name CTP,CTP,ATP:tRNA cytidylyl,cytidylyl,adenylyltransferase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Expanded genetic code</span> Modified genetic code

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<span class="mw-page-title-main">Chloroplast DNA</span> DNA located in cellular organelles called chloroplasts

Chloroplast DNA (cpDNA) is the DNA located in chloroplasts, which are photosynthetic organelles located within the cells of some eukaryotic organisms. Chloroplasts, like other types of plastid, contain a genome separate from that in the cell nucleus. The existence of chloroplast DNA was identified biochemically in 1959, and confirmed by electron microscopy in 1962. The discoveries that the chloroplast contains ribosomes and performs protein synthesis revealed that the chloroplast is genetically semi-autonomous. The first complete chloroplast genome sequences were published in 1986, Nicotiana tabacum (tobacco) by Sugiura and colleagues and Marchantia polymorpha (liverwort) by Ozeki et al. Since then, a great number of chloroplast DNAs from various species have been sequenced.

References

  1. Hopper AK, Phizicky EM (January 2003). "tRNA transfers to the limelight". Genes Dev. 17 (2): 162–80. doi: 10.1101/gad.1049103 . PMID   12533506.
  2. Gu J (2000). Identification of proteins interacting with lupin and Arabidopsis tRNA nucleotidyltransferase (MSc). Concordia University, Canada. pp. 51–55.
  3. 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.
  4. 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