Degradation of nanoRNA is performed by multiple redundant RNases in Bacillus subtilis
Identifieur interne : 000F43 ( Pmc/Curation ); précédent : 000F42; suivant : 000F44Degradation of nanoRNA is performed by multiple redundant RNases in Bacillus subtilis
Auteurs : Ming Fang ; Wencke-Maria Zeisberg ; Ciaran Condon [France] ; Vasily Ogryzko [France] ; Antoine Danchin ; Undine MecholdSource :
- Nucleic Acids Research [ 0305-1048 ] ; 2009.
Abstract
Url:
DOI: 10.1093/nar/gkp527
PubMed: 19553197
PubMed Central: 2731908
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Ming Fang<affiliation><nlm:aff 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 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 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 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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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Degradation of nanoRNA is performed by multiple redundant RNases in <italic>Bacillus subtilis</italic>
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<author><name sortKey="Zeisberg, Wencke Maria" sort="Zeisberg, Wencke Maria" uniqKey="Zeisberg W" first="Wencke-Maria" last="Zeisberg">Wencke-Maria Zeisberg</name>
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<author><name sortKey="Condon, Ciaran" sort="Condon, Ciaran" uniqKey="Condon C" first="Ciaran" last="Condon">Ciaran Condon</name>
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<author><name sortKey="Mechold, Undine" sort="Mechold, Undine" uniqKey="Mechold U" first="Undine" last="Mechold">Undine Mechold</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="2009">2009</date>
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<front><div type="abstract" xml:lang="en"><p><italic>Escherichia coli</italic>
possesses only one essential oligoribonuclease (Orn), an enzyme that can degrade oligoribonucleotides of five residues and shorter in length (nanoRNA). Firmicutes including <italic>Bacillus subtilis</italic>
do not have an Orn homolog. We had previously identified YtqI (NrnA) as functional analog of Orn in <italic>B. subtilis</italic>
. Screening a genomic library from <italic>B. subtilis</italic>
for genes that can complement a conditional <italic>orn</italic>
mutant, we identify here YngD (NrnB) as a second nanoRNase in <italic>B. subtilis</italic>
. Like NrnA, NrnB is a member of the DHH/DHHA1 protein family of phosphoesterases. NrnB degrades nanoRNA 5-mers <italic>in vitro</italic>
similarily to Orn. Low expression levels of NrnB are sufficient for <italic>orn</italic>
complementation. YhaM, a known RNase present in <italic>B. subtilis</italic>
, degrades nanoRNA efficiently <italic>in vitro</italic>
but requires high levels of expression for only partial complementation of the <italic>orn<sup>–</sup>
</italic>
strain. A triple mutant (<italic>nrnA</italic>
<sup>–</sup>
, <italic>nrnB</italic>
<sup>–</sup>
, <italic>yhaM</italic>
<sup>–</sup>
) in <italic>B. subtilis</italic>
is viable and shows almost no impairment in growth. Lastly, RNase J1 seems also to have some 5′-to-3′ exoribonuclease activity on nanoRNA and thus can potentially finish degradation of RNA. We conclude that, unlike in <italic>E. coli</italic>
, degradation of nanoRNA is performed in a redundant fashion in <italic>B. subtilis</italic>
.</p>
</div>
</front>
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</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">19553197</article-id>
<article-id pub-id-type="pmc">2731908</article-id>
<article-id pub-id-type="doi">10.1093/nar/gkp527</article-id>
<article-id pub-id-type="publisher-id">gkp527</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Nucleic Acid Enzymes</subject>
</subj-group>
</article-categories>
<title-group><article-title>Degradation of nanoRNA is performed by multiple redundant RNases in <italic>Bacillus subtilis</italic>
</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Fang</surname>
<given-names>Ming</given-names>
</name>
<xref ref-type="aff" rid="AFF1"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Zeisberg</surname>
<given-names>Wencke-Maria</given-names>
</name>
<xref ref-type="aff" rid="AFF1"><sup>1</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Condon</surname>
<given-names>Ciaran</given-names>
</name>
<xref ref-type="aff" rid="AFF1"><sup>2</sup>
</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Ogryzko</surname>
<given-names>Vasily</given-names>
</name>
<xref ref-type="aff" rid="AFF1"><sup>3</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 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-group>
<aff id="AFF1"><sup>1</sup>
Institut Pasteur, URA 2171, Unité de Génétique des Génomes Bactériens, 75724 Paris Cedex 15,<sup>2</sup>
Institut de Biologie Physico-Chimique, CNRS UPR 9073, 75005 Paris and<sup>3</sup>
Institut Gustave Roussy, UMR 8126, Unité d’ Interactions Moléculaires et Cancer, 94805 Villejuif, France</aff>
<author-notes><corresp id="COR1">*To whom correspondence should be addressed. Tel: <phone>+33 14 0613870</phone>
; Fax: <fax>+33 14 5688948</fax>
; Email: <email>undine.mechold@pasteur.fr</email>
</corresp>
</author-notes>
<pub-date pub-type="ppub"><month>8</month>
<year>2009</year>
</pub-date>
<pub-date pub-type="epub"><day>24</day>
<month>6</month>
<year>2009</year>
</pub-date>
<pub-date pub-type="pmc-release"><day>24</day>
<month>6</month>
<year>2009</year>
</pub-date>
<pmc-comment> PMC Release delay is 0 months and 0 days and was based on the
. </pmc-comment>
<volume>37</volume>
<issue>15</issue>
<fpage>5114</fpage>
<lpage>5125</lpage>
<history><date date-type="received"><day>28</day>
<month>1</month>
<year>2009</year>
</date>
<date date-type="rev-recd"><day>30</day>
<month>4</month>
<year>2009</year>
</date>
<date date-type="accepted"><day>3</day>
<month>6</month>
<year>2009</year>
</date>
</history>
<permissions><copyright-statement>© 2009 The Author(s)</copyright-statement>
<copyright-year>2009</copyright-year>
<license license-type="creative-commons" 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><italic>Escherichia coli</italic>
possesses only one essential oligoribonuclease (Orn), an enzyme that can degrade oligoribonucleotides of five residues and shorter in length (nanoRNA). Firmicutes including <italic>Bacillus subtilis</italic>
do not have an Orn homolog. We had previously identified YtqI (NrnA) as functional analog of Orn in <italic>B. subtilis</italic>
. Screening a genomic library from <italic>B. subtilis</italic>
for genes that can complement a conditional <italic>orn</italic>
mutant, we identify here YngD (NrnB) as a second nanoRNase in <italic>B. subtilis</italic>
. Like NrnA, NrnB is a member of the DHH/DHHA1 protein family of phosphoesterases. NrnB degrades nanoRNA 5-mers <italic>in vitro</italic>
similarily to Orn. Low expression levels of NrnB are sufficient for <italic>orn</italic>
complementation. YhaM, a known RNase present in <italic>B. subtilis</italic>
, degrades nanoRNA efficiently <italic>in vitro</italic>
but requires high levels of expression for only partial complementation of the <italic>orn<sup>–</sup>
</italic>
strain. A triple mutant (<italic>nrnA</italic>
<sup>–</sup>
, <italic>nrnB</italic>
<sup>–</sup>
, <italic>yhaM</italic>
<sup>–</sup>
) in <italic>B. subtilis</italic>
is viable and shows almost no impairment in growth. Lastly, RNase J1 seems also to have some 5′-to-3′ exoribonuclease activity on nanoRNA and thus can potentially finish degradation of RNA. We conclude that, unlike in <italic>E. coli</italic>
, degradation of nanoRNA is performed in a redundant fashion in <italic>B. subtilis</italic>
.</p>
</abstract>
</article-meta>
</front>
</pmc>
</record>
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