Expression analysis of the nrdHIEF operon from Escherichia coli. Conditions that trigger the transcript level in vivo.
Identifieur interne : 001032 ( Main/Exploration ); précédent : 001031; suivant : 001033Expression analysis of the nrdHIEF operon from Escherichia coli. Conditions that trigger the transcript level in vivo.
Auteurs : F. Monje-Casas [Espagne] ; J. Jurado ; M J Prieto-Alamo ; A. Holmgren ; C. PueyoSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 2001.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , genetics : Ribonucleotide Reductases.
- genetics : Escherichia coli, Operon.
- Gene Expression Regulation, Bacterial, Transcription, Genetic.
Abstract
Escherichia coli has two aerobic ribonucleotide reductases encoded by the nrdAB and nrdHIEF operons. While NrdAB is active during aerobiosis, NrdEF is considered a cryptic enzyme with no obvious function. Here, we present evidence that nrdHIEF expression might be important under certain circumstances. Basal transcript levels were dramatically enhanced (25-75-fold), depending on the growth-phase and the growth-medium composition. Likewise, a large increase of >100-fold in nrdHIEF mRNA was observed in bacteria lacking Trx1 and Grx1, the two main NrdAB reductants. Moreover, nrdHIEF expression was triggered in response to oxidative stress, particularly in mutants missing hydroperoxidase I and alkyl-hydroperoxide reductase activities (69.7-fold) and in cells treated with oxidants (up to 23.4-fold over the enhanced transcript level possessed by cells grown on minimal medium). The mechanism(s) that triggers nrdHIEF expression remains unknown, but our findings exclude putative global regulators like RpoS, Fis, cAMP, OxyR, SoxR/S, or RecA. What we have learned about nrdHIEF expression indicates strong differences between its regulation and that of the nrdAB operon and of genes coding for components of both thioredoxin/glutaredoxin pathways. We propose that E. coli might optimize the responses to different stimuli by co-evolving the expression levels for its multiple reductases and electron donors.
DOI: 10.1074/jbc.M011728200
PubMed: 11278973
Affiliations:
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Le document en format XML
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While NrdAB is active during aerobiosis, NrdEF is considered a cryptic enzyme with no obvious function. Here, we present evidence that nrdHIEF expression might be important under certain circumstances. Basal transcript levels were dramatically enhanced (25-75-fold), depending on the growth-phase and the growth-medium composition. Likewise, a large increase of >100-fold in nrdHIEF mRNA was observed in bacteria lacking Trx1 and Grx1, the two main NrdAB reductants. Moreover, nrdHIEF expression was triggered in response to oxidative stress, particularly in mutants missing hydroperoxidase I and alkyl-hydroperoxide reductase activities (69.7-fold) and in cells treated with oxidants (up to 23.4-fold over the enhanced transcript level possessed by cells grown on minimal medium). The mechanism(s) that triggers nrdHIEF expression remains unknown, but our findings exclude putative global regulators like RpoS, Fis, cAMP, OxyR, SoxR/S, or RecA. What we have learned about nrdHIEF expression indicates strong differences between its regulation and that of the nrdAB operon and of genes coding for components of both thioredoxin/glutaredoxin pathways. We propose that E. coli might optimize the responses to different stimuli by co-evolving the expression levels for its multiple reductases and electron donors.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">11278973</PMID><DateCompleted><Year>2001</Year><Month>07</Month><Day>05</Day></DateCompleted><DateRevised><Year>2006</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>276</Volume><Issue>21</Issue><PubDate><Year>2001</Year><Month>May</Month><Day>25</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>Expression analysis of the nrdHIEF operon from Escherichia coli. Conditions that trigger the transcript level in vivo.</ArticleTitle><Pagination><MedlinePgn>18031-7</MedlinePgn></Pagination><Abstract><AbstractText>Escherichia coli has two aerobic ribonucleotide reductases encoded by the nrdAB and nrdHIEF operons. While NrdAB is active during aerobiosis, NrdEF is considered a cryptic enzyme with no obvious function. Here, we present evidence that nrdHIEF expression might be important under certain circumstances. Basal transcript levels were dramatically enhanced (25-75-fold), depending on the growth-phase and the growth-medium composition. Likewise, a large increase of >100-fold in nrdHIEF mRNA was observed in bacteria lacking Trx1 and Grx1, the two main NrdAB reductants. Moreover, nrdHIEF expression was triggered in response to oxidative stress, particularly in mutants missing hydroperoxidase I and alkyl-hydroperoxide reductase activities (69.7-fold) and in cells treated with oxidants (up to 23.4-fold over the enhanced transcript level possessed by cells grown on minimal medium). The mechanism(s) that triggers nrdHIEF expression remains unknown, but our findings exclude putative global regulators like RpoS, Fis, cAMP, OxyR, SoxR/S, or RecA. What we have learned about nrdHIEF expression indicates strong differences between its regulation and that of the nrdAB operon and of genes coding for components of both thioredoxin/glutaredoxin pathways. We propose that E. coli might optimize the responses to different stimuli by co-evolving the expression levels for its multiple reductases and electron donors.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Monje-Casas</LastName><ForeName>F</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Departamento de Bioquimica y Biologia Molecular, Universidad de Córdoba, 14071-Córdoba, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jurado</LastName><ForeName>J</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Prieto-Alamo</LastName><ForeName>M J</ForeName><Initials>MJ</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Pueyo</LastName><ForeName>C</ForeName><Initials>C</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2001</Year><Month>02</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Biol Chem</MedlineTA><NlmUniqueID>2985121R</NlmUniqueID><ISSNLinking>0021-9258</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 1.17.4.-</RegistryNumber><NameOfSubstance UI="D012264">Ribonucleotide Reductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015964" MajorTopicYN="Y">Gene Expression Regulation, Bacterial</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009876" MajorTopicYN="N">Operon</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012264" MajorTopicYN="N">Ribonucleotide Reductases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014158" MajorTopicYN="N">Transcription, Genetic</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2001</Year><Month>3</Month><Day>30</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2001</Year><Month>7</Month><Day>6</Day><Hour>10</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2001</Year><Month>3</Month><Day>30</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">11278973</ArticleId><ArticleId IdType="doi">10.1074/jbc.M011728200</ArticleId><ArticleId IdType="pii">M011728200</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Andalousie</li></region></list><tree><noCountry><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Jurado, J" sort="Jurado, J" uniqKey="Jurado J" first="J" last="Jurado">J. Jurado</name><name sortKey="Prieto Alamo, M J" sort="Prieto Alamo, M J" uniqKey="Prieto Alamo M" first="M J" last="Prieto-Alamo">M J Prieto-Alamo</name><name sortKey="Pueyo, C" sort="Pueyo, C" uniqKey="Pueyo C" first="C" last="Pueyo">C. Pueyo</name></noCountry><country name="Espagne"><region name="Andalousie"><name sortKey="Monje Casas, F" sort="Monje Casas, F" uniqKey="Monje Casas F" first="F" last="Monje-Casas">F. Monje-Casas</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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