YtqI from Bacillus subtilis has both oligoribonuclease and pAp-phosphatase activity
Identifieur interne : 000F40 ( Pmc/Curation ); précédent : 000F39; suivant : 000F41YtqI 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.
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>
<wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry>
</affiliation>
<affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff>
<wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry>
</affiliation>
<affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff>
<wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry>
</affiliation>
<affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff>
<wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry>
</affiliation>
Le document en format XML
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has both oligoribonuclease and pAp-phosphatase activity</title>
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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>
<author><name sortKey="Mechold, Undine" sort="Mechold, Undine" uniqKey="Mechold U" first="Undine" last="Mechold">Undine Mechold</name>
<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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<author><name sortKey="Fang, Gang" sort="Fang, Gang" uniqKey="Fang G" first="Gang" last="Fang">Gang Fang</name>
<affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff>
<wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry>
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<author><name sortKey="Ngo, Saravuth" sort="Ngo, Saravuth" uniqKey="Ngo S" first="Saravuth" last="Ngo">Saravuth Ngo</name>
<affiliation><nlm:aff wicri:cut=" and" id="AFF1">Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15</nlm:aff>
<wicri:noCountry code="subfield">75724 Paris Cedex 15</wicri:noCountry>
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<author><name sortKey="Ogryzko, Vasily" sort="Ogryzko, Vasily" uniqKey="Ogryzko V" first="Vasily" last="Ogryzko">Vasily Ogryzko</name>
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<country xml:lang="fr">France</country>
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<author><name sortKey="Danchin, Antoine" sort="Danchin, Antoine" uniqKey="Danchin A" first="Antoine" last="Danchin">Antoine Danchin</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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<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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</back>
</TEI>
<pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">Nucleic Acids Res</journal-id>
<journal-id journal-id-type="iso-abbrev">Nucleic Acids Res</journal-id>
<journal-id journal-id-type="publisher-id">nar</journal-id>
<journal-id journal-id-type="hwp">nar</journal-id>
<journal-title-group><journal-title>Nucleic Acids Research</journal-title>
</journal-title-group>
<issn pub-type="ppub">0305-1048</issn>
<issn pub-type="epub">1362-4962</issn>
<publisher><publisher-name>Oxford University Press</publisher-name>
</publisher>
</journal-meta>
<article-meta><article-id pub-id-type="pmid">17586819</article-id>
<article-id pub-id-type="pmc">1935014</article-id>
<article-id pub-id-type="doi">10.1093/nar/gkm462</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Nucleic Acid Enzymes</subject>
</subj-group>
</article-categories>
<title-group><article-title>YtqI from <italic>Bacillus subtilis</italic>
has both oligoribonuclease and pAp-phosphatase activity</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Mechold</surname>
<given-names>Undine</given-names>
</name>
<xref ref-type="aff" rid="AFF1"><sup>1</sup>
</xref>
<xref ref-type="corresp" rid="COR1">*</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Fang</surname>
<given-names>Gang</given-names>
</name>
<xref ref-type="aff" rid="AFF1"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Ngo</surname>
<given-names>Saravuth</given-names>
</name>
<xref ref-type="aff" rid="AFF1"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Ogryzko</surname>
<given-names>Vasily</given-names>
</name>
<xref ref-type="aff" rid="AFF1"><sup>2</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Danchin</surname>
<given-names>Antoine</given-names>
</name>
<xref ref-type="aff" rid="AFF1"><sup>1</sup>
</xref>
</contrib>
</contrib-group>
<aff id="AFF1"><sup>1</sup>
Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15 and<sup>2</sup>
Institut Gustave Roussy, UMR 8126, Unité Interactions Moléculaires et Cancer, 94805 Villejuif, France</aff>
<author-notes><corresp id="COR1">*To whom correspondence should be addressed. <phone>33 140613870</phone>
<fax>33 145688948</fax>
<email>umechold@pasteur.fr</email>
</corresp>
</author-notes>
<pub-date pub-type="ppub"><month>7</month>
<year>2007</year>
</pub-date>
<pub-date pub-type="epub"><day>22</day>
<month>6</month>
<year>2007</year>
</pub-date>
<pub-date pub-type="pmc-release"><day>22</day>
<month>6</month>
<year>2007</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
. </pmc-comment>
<volume>35</volume>
<issue>13</issue>
<fpage>4552</fpage>
<lpage>4561</lpage>
<history><date date-type="received"><day>2</day>
<month>4</month>
<year>2007</year>
</date>
<date date-type="rev-recd"><day>25</day>
<month>5</month>
<year>2007</year>
</date>
<date date-type="accepted"><day>25</day>
<month>5</month>
<year>2007</year>
</date>
</history>
<permissions><copyright-statement>© 2007 The Author(s)</copyright-statement>
<copyright-year>2007</copyright-year>
<license license-type="open-access" xlink:href="http://creativecommons.org/licenses/by-nc/2.0/uk/"><license-p><pmc-comment>CREATIVE COMMONS</pmc-comment>
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (<ext-link ext-link-type="uri" xlink:href="http://creativecommons.org/licenses/by-nc/2.0/uk/">http://creativecommons.org/licenses/by-nc/2.0/uk/</ext-link>
) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.</license-p>
</license>
</permissions>
<abstract><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>
</abstract>
</article-meta>
</front>
</pmc>
</record>
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