Molecular mechanisms of template-independent RNA polymerization by tRNA nucleotidyltransferases

The universal 3'-terminal CCA sequence of tRNA is built and/or synthesized by the CCA-adding enzyme, CTP:(ATP) tRNA nucleotidyltransferase. This RNA polymerase has no nucleic acid template, but faithfully synthesizes the defined CCA sequence on the 3'-terminus of tRNA at one time, using CT...

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Main Authors: Kozo eTomita, Seisueke eYamashita
Format: Article
Language:English
Published: Frontiers Media S.A. 2014-02-01
Series:Frontiers in Genetics
Subjects:
CCA
Online Access:http://journal.frontiersin.org/Journal/10.3389/fgene.2014.00036/full
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spelling doaj-24924c21dfa148bcbd66cdbae018dc462020-11-24T23:56:02ZengFrontiers Media S.A.Frontiers in Genetics1664-80212014-02-01510.3389/fgene.2014.0003681062Molecular mechanisms of template-independent RNA polymerization by tRNA nucleotidyltransferasesKozo eTomita0Seisueke eYamashita1RNA Processing Research Group, Biomedical Research Institute, National Institute of Advanced Industrial Science and TechnologyRNA Processing Research Group, Biomedical Research Institute, National Institute of Advanced Industrial Science and TechnologyThe universal 3'-terminal CCA sequence of tRNA is built and/or synthesized by the CCA-adding enzyme, CTP:(ATP) tRNA nucleotidyltransferase. This RNA polymerase has no nucleic acid template, but faithfully synthesizes the defined CCA sequence on the 3'-terminus of tRNA at one time, using CTP and ATP as substrates. The mystery of CCA-addition without a nucleic acid template by unique RNA polymerases has long fascinated researchers in the field of RNA enzymology. In this review, the mechanisms of RNA polymerization by the remarkable CCA-adding enzyme and its related enzymes are presented, based on their structural features.http://journal.frontiersin.org/Journal/10.3389/fgene.2014.00036/fulltRNACCAtemplate-independentnucleotidyltransferaseclass-I and II
collection DOAJ
language English
format Article
sources DOAJ
author Kozo eTomita
Seisueke eYamashita
spellingShingle Kozo eTomita
Seisueke eYamashita
Molecular mechanisms of template-independent RNA polymerization by tRNA nucleotidyltransferases
Frontiers in Genetics
tRNA
CCA
template-independent
nucleotidyltransferase
class-I and II
author_facet Kozo eTomita
Seisueke eYamashita
author_sort Kozo eTomita
title Molecular mechanisms of template-independent RNA polymerization by tRNA nucleotidyltransferases
title_short Molecular mechanisms of template-independent RNA polymerization by tRNA nucleotidyltransferases
title_full Molecular mechanisms of template-independent RNA polymerization by tRNA nucleotidyltransferases
title_fullStr Molecular mechanisms of template-independent RNA polymerization by tRNA nucleotidyltransferases
title_full_unstemmed Molecular mechanisms of template-independent RNA polymerization by tRNA nucleotidyltransferases
title_sort molecular mechanisms of template-independent rna polymerization by trna nucleotidyltransferases
publisher Frontiers Media S.A.
series Frontiers in Genetics
issn 1664-8021
publishDate 2014-02-01
description The universal 3'-terminal CCA sequence of tRNA is built and/or synthesized by the CCA-adding enzyme, CTP:(ATP) tRNA nucleotidyltransferase. This RNA polymerase has no nucleic acid template, but faithfully synthesizes the defined CCA sequence on the 3'-terminus of tRNA at one time, using CTP and ATP as substrates. The mystery of CCA-addition without a nucleic acid template by unique RNA polymerases has long fascinated researchers in the field of RNA enzymology. In this review, the mechanisms of RNA polymerization by the remarkable CCA-adding enzyme and its related enzymes are presented, based on their structural features.
topic tRNA
CCA
template-independent
nucleotidyltransferase
class-I and II
url http://journal.frontiersin.org/Journal/10.3389/fgene.2014.00036/full
work_keys_str_mv AT kozoetomita molecularmechanismsoftemplateindependentrnapolymerizationbytrnanucleotidyltransferases
AT seisuekeeyamashita molecularmechanismsoftemplateindependentrnapolymerizationbytrnanucleotidyltransferases
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