YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity
Identifieur interne : 000529 ( Ncbi/Curation ); précédent : 000528; suivant : 000530YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity
Auteurs : Undine Mechold ; Gang Fang ; Saravuth Ngo ; Vasily Ogryzko [France] ; Antoine DanchinSource :
- Nucleic Acids Research [ 0305-1048 ] ; 2007.
Descripteurs français
- KwdFr :
- ADP (métabolisme), ARN (métabolisme), Bacillus subtilis (enzymologie), Escherichia coli (génétique), Exoribonucleases (génétique), Exoribonucleases (métabolisme), Phosphoric monoester hydrolases (génétique), Phosphoric monoester hydrolases (métabolisme), Phylogénie, Protéines bactériennes (), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Spécificité du substrat, Test de complémentation.
- MESH :
- enzymologie : Bacillus subtilis.
- génétique : Escherichia coli, Exoribonucleases, Phosphoric monoester hydrolases, Protéines bactériennes.
- métabolisme : ADP, ARN, Exoribonucleases, Phosphoric monoester hydrolases, Protéines bactériennes.
- Phylogénie, Protéines bactériennes, Spécificité du substrat, Test de complémentation.
English descriptors
- KwdEn :
- Adenosine Diphosphate (metabolism), Bacillus subtilis (enzymology), Bacterial Proteins (classification), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Escherichia coli (genetics), Exoribonucleases (genetics), Exoribonucleases (metabolism), Genetic Complementation Test, Phosphoric Monoester Hydrolases (genetics), Phosphoric Monoester Hydrolases (metabolism), Phylogeny, RNA (metabolism), Substrate Specificity.
- MESH :
- chemical , classification : Bacterial Proteins.
- chemical , genetics : Bacterial Proteins, Exoribonucleases, Phosphoric Monoester Hydrolases.
- chemical , metabolism : Adenosine Diphosphate, Bacterial Proteins, Exoribonucleases, Phosphoric Monoester Hydrolases, RNA.
- enzymology : Bacillus subtilis.
- genetics : Escherichia coli.
- Genetic Complementation Test, Phylogeny, Substrate Specificity.
Abstract
Oligoribonuclease is the only RNase in
Url:
DOI: 10.1093/nar/gkm462
PubMed: 17586819
PubMed Central: 1935014
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Undine Mechold<affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff>
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Le document en format XML
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">YtqI from <italic>Bacillus subtilis</italic>
has both oligoribonuclease and pAp-phosphatase activity</title>
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<author><name sortKey="Fang, Gang" sort="Fang, Gang" uniqKey="Fang G" first="Gang" last="Fang">Gang Fang</name>
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<series><title level="j">Nucleic Acids Research</title>
<idno type="ISSN">0305-1048</idno>
<idno type="eISSN">1362-4962</idno>
<imprint><date when="2007">2007</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Diphosphate (metabolism)</term>
<term>Bacillus subtilis (enzymology)</term>
<term>Bacterial Proteins (classification)</term>
<term>Bacterial Proteins (genetics)</term>
<term>Bacterial Proteins (metabolism)</term>
<term>Escherichia coli (genetics)</term>
<term>Exoribonucleases (genetics)</term>
<term>Exoribonucleases (metabolism)</term>
<term>Genetic Complementation Test</term>
<term>Phosphoric Monoester Hydrolases (genetics)</term>
<term>Phosphoric Monoester Hydrolases (metabolism)</term>
<term>Phylogeny</term>
<term>RNA (metabolism)</term>
<term>Substrate Specificity</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>ADP (métabolisme)</term>
<term>ARN (métabolisme)</term>
<term>Bacillus subtilis (enzymologie)</term>
<term>Escherichia coli (génétique)</term>
<term>Exoribonucleases (génétique)</term>
<term>Exoribonucleases (métabolisme)</term>
<term>Phosphoric monoester hydrolases (génétique)</term>
<term>Phosphoric monoester hydrolases (métabolisme)</term>
<term>Phylogénie</term>
<term>Protéines bactériennes ()</term>
<term>Protéines bactériennes (génétique)</term>
<term>Protéines bactériennes (métabolisme)</term>
<term>Spécificité du substrat</term>
<term>Test de complémentation</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="classification" xml:lang="en"><term>Bacterial Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term>
<term>Exoribonucleases</term>
<term>Phosphoric Monoester Hydrolases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Adenosine Diphosphate</term>
<term>Bacterial Proteins</term>
<term>Exoribonucleases</term>
<term>Phosphoric Monoester Hydrolases</term>
<term>RNA</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Bacillus subtilis</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Bacillus subtilis</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term>
<term>Exoribonucleases</term>
<term>Phosphoric monoester hydrolases</term>
<term>Protéines bactériennes</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>ADP</term>
<term>ARN</term>
<term>Exoribonucleases</term>
<term>Phosphoric monoester hydrolases</term>
<term>Protéines bactériennes</term>
</keywords>
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<term>Phylogeny</term>
<term>Substrate Specificity</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Phylogénie</term>
<term>Protéines bactériennes</term>
<term>Spécificité du substrat</term>
<term>Test de complémentation</term>
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<front><div type="abstract" xml:lang="en"><p>Oligoribonuclease is the only RNase in <italic>Escherichia coli</italic>
that is able to degrade RNA oligonucleotides five residues and shorter in length. Firmicutes including <italic>Bacillus subtilis</italic>
do not have an Oligoribonuclease (Orn) homologous protein and it is not yet understood which proteins accomplish the equivalent function in these organisms. We had previously identified oligoribonucleases Orn from <italic>E. coli</italic>
and its human homolog Sfn in a screen for proteins that are regulated by 3′-phosphoadenosine 5′-phosphate (pAp). Here, we identify YtqI as a potential functional analog of Orn through its interaction with pAp. YtqI degrades RNA oligonucleotides <italic>in vitro</italic>
with preference for 3-mers. In addition, YtqI has pAp-phosphatase activity <italic>in vitro</italic>
. In agreement with these data, YtqI is able to complement both <italic>orn</italic>
and <italic>cysQ</italic>
mutants in <italic>E. coli</italic>
. An <italic>ytqI</italic>
mutant in <italic>B. subtilis</italic>
shows impairment of growth in the absence of cysteine, a phenotype resembling that of a <italic>cysQ</italic>
mutant in <italic>E. coli</italic>
. Phylogenetic distribution of YtqI, Orn and CysQ supports bifunctionality of YtqI.</p>
</div>
</front>
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</author>
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</author>
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