About: Diversity and roles of (t)RNA ligases

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	Diversity and roles of (t)RNA ligases
Creator	Martinez, Javier Popow, Johannes Schleiffer, Alexander Schleiffer, A
source	PMC
abstract	The discovery of discontiguous tRNA genes triggered studies dissecting the process of tRNA splicing. As a result, we have gained detailed mechanistic knowledge on enzymatic removal of tRNA introns catalyzed by endonuclease and ligase proteins. In addition to the elucidation of tRNA processing, these studies facilitated the discovery of additional functions of RNA ligases such as RNA repair and non-conventional mRNA splicing events. Recently, the identification of a new type of RNA ligases in bacteria, archaea, and humans closed a long-standing gap in the field of tRNA processing. This review summarizes past and recent findings in the field of tRNA splicing with a focus on RNA ligation as it preferentially occurs in archaea and humans. In addition to providing an integrated view of the types and phyletic distribution of RNA ligase proteins known to date, this survey also aims at highlighting known and potential accessory biological functions of RNA ligases. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1007/s00018-012-0944-2) contains supplementary material, which is available to authorized users.
has issue date	2012-03-17(xsd:dateTime)
bibo:doi	10.1007/s00018-012-0944-2
bibo:pmid	22426497
has license	no-cc
sha1sum (hex)	eba4fe7ae5e8a69de34227a077e2050f4a93cb2f
schema:url	https://doi.org/10.1007/s00018-012-0944-2
resource representing a document's title	Diversity and roles of (t)RNA ligases
has PubMed Central identifier	PMC3400036
has PubMed identifier	22426497
schema:publication	Cell Mol Life Sci
resource representing a document's body	covid:eba4fe7ae5e8a69de34227a077e2050f4a93cb2f#body_text
is schema:about of	named entity 'mechanistic' named entity 'discovery' named entity 'tRNA' named entity 'field' named entity 'catalyzed' named entity 'RNA' named entity 'ligases' named entity 'triggered' named entity 'ligation' named entity 'RNA' named entity 'dissecting' named entity 'archaea' named entity 'proteins' named entity 'The' named entity 'RNA' named entity 'phyletic' named entity 'RNA' named entity 'ligation' named entity 'tRNA' named entity 'tRNA' named entity 'RNA ligase' named entity 'bacteria' named entity 'tRNA' named entity 'tRNA' named entity 'biological functions' named entity 'archaea' named entity 'tRNA' named entity 'RNA' named entity 'tRNA' named entity 'tRNA' named entity 'helix' named entity 'homologous' named entity 'substrate' named entity 'archaea' named entity 'structural studies' named entity 'archaeal' named entity 'tRNA' named entity 'RNA' named entity 'phosphodiester' named entity 'tRNA' named entity 'bivalent' named entity 'Archaeal' named entity 'endonuclease' named entity 'homologous' named entity 'kinase' named entity 'ligase' named entity 'ligation' named entity 'protein families' named entity 'endonucleases' named entity 'genetic screen' named entity 'endonuclease' named entity 'exon' named entity 'viroids' named entity 'bacteria' named entity 'endonucleases' named entity 'intron' named entity 'RNA ligase' named entity 'RNA ligase' named entity 'exon' named entity 'diol' named entity 'biological functions' named entity 'phosphate' named entity 'nuclear proteins' named entity 'Saccharomyces cerevisiae' named entity 'protein' named entity 'ligation' named entity 'yeast' named entity 'tRNA' named entity 'yeast' named entity 'bacteria' named entity 'stoichiometric' named entity 'tRNAs' named entity 'phosphate' named entity 'cleavage site' named entity 'eukaryotic' named entity 'homologs' named entity 'tRNA' named entity 'vertebrate'

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