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About:
Polysomes Bypass a 50 Nucleotide Coding Gap less Efficiently than Monosomes Due to Attenuation of a 5’ mRNA Stem Loop and Enhanced Drop-off
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covidontheweb.inria.fr
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Academic Article
research paper
schema:ScholarlyArticle
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type
Academic Article
research paper
schema:ScholarlyArticle
isDefinedBy
Covid-on-the-Web dataset
title
Polysomes Bypass a 50 Nucleotide Coding Gap less Efficiently than Monosomes Due to Attenuation of a 5’ mRNA Stem Loop and Enhanced Drop-off
Creator
Samatova, Ekaterina
Klimova, Mariia
Loughran, Gary
Atkins, John
Baranov, Pavel
Rodnina, Marina
Weissman, Jonathan
Wills, Norma
Puglisi, Joseph
Capece, Mark
Coakley, Arthur
O'connor, Patrick
O'loughlin, Sinéad
source
Elsevier; Medline; PMC
abstract
Efficient translational bypassing of a 50 nt non-coding gap in a phage T4 topoisomerase subunit gene (gp60) requires several recoding signals. Here we investigate the function of the mRNA stem loop 5′ of the take-off codon, as well as the importance of ribosome loading density on the mRNA for efficient bypassing. We show that polysomes are less efficient at mediating bypassing than monosomes, both in vitro and in vivo, due to their preventing formation of a stem loop 5′ of the take-off codon and allowing greater peptidyl-tRNA drop off. A ribosome profiling analysis of phage T4 infected E. coli yielded protected mRNA fragments within the normal size range derived from ribosomes stalled at the take-off codon. However, ribosomes at this position also yielded some 53 nucleotide fragments, 16 longer. These were due to protection of the nucleotides that form the 5′ stem loop. NMR shows that the 5′ stem loop is highly dynamic. The importance of different nucleotides in the 5′ stem loop is revealed by mutagenesis studies. These data highlight the significance of the 5′ stem loop for the 50 nt bypassing, and further enhance appreciation of relevance of the extent of ribosome loading for recoding.
has issue date
2020-05-23
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xsd:dateTime
)
bibo:doi
10.1016/j.jmb.2020.05.010
bibo:pmid
32454154
has license
no-cc
sha1sum (hex)
3c643c7dfd1383dcb16e4ef5e98b208b58483ef7
schema:url
https://doi.org/10.1016/j.jmb.2020.05.010
resource representing a document's title
Polysomes Bypass a 50 Nucleotide Coding Gap less Efficiently than Monosomes Due to Attenuation of a 5’ mRNA Stem Loop and Enhanced Drop-off
has PubMed Central identifier
PMC7245268
has PubMed identifier
32454154
schema:publication
J Mol Biol
resource representing a document's body
covid:3c643c7dfd1383dcb16e4ef5e98b208b58483ef7#body_text
is
schema:about
of
named entity 'Bypass'
named entity 'Enhanced'
named entity 'Stem'
named entity 'mRNA'
named entity 'Polysomes'
named entity 'Stem Loop'
named entity 'structural analysis'
named entity 'ribosomal subunits'
named entity 'MNase'
named entity 'nucleotide'
named entity 'ribosome'
named entity 'SHAPE'
named entity 'NMR experiments'
named entity 'S3C'
named entity 'amino acids'
named entity 'tetraloop'
named entity 'RNase'
named entity 'wild-type'
named entity 'heterologous expression'
named entity 'RNA'
named entity 'Shine Dalgarno'
named entity 'vector'
named entity 'ribosome'
named entity 'complete synthesis'
named entity 'peptide signal'
named entity 'leading edge'
named entity 'vector'
named entity 'cleavage'
named entity 'mRNA'
named entity 'fluorescent label'
named entity 'mRNA'
named entity 'compensatory mutations'
named entity 'ribosomes'
named entity 'E. coli'
named entity 'translation initiation'
named entity 'plasmid-borne'
named entity 'Crick'
named entity 'ribosome'
named entity 'ribosome'
named entity 'SHAPE analysis'
named entity 'ribosome'
named entity 'stop codons'
named entity 'ribosome'
named entity 'ribonuclease'
named entity 'NMR'
named entity 'codons'
named entity 'protein'
named entity 'codon'
named entity '16S rRNA'
named entity 'translational machinery'
named entity 'ribosome'
named entity 'gene'
named entity 'KKYK'
named entity 'vectors'
named entity 'ribosome'
named entity 'Cricket Paralysis virus'
named entity 'A-site'
named entity 'Arg'
named entity 'ribosome'
named entity 'initiation factors'
named entity 'ribosome'
named entity 'cryoEM'
named entity 'codon'
named entity 'codon'
named entity 'translational machinery'
named entity 'homing endonuclease gene'
named entity 'cleavage'
named entity 'ribosome'
named entity 'oligonucleotide'
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