schliessen

Filtern

 

Bibliotheken

Rational design and directed evolution of a bacterial-type glutaminyl-tRNA synthetase precursor

Protein biosynthesis requires aminoacyl-transfer RNA (tRNA) synthetases to provide aminoacyl-tRNA substrates for the ribosome. Most bacteria and all archaea lack a glutaminyl-tRNA synthetase (GlnRS); instead, Gln-tRNA(Gln) is produced via an indirect pathway: a glutamyl-tRNA synthetase (GluRS) first... Full description

Journal Title: Nucleic acids research September 2012, Vol.40(16), pp.7967-74
Main Author: Guo, Li-Tao
Other Authors: Helgadóttir, Sunna , Söll, Dieter , Ling, Jiqiang
Format: Electronic Article Electronic Article
Language: English
Subjects:
ID: E-ISSN: 1362-4962 ; PMID: 22661575 Version:1 ; DOI: 10.1093/nar/gks507
Link: http://pubmed.gov/22661575
Zum Text:
SendSend as email Add to Book BagAdd to Book Bag
Staff View
recordid: medline22661575
title: Rational design and directed evolution of a bacterial-type glutaminyl-tRNA synthetase precursor
format: Article
creator:
  • Guo, Li-Tao
  • Helgadóttir, Sunna
  • Söll, Dieter
  • Ling, Jiqiang
subjects:
  • Amino Acyl-Trna Synthetases -- Chemistry
  • Glutamate-Trna Ligase -- Chemistry
ispartof: Nucleic acids research, September 2012, Vol.40(16), pp.7967-74
description: Protein biosynthesis requires aminoacyl-transfer RNA (tRNA) synthetases to provide aminoacyl-tRNA substrates for the ribosome. Most bacteria and all archaea lack a glutaminyl-tRNA synthetase (GlnRS); instead, Gln-tRNA(Gln) is produced via an indirect pathway: a glutamyl-tRNA synthetase (GluRS) first attaches glutamate (Glu) to tRNA(Gln), and an amidotransferase converts Glu-tRNA(Gln) to Gln-tRNA(Gln). The human pathogen Helicobacter pylori encodes two GluRS enzymes, with GluRS2 specifically aminoacylating Glu onto tRNA(Gln). It was proposed that GluRS2 is evolving into a bacterial-type GlnRS. Herein, we have combined rational design and directed evolution approaches to test this hypothesis. We show that, in contrast to wild-type (WT) GlnRS2, an engineered enzyme variant (M110) with seven amino acid changes is able to rescue growth of the temperature-sensitive Escherichia coli glnS strain UT172 at its non-permissive temperature. In vitro kinetic analyses reveal that WT GluRS2 selectively...
language: eng
source:
identifier: E-ISSN: 1362-4962 ; PMID: 22661575 Version:1 ; DOI: 10.1093/nar/gks507
fulltext: fulltext
issn:
  • 13624962
  • 1362-4962
url: Link


@attributes
ID1168745293
RANK0.07
NO1
SEARCH_ENGINEprimo_central_multiple_fe
SEARCH_ENGINE_TYPEPrimo Central Search Engine
LOCALfalse
PrimoNMBib
record
control
sourcerecordid22661575
sourceidmedline
recordidTN_medline22661575
sourceformatXML
sourcesystemPC
pqid1039886678
display
typearticle
titleRational design and directed evolution of a bacterial-type glutaminyl-tRNA synthetase precursor
creatorGuo, Li-Tao ; Helgadóttir, Sunna ; Söll, Dieter ; Ling, Jiqiang
ispartofNucleic acids research, September 2012, Vol.40(16), pp.7967-74
identifier
subjectAmino Acyl-Trna Synthetases -- Chemistry ; Glutamate-Trna Ligase -- Chemistry
descriptionProtein biosynthesis requires aminoacyl-transfer RNA (tRNA) synthetases to provide aminoacyl-tRNA substrates for the ribosome. Most bacteria and all archaea lack a glutaminyl-tRNA synthetase (GlnRS); instead, Gln-tRNA(Gln) is produced via an indirect pathway: a glutamyl-tRNA synthetase (GluRS) first attaches glutamate (Glu) to tRNA(Gln), and an amidotransferase converts Glu-tRNA(Gln) to Gln-tRNA(Gln). The human pathogen Helicobacter pylori encodes two GluRS enzymes, with GluRS2 specifically aminoacylating Glu onto tRNA(Gln). It was proposed that GluRS2 is evolving into a bacterial-type GlnRS. Herein, we have combined rational design and directed evolution approaches to test this hypothesis. We show that, in contrast to wild-type (WT) GlnRS2, an engineered enzyme variant (M110) with seven amino acid changes is able to rescue growth of the temperature-sensitive Escherichia coli glnS strain UT172 at its non-permissive temperature. In vitro kinetic analyses reveal that WT GluRS2 selectively...
languageeng
source
version4
lds50peer_reviewed
links
openurl$$Topenurl_article
backlink$$Uhttp://pubmed.gov/22661575$$EView_this_record_in_MEDLINE/PubMed
openurlfulltext$$Topenurlfull_article
addlink$$Uhttp://exlibris-pub.s3.amazonaws.com/aboutMedline.html$$EView_the_MEDLINE/PubMed_Copyright_Statement
search
creatorcontrib
0Guo, Li-Tao
1Helgadóttir, Sunna
2Söll, Dieter
3Ling, Jiqiang
titleRational design and directed evolution of a bacterial-type glutaminyl-tRNA synthetase precursor
descriptionProtein biosynthesis requires aminoacyl-transfer RNA (tRNA) synthetases to provide aminoacyl-tRNA substrates for the ribosome. Most bacteria and all archaea lack a glutaminyl-tRNA synthetase (GlnRS); instead, Gln-tRNA(Gln) is produced via an indirect pathway: a glutamyl-tRNA synthetase (GluRS) first attaches glutamate (Glu) to tRNA(Gln), and an amidotransferase converts Glu-tRNA(Gln) to Gln-tRNA(Gln). The human pathogen Helicobacter pylori encodes two GluRS enzymes, with GluRS2 specifically aminoacylating Glu onto tRNA(Gln). It was proposed that GluRS2 is evolving into a bacterial-type GlnRS. Herein, we have combined rational design and directed evolution approaches to test this hypothesis. We show that, in contrast to wild-type (WT) GlnRS2, an engineered enzyme variant (M110) with seven amino acid changes is able to rescue growth of the temperature-sensitive Escherichia coli glnS strain UT172 at its non-permissive temperature. In vitro kinetic analyses reveal that WT GluRS2 selectively...
subject
0Amino Acyl-Trna Synthetases -- Chemistry
1Glutamate-Trna Ligase -- Chemistry
general
022661575
1English
2MEDLINE/PubMed (U.S. National Library of Medicine)
310.1093/nar/gks507
4MEDLINE/PubMed (NLM)
sourceidmedline
recordidmedline22661575
issn
013624962
11362-4962
rsrctypearticle
creationdate2012
addtitleNucleic acids research
searchscope
0medline
1nlm_medline
2MEDLINE
scope
0medline
1nlm_medline
2MEDLINE
lsr41201209
citationpf 7967 vol 40 issue 16
startdate20120901
enddate20120931
lsr30VSR-Enriched:[pages, pqid]
sort
titleRational design and directed evolution of a bacterial-type glutaminyl-tRNA synthetase precursor
authorGuo, Li-Tao ; Helgadóttir, Sunna ; Söll, Dieter ; Ling, Jiqiang
creationdate20120900
lso0120120900
facets
frbrgroupid6298712713609367416
frbrtype5
newrecords20190701
languageeng
creationdate2012
topic
0Amino Acyl-Trna Synthetases–Chemistry
1Glutamate-Trna Ligase–Chemistry
collectionMEDLINE/PubMed (NLM)
prefilterarticles
rsrctypearticles
creatorcontrib
0Guo, Li-Tao
1Helgadóttir, Sunna
2Söll, Dieter
3Ling, Jiqiang
jtitleNucleic Acids Research
toplevelpeer_reviewed
delivery
delcategoryRemote Search Resource
fulltextfulltext
addata
aulast
0Guo
1Helgadóttir
2Söll
3Ling
aufirst
0Li-Tao
1Sunna
2Dieter
3Jiqiang
au
0Guo, Li-Tao
1Helgadóttir, Sunna
2Söll, Dieter
3Ling, Jiqiang
atitleRational design and directed evolution of a bacterial-type glutaminyl-tRNA synthetase precursor
jtitleNucleic acids research
risdate201209
volume40
issue16
spage7967
pages7967-7974
issn0305-1048
eissn1362-4962
formatjournal
genrearticle
ristypeJOUR
abstractProtein biosynthesis requires aminoacyl-transfer RNA (tRNA) synthetases to provide aminoacyl-tRNA substrates for the ribosome. Most bacteria and all archaea lack a glutaminyl-tRNA synthetase (GlnRS); instead, Gln-tRNA(Gln) is produced via an indirect pathway: a glutamyl-tRNA synthetase (GluRS) first attaches glutamate (Glu) to tRNA(Gln), and an amidotransferase converts Glu-tRNA(Gln) to Gln-tRNA(Gln). The human pathogen Helicobacter pylori encodes two GluRS enzymes, with GluRS2 specifically aminoacylating Glu onto tRNA(Gln). It was proposed that GluRS2 is evolving into a bacterial-type GlnRS. Herein, we have combined rational design and directed evolution approaches to test this hypothesis. We show that, in contrast to wild-type (WT) GlnRS2, an engineered enzyme variant (M110) with seven amino acid changes is able to rescue growth of the temperature-sensitive Escherichia coli glnS strain UT172 at its non-permissive temperature. In vitro kinetic analyses reveal that WT GluRS2 selectively...
doi10.1093/nar/gks507
pmid22661575
date2012-09