About: The role of wobble uridine modifications in +1 translational frameshifting in eukaryotes

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About: The role of wobble uridine modifications in +1 translational frameshifting in eukaryotes Goto Sponge NotDistinct Permalink

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

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	The role of wobble uridine modifications in +1 translational frameshifting in eukaryotes
Creator	Xu, Hao Byström, Anders Esberg, Anders Tükenmez, Hasan
source	PMC
abstract	In Saccharomyces cerevisiae, 11 out of 42 tRNA species contain 5-methoxycarbonylmethyl-2-thiouridine (mcm(5)s(2)U), 5-methoxycarbonylmethyluridine (mcm(5)U), 5-carbamoylmethyluridine (ncm(5)U) or 5-carbamoylmethyl-2′-O-methyluridine (ncm(5)Um) nucleosides in the anticodon at the wobble position (U(34)). Earlier we showed that mutants unable to form the side chain at position 5 (ncm(5) or mcm(5)) or lacking sulphur at position 2 (s(2)) of U(34) result in pleiotropic phenotypes, which are all suppressed by overexpression of hypomodified tRNAs. This observation suggests that the observed phenotypes are due to inefficient reading of cognate codons or an increased frameshifting. The latter may be caused by a ternary complex (aminoacyl-tRNAeEF1AGTP) with a modification deficient tRNA inefficiently being accepted to the ribosomal A-site and thereby allowing an increased peptidyl-tRNA slippage and thus a frameshift error. In this study, we have investigated the role of wobble uridine modifications in reading frame maintenance, using either the Renilla/Firefly luciferase bicistronic reporter system or a modified Ty1 frameshifting site in a HIS4A::lacZ reporter system. We here show that the presence of mcm(5) and s(2) side groups at wobble uridines are important for reading frame maintenance and thus the aforementioned mutant phenotypes might partly be due to frameshift errors.
has issue date	2015-10-30(xsd:dateTime)
bibo:doi	10.1093/nar/gkv832
bibo:pmid	26283182
has license	cc-by
sha1sum (hex)	053aa0c7280e2bb41a033cb0ae7c0d6bd07afc40
schema:url	https://doi.org/10.1093/nar/gkv832
resource representing a document's title	The role of wobble uridine modifications in +1 translational frameshifting in eukaryotes
has PubMed Central identifier	PMC4627075
has PubMed identifier	26283182
schema:publication	Nucleic Acids Res
resource representing a document's body	covid:053aa0c7280e2bb41a033cb0ae7c0d6bd07afc40#body_text
is schema:about of	named entity 'WOBBLE' named entity 'side chain' named entity 'ribosomal' named entity 'phenotypes' named entity 'ncm' named entity 'slippage' named entity 'cognate' named entity 'bicistronic' named entity 'codons' named entity 'URIDINE' named entity 'WOBBLE' named entity 'SUPPRESSED' named entity '5-METHOXYCARBONYLMETHYLURIDINE' named entity 'MODIFICATION' named entity 'SULPHUR' named entity 'PHENOTYPES' named entity 'HAVE' named entity '28S' named entity 'MUTANT' named entity 'SITE' named entity 'MODIFIED' named entity 'LACKING' named entity 'TRNA' named entity 'OBSERVATION' named entity 'SIDE CHAIN' named entity 'ALLOWING' named entity 'METHYLURIDINE' named entity 'ERRORS' named entity 'READING' named entity 'ACCEPTED' named entity 'A-SITE' named entity '5-CARBAMOYLMETHYLURIDINE' named entity 'ROLE' named entity 'URIDINE' named entity 'NUCLEOSIDES' named entity 'TRANSLATIONAL FRAMESHIFTING' named entity 'ROLE' named entity 'EUKARYOTES' named entity '2B1' named entity 'DUE TO' named entity 'TO FORM' named entity 'CAUSED BY' named entity 'SYSTEM' named entity 'PEPTIDYL-TRNA' named entity 'EITHER' named entity 'PRESENCE OF' named entity 'TY1' named entity 'EARLIER' named entity 'BEING' named entity 'THIOU' named entity 'MAY BE' named entity 'POSITION' named entity 'REPORTER' named entity 'STUDY' named entity 'SPECIES' named entity 'MCM' named entity 'INVESTIGATED' named entity 'MUTANTS' named entity 'USING' named entity 'ANTICODON' named entity 'IMPORTANT' named entity 'DEFICIENT' named entity 'FRAMESHIFT' named entity 'MAINTENANCE' named entity 'OVEREXPRESSION' named entity 'RENILLA' named entity 'SACCHAROMYCES CEREVISIAE' named entity 'INEFFICIENT' named entity 'TERNARY COMPLEX' named entity 'INCREASED' named entity 'LUCIFERASE' named entity 'RIBOSOMAL' named entity 'HERE' named entity 'CONTAIN' named entity 'GROUPS' named entity 'READING FRAME' named entity 'OBSERVED' named entity 'CODONS'

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