GlutaredoxinV1, Main, Exploration, bibRecord, 000E73

Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.

Identifieur interne : 000E73 ( Main/Exploration ); précédent : 000E72; suivant : 000E74

Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.

Auteurs : Ron Ortenberg [États-Unis] ; Stéphanie Gon ; Amir Porat ; Jon Beckwith

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 2004.

RBID : pubmed:15123823

Descripteurs français

KwdFr :
- Données de séquences moléculaires (MeSH), Escherichia coli (croissance et développement), Escherichia coli (génétique), Escherichia coli (métabolisme), Glutarédoxines (MeSH), Liaison aux protéines (MeSH), Mutation (MeSH), Oxidoreductases (génétique), Oxidoreductases (métabolisme), Ribonucleotide reductases (métabolisme), Réplication de l'ADN (MeSH), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH).
MESH :
- croissance et développement : Escherichia coli.
- génétique : Escherichia coli, Oxidoreductases.
- métabolisme : Escherichia coli, Oxidoreductases, Ribonucleotide reductases.
- Données de séquences moléculaires, Glutarédoxines, Liaison aux protéines, Mutation, Réplication de l'ADN, Similitude de séquences d'acides aminés, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), DNA Replication (MeSH), Escherichia coli (genetics), Escherichia coli (growth & development), Escherichia coli (metabolism), Glutaredoxins (MeSH), Molecular Sequence Data (MeSH), Mutation (MeSH), Oxidoreductases (genetics), Oxidoreductases (metabolism), Protein Binding (MeSH), Ribonucleotide Reductases (metabolism), Sequence Homology, Amino Acid (MeSH).
MESH :
- chemical , genetics : Oxidoreductases.
- chemical , metabolism : Oxidoreductases, Ribonucleotide Reductases.
- chemical : Glutaredoxins.
- genetics : Escherichia coli.
- growth & development : Escherichia coli.
- metabolism : Escherichia coli.
- Amino Acid Sequence, DNA Replication, Molecular Sequence Data, Mutation, Protein Binding, Sequence Homology, Amino Acid.

Abstract

A strain of Escherichia coli missing three members of the thioredoxin superfamily, thioredoxins 1 and 2 and glutaredoxin 1, is unable to grow, a phenotype presumed to be due to the inability of cells to reduce the essential enzyme ribonucleotide reductase. Two classes of mutations can restore growth to such a strain. First, we have isolated a collection of mutations in the gene for the protein glutaredoxin 3 that suppress the growth defect. Remarkably, all eight independent mutations alter the same amino acid, methionine-43, changing it to valine, isoleucine, or leucine. From the position of the amino acid changes and their effects, we propose that these alterations change the protein so that its properties are closer to those of glutaredoxin 1. The second means of suppressing the growth defects of the multiply mutant strain was by mutations in the DNA replication genes, dnaA and dnaN. These mutations substantially increase the expression of ribonucleotide reductase, most likely by altering the interaction of the regulatory protein DnaA with the ribonucleotide reductase promoter. Our results suggest that this increase in the concentration of ribonucleotide reductase in the cell allows more effective interaction with glutaredoxin 3, thus restoring an effective pool of deoxyribonucleotides. Our studies present direct evidence that ribonucleotide reductase is the only essential enzyme that requires the three reductive proteins missing in our strains. Our results also suggest an unexpected regulatory interaction between the DnaA and DnaN proteins.

DOI: 10.1073/pnas.0401965101
PubMed: 15123823
PubMed Central: PMC409937

Affiliations:

Links toward previous steps (curation, corpus...)

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Le document en format XML

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<term>Escherichia coli (métabolisme)</term>
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<term>Oxidoreductases (métabolisme)</term>
<term>Ribonucleotide reductases (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">A strain of Escherichia coli missing three members of the thioredoxin superfamily, thioredoxins 1 and 2 and glutaredoxin 1, is unable to grow, a phenotype presumed to be due to the inability of cells to reduce the essential enzyme ribonucleotide reductase. Two classes of mutations can restore growth to such a strain. First, we have isolated a collection of mutations in the gene for the protein glutaredoxin 3 that suppress the growth defect. Remarkably, all eight independent mutations alter the same amino acid, methionine-43, changing it to valine, isoleucine, or leucine. From the position of the amino acid changes and their effects, we propose that these alterations change the protein so that its properties are closer to those of glutaredoxin 1. The second means of suppressing the growth defects of the multiply mutant strain was by mutations in the DNA replication genes, dnaA and dnaN. These mutations substantially increase the expression of ribonucleotide reductase, most likely by altering the interaction of the regulatory protein DnaA with the ribonucleotide reductase promoter. Our results suggest that this increase in the concentration of ribonucleotide reductase in the cell allows more effective interaction with glutaredoxin 3, thus restoring an effective pool of deoxyribonucleotides. Our studies present direct evidence that ribonucleotide reductase is the only essential enzyme that requires the three reductive proteins missing in our strains. Our results also suggest an unexpected regulatory interaction between the DnaA and DnaN proteins.</div>
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</affiliations>
</record>

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EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000E73 | SxmlIndent | more

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{{Explor lien
   |wiki=    Bois
   |area=    GlutaredoxinV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:15123823
   |texte=   Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.
}}

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       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a GlutaredoxinV1

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	Serveur d'exploration sur la glutarédoxine
	Attention, ce site est en cours de développement ! Attention, site généré par des moyens informatiques à partir de corpus bruts. Les informations ne sont donc pas validées.

Serveur d'exploration sur la glutarédoxine

Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.

Interactions of glutaredoxins, ribonucleotide reductase, and components of the DNA replication system of Escherichia coli.

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