The ribonucleotide reductase system of Lactococcus lactis. Characterization of an NrdEF enzyme and a new electron transport protein.
Identifieur interne : 001187 ( Main/Exploration ); précédent : 001186; suivant : 001188The ribonucleotide reductase system of Lactococcus lactis. Characterization of an NrdEF enzyme and a new electron transport protein.
Auteurs : A. Jordan [Suède] ; E. Pontis ; F. Aslund ; U. Hellman ; I. Gibert ; P. ReichardSource :
- The Journal of biological chemistry [ 0021-9258 ] ; 1996.
Descripteurs français
- KwdFr :
- ADN bactérien (génétique), Alignement de séquences (MeSH), Données de séquences moléculaires (MeSH), Fragments peptidiques (composition chimique), Glutarédoxines (MeSH), Gènes bactériens (MeSH), Lactococcus lactis (métabolisme), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Protéines (composition chimique), Protéines bactériennes (composition chimique), Ribonucleotide reductases (composition chimique), Ribonucleotide reductases (génétique), Ribonucleotide reductases (métabolisme), Similitude de séquences d'acides aminés (MeSH), Séquence consensus (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
- MESH :
- composition chimique : Fragments peptidiques, Protéines, Protéines bactériennes, Ribonucleotide reductases.
- génétique : ADN bactérien, Ribonucleotide reductases.
- métabolisme : Lactococcus lactis, Ribonucleotide reductases.
- Alignement de séquences, Données de séquences moléculaires, Glutarédoxines, Gènes bactériens, Oxidoreductases, Oxydoréduction, Similitude de séquences d'acides aminés, Séquence consensus, Séquence d'acides aminés, Séquence nucléotidique.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Bacterial Proteins (chemistry), Base Sequence (MeSH), Consensus Sequence (MeSH), DNA, Bacterial (genetics), Genes, Bacterial (MeSH), Glutaredoxins (MeSH), Lactococcus lactis (metabolism), Molecular Sequence Data (MeSH), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Peptide Fragments (chemistry), Proteins (chemistry), Ribonucleotide Reductases (chemistry), Ribonucleotide Reductases (genetics), Ribonucleotide Reductases (metabolism), Sequence Alignment (MeSH), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , chemistry : Bacterial Proteins, Peptide Fragments, Proteins, Ribonucleotide Reductases.
- chemical , genetics : DNA, Bacterial, Ribonucleotide Reductases.
- metabolism : Lactococcus lactis, Ribonucleotide Reductases.
- Amino Acid Sequence, Base Sequence, Consensus Sequence, Genes, Bacterial, Glutaredoxins, Molecular Sequence Data, Oxidation-Reduction, Oxidoreductases, Sequence Alignment, Sequence Homology, Amino Acid.
Abstract
Escherichia coli contains the genetic information for three separate ribonucleotide reductases. Two of them (class I enzymes), coded by the nrdAB and nrdEF genes, respectively, contain a tyrosyl radical, whose generation requires oxygen. The NrdAB enzyme is physiologically active. The function of the nrdEF gene is not known. The third enzyme (class III), coded by nrdDG, operates during anaerobiosis. The DNA of Lactococcus lactis contains sequences homologous to the nrdDG genes. Surprisingly, an nrdD- mutant of L. lactis grew well under standard anaerobic growth conditions. The ribonucleotide reductase system of this mutant was shown to consist of an enzyme of the NrdEF-type and a small electron transport protein. The coding operon contains the nrdEF genes and two open reading frames, one of which (nrdH) codes for the small protein. The same gene organization is present in E. coli. We propose that the aerobic class I ribonucleotide reductases contain two subclasses, one coded by nrdAB, active in E. coli and eukaryotes (class Ia), the other coded by nrdEF, present in various microorganisms (class Ib). The NrdEF enzymes use NrdH proteins as electron transporter in place of thioredoxin or glutaredoxin used by NrdAB enzymes. The two classes also differ in their allosteric regulation by dATP.
DOI: 10.1074/jbc.271.15.8779
PubMed: 8621514
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Aslund</name></author><author><name sortKey="Hellman, U" sort="Hellman, U" uniqKey="Hellman U" first="U" last="Hellman">U. Hellman</name></author><author><name sortKey="Gibert, I" sort="Gibert, I" uniqKey="Gibert I" first="I" last="Gibert">I. Gibert</name></author><author><name sortKey="Reichard, P" sort="Reichard, P" uniqKey="Reichard P" first="P" last="Reichard">P. 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Two of them (class I enzymes), coded by the nrdAB and nrdEF genes, respectively, contain a tyrosyl radical, whose generation requires oxygen. The NrdAB enzyme is physiologically active. The function of the nrdEF gene is not known. The third enzyme (class III), coded by nrdDG, operates during anaerobiosis. The DNA of Lactococcus lactis contains sequences homologous to the nrdDG genes. Surprisingly, an nrdD- mutant of L. lactis grew well under standard anaerobic growth conditions. The ribonucleotide reductase system of this mutant was shown to consist of an enzyme of the NrdEF-type and a small electron transport protein. The coding operon contains the nrdEF genes and two open reading frames, one of which (nrdH) codes for the small protein. The same gene organization is present in E. coli. We propose that the aerobic class I ribonucleotide reductases contain two subclasses, one coded by nrdAB, active in E. coli and eukaryotes (class Ia), the other coded by nrdEF, present in various microorganisms (class Ib). The NrdEF enzymes use NrdH proteins as electron transporter in place of thioredoxin or glutaredoxin used by NrdAB enzymes. The two classes also differ in their allosteric regulation by dATP.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8621514</PMID><DateCompleted><Year>1996</Year><Month>06</Month><Day>20</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0021-9258</ISSN><JournalIssue CitedMedium="Print"><Volume>271</Volume><Issue>15</Issue><PubDate><Year>1996</Year><Month>Apr</Month><Day>12</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J Biol Chem</ISOAbbreviation></Journal><ArticleTitle>The ribonucleotide reductase system of Lactococcus lactis. Characterization of an NrdEF enzyme and a new electron transport protein.</ArticleTitle><Pagination><MedlinePgn>8779-85</MedlinePgn></Pagination><Abstract><AbstractText>Escherichia coli contains the genetic information for three separate ribonucleotide reductases. Two of them (class I enzymes), coded by the nrdAB and nrdEF genes, respectively, contain a tyrosyl radical, whose generation requires oxygen. The NrdAB enzyme is physiologically active. The function of the nrdEF gene is not known. The third enzyme (class III), coded by nrdDG, operates during anaerobiosis. The DNA of Lactococcus lactis contains sequences homologous to the nrdDG genes. Surprisingly, an nrdD- mutant of L. lactis grew well under standard anaerobic growth conditions. The ribonucleotide reductase system of this mutant was shown to consist of an enzyme of the NrdEF-type and a small electron transport protein. The coding operon contains the nrdEF genes and two open reading frames, one of which (nrdH) codes for the small protein. The same gene organization is present in E. coli. We propose that the aerobic class I ribonucleotide reductases contain two subclasses, one coded by nrdAB, active in E. coli and eukaryotes (class Ia), the other coded by nrdEF, present in various microorganisms (class Ib). The NrdEF enzymes use NrdH proteins as electron transporter in place of thioredoxin or glutaredoxin used by NrdAB enzymes. 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Acid</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1996</Year><Month>4</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1996</Year><Month>4</Month><Day>12</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1996</Year><Month>4</Month><Day>12</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8621514</ArticleId><ArticleId IdType="doi">10.1074/jbc.271.15.8779</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Aslund, F" sort="Aslund, F" uniqKey="Aslund F" first="F" last="Aslund">F. Aslund</name><name sortKey="Gibert, I" sort="Gibert, I" uniqKey="Gibert I" first="I" last="Gibert">I. Gibert</name><name sortKey="Hellman, U" sort="Hellman, U" uniqKey="Hellman U" first="U" last="Hellman">U. Hellman</name><name sortKey="Pontis, E" sort="Pontis, E" uniqKey="Pontis E" first="E" last="Pontis">E. Pontis</name><name sortKey="Reichard, P" sort="Reichard, P" uniqKey="Reichard P" first="P" last="Reichard">P. Reichard</name></noCountry><country name="Suède"><noRegion><name sortKey="Jordan, A" sort="Jordan, A" uniqKey="Jordan A" first="A" last="Jordan">A. Jordan</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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