GlutaredoxinV1, Main, Exploration, bibRecord, 000B06

Molecular mechanisms of thioredoxin and glutaredoxin as hydrogen donors for Mammalian s phase ribonucleotide reductase.

Identifieur interne : 000B06 ( Main/Exploration ); précédent : 000B05; suivant : 000B07

Molecular mechanisms of thioredoxin and glutaredoxin as hydrogen donors for Mammalian s phase ribonucleotide reductase.

Auteurs : Farnaz Zahedi Avval [Suède] ; Arne Holmgren

Source :

The Journal of biological chemistry [ 0021-9258 ] ; 2009.

RBID : pubmed:19176520

Descripteurs français

KwdFr :
- Animaux (MeSH), Catalyse (MeSH), Domaine catalytique (physiologie), Désoxyribonucléotides (biosynthèse), Désoxyribonucléotides (composition chimique), Escherichia coli (enzymologie), Glutarédoxines (composition chimique), Glutarédoxines (métabolisme), Hydrogène (composition chimique), Hydrogène (métabolisme), Phase S (physiologie), Protéines Escherichia coli (composition chimique), Protéines Escherichia coli (métabolisme), Ribonucleotide reductases (composition chimique), Ribonucleotide reductases (métabolisme), Réplication de l'ADN (physiologie), Souris (MeSH), Thiorédoxines (composition chimique), Thiorédoxines (métabolisme).
MESH :
- biosynthèse : Désoxyribonucléotides.
- composition chimique : Désoxyribonucléotides, Glutarédoxines, Hydrogène, Protéines Escherichia coli, Ribonucleotide reductases, Thiorédoxines.
- enzymologie : Escherichia coli.
- métabolisme : Glutarédoxines, Hydrogène, Protéines Escherichia coli, Ribonucleotide reductases, Thiorédoxines.
- physiologie : Domaine catalytique, Phase S, Réplication de l'ADN.
- Animaux, Catalyse, Souris.

English descriptors

KwdEn :
- Animals (MeSH), Catalysis (MeSH), Catalytic Domain (physiology), DNA Replication (physiology), Deoxyribonucleotides (biosynthesis), Deoxyribonucleotides (chemistry), Escherichia coli (enzymology), Escherichia coli Proteins (chemistry), Escherichia coli Proteins (metabolism), Glutaredoxins (chemistry), Glutaredoxins (metabolism), Hydrogen (chemistry), Hydrogen (metabolism), Mice (MeSH), Ribonucleotide Reductases (chemistry), Ribonucleotide Reductases (metabolism), S Phase (physiology), Thioredoxins (chemistry), Thioredoxins (metabolism).
MESH :
- chemical , biosynthesis : Deoxyribonucleotides.
- chemical , chemistry : Deoxyribonucleotides, Escherichia coli Proteins, Glutaredoxins, Hydrogen, Ribonucleotide Reductases, Thioredoxins.
- enzymology : Escherichia coli.
- chemical , metabolism : Escherichia coli Proteins, Glutaredoxins, Hydrogen, Ribonucleotide Reductases, Thioredoxins.
- physiology : Catalytic Domain, DNA Replication, S Phase.
- Animals, Catalysis, Mice.

Abstract

Ribonucleotide reductase (RNR) catalyzes the rate-limiting step in deoxyribonucleotide synthesis essential for DNA replication and repair. RNR in S phase mammalian cells comprises a weak cytosolic complex of the catalytic R1 protein containing redox active cysteine residues and the R2 protein harboring the tyrosine free radical. Each enzyme turnover generates a disulfide in the active site of R1, which is reduced by C-terminally located shuttle dithiols leaving a disulfide to be reduced. Electrons for reduction come ultimately from NADPH via thioredoxin reductase and thioredoxin (Trx) or glutathione reductase, glutathione, and glutaredoxin (Grx), but the mechanism has not been clarified for mammalian RNR. Using recombinant mouse RNR, we found that Trx1 and Grx1 had similar catalytic efficiency (k(cat)/K(m)). With 4 mm GSH, Grx1 showed a higher affinity (apparent K(m) value, 0.18 microm) compared with Trx1 which displayed a higher apparent k(cat), suggesting its major role in S phase DNA replication. Surprisingly, Grx activity was strongly dependent on GSH concentrations (apparent K(m) value, 3 mm) and a Grx2 C40S mutant was active despite only one cysteine residue in the active site. This demonstrates a GSH-mixed disulfide mechanism for glutaredoxin catalysis in contrast to the dithiol mechanism for thioredoxin. This may be an advantage with the low levels of RNR for DNA repair or in tumor cells with high RNR and no or low Trx expression. Our results demonstrate mechanistic differences between the mammalian and canonical Escherichia coli RNR enzymes, which may offer an explanation for the nonconserved shuttle dithiol sequences in the C terminus of the R1.

DOI: 10.1074/jbc.M809338200
PubMed: 19176520
PubMed Central: PMC2659180

Affiliations:

Suède

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

to stream Main, to step Corpus: 000B29
to stream Main, to step Curation: 000B29

Le document en format XML

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<term>Réplication de l'ADN (physiologie)</term>
<term>Souris (MeSH)</term>
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<term>Thiorédoxines (métabolisme)</term>
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<term>Ribonucleotide Reductases</term>
<term>Thioredoxins</term>
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<term>Protéines Escherichia coli</term>
<term>Ribonucleotide reductases</term>
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<term>Glutaredoxins</term>
<term>Hydrogen</term>
<term>Ribonucleotide Reductases</term>
<term>Thioredoxins</term>
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<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term>
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<term>Ribonucleotide reductases</term>
<term>Thiorédoxines</term>
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<front><div type="abstract" xml:lang="en">Ribonucleotide reductase (RNR) catalyzes the rate-limiting step in deoxyribonucleotide synthesis essential for DNA replication and repair. RNR in S phase mammalian cells comprises a weak cytosolic complex of the catalytic R1 protein containing redox active cysteine residues and the R2 protein harboring the tyrosine free radical. Each enzyme turnover generates a disulfide in the active site of R1, which is reduced by C-terminally located shuttle dithiols leaving a disulfide to be reduced. Electrons for reduction come ultimately from NADPH via thioredoxin reductase and thioredoxin (Trx) or glutathione reductase, glutathione, and glutaredoxin (Grx), but the mechanism has not been clarified for mammalian RNR. Using recombinant mouse RNR, we found that Trx1 and Grx1 had similar catalytic efficiency (k(cat)/K(m)). With 4 mm GSH, Grx1 showed a higher affinity (apparent K(m) value, 0.18 microm) compared with Trx1 which displayed a higher apparent k(cat), suggesting its major role in S phase DNA replication. Surprisingly, Grx activity was strongly dependent on GSH concentrations (apparent K(m) value, 3 mm) and a Grx2 C40S mutant was active despite only one cysteine residue in the active site. This demonstrates a GSH-mixed disulfide mechanism for glutaredoxin catalysis in contrast to the dithiol mechanism for thioredoxin. This may be an advantage with the low levels of RNR for DNA repair or in tumor cells with high RNR and no or low Trx expression. Our results demonstrate mechanistic differences between the mammalian and canonical Escherichia coli RNR enzymes, which may offer an explanation for the nonconserved shuttle dithiol sequences in the C terminus of the R1.</div>
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<Abstract><AbstractText>Ribonucleotide reductase (RNR) catalyzes the rate-limiting step in deoxyribonucleotide synthesis essential for DNA replication and repair. RNR in S phase mammalian cells comprises a weak cytosolic complex of the catalytic R1 protein containing redox active cysteine residues and the R2 protein harboring the tyrosine free radical. Each enzyme turnover generates a disulfide in the active site of R1, which is reduced by C-terminally located shuttle dithiols leaving a disulfide to be reduced. Electrons for reduction come ultimately from NADPH via thioredoxin reductase and thioredoxin (Trx) or glutathione reductase, glutathione, and glutaredoxin (Grx), but the mechanism has not been clarified for mammalian RNR. Using recombinant mouse RNR, we found that Trx1 and Grx1 had similar catalytic efficiency (k(cat)/K(m)). With 4 mm GSH, Grx1 showed a higher affinity (apparent K(m) value, 0.18 microm) compared with Trx1 which displayed a higher apparent k(cat), suggesting its major role in S phase DNA replication. Surprisingly, Grx activity was strongly dependent on GSH concentrations (apparent K(m) value, 3 mm) and a Grx2 C40S mutant was active despite only one cysteine residue in the active site. This demonstrates a GSH-mixed disulfide mechanism for glutaredoxin catalysis in contrast to the dithiol mechanism for thioredoxin. This may be an advantage with the low levels of RNR for DNA repair or in tumor cells with high RNR and no or low Trx expression. Our results demonstrate mechanistic differences between the mammalian and canonical Escherichia coli RNR enzymes, which may offer an explanation for the nonconserved shuttle dithiol sequences in the C terminus of the R1.</AbstractText>
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<ReferenceList><Reference><Citation>Nature. 2000 Mar 2;404(6773):42-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10716435</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1991 Feb 19;30(7):1939-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1847079</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2000 May 5;275(18):13398-405</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10788450</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2000 Jun 9;275(23):17747-53</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10747958</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2001 Jul 13;276(28):26269-75</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11297543</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2001 Aug 10;276(32):30374-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11397793</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2001 Aug 28;98(18):10067-72</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11526232</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2001 Nov 2;276(44):40647-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11517226</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Genet. 2001;35:673-745</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11700297</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 2002 Jan 15;41(2):462-74</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11781084</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Arch Biochem Biophys. 2002 Jan 15;397(2):149-55</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11795865</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 2002;348:1-21</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11885264</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Cancer Res. 2003 Mar 1;63(5):980-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12615712</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2003 Aug 29;278(35):33408-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12816947</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 Feb 27;279(9):7537-43</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14676218</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2004 Jun 1;1699(1-2):1-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15158709</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 2004 Jul 2;319(3):801-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15184054</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2004 Jul 23;279(30):31050-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15145955</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Appl Environ Microbiol. 2004 Sep;70(9):5159-67</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15345395</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eur J Biochem. 1975 Aug 1;56(1):289-94</Citation>
<ArticleIdList><ArticleId IdType="pubmed">240707</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1976 Jul;73(7):2275-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7783</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1978 Sep 19;17(19):4071-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">101237</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1979 May 10;254(9):3672-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">34620</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1979 May;76(5):2158-62</Citation>
<ArticleIdList><ArticleId IdType="pubmed">377293</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1979 Jul 10;18(14):2941-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">111707</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 1979;48:133-58</Citation>
<ArticleIdList><ArticleId IdType="pubmed">382982</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1979 Oct 10;254(19):9627-32</Citation>
<ArticleIdList><ArticleId IdType="pubmed">385588</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 1981 Apr;78(4):2447-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7017732</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Arch Biochem Biophys. 1982 Mar;214(1):102-13</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6177288</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1992 Sep 29;31(38):9288-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1390715</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1993 Sep 21;32(37):9701-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8373774</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 1994 Aug 18;370(6490):533-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8052308</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1994 Sep 16;269(37):23171-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8083221</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Eur J Cell Biol. 1993 Dec;62(2):314-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7925487</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochem Biophys Res Commun. 1996 Mar 7;220(1):42-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8602854</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1998 Apr 28;37(17):5849-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9558318</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1998 Jul 17;273(29):18382-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9660805</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1964 Oct;239:3436-44</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14245400</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Methods Enzymol. 2005;401:78-99</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16399380</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2006 Mar 24;281(12):7834-41</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16436374</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2006 Jun 2;281(22):15058-63</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16574642</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 2006;75:681-706</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16756507</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2006 May-Jun;8(5-6):735-42</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16771665</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2006 Sep 22;281(38):27705-11</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16861739</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2007 Jan;9(1):25-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17115886</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Free Radic Biol Med. 2007 Apr 1;42(7):1008-16</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17349928</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2007 Jun 8;282(23):16820-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17416930</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2007 Sep 4;104(36):14324-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17726094</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>PLoS One. 2007;2(10):e1112</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17971875</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antioxid Redox Signal. 2008 Mar;10(3):547-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18092940</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochim Biophys Acta. 2008 Nov;1780(11):1304-17</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18621099</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proc Natl Acad Sci U S A. 2008 Nov 18;105(46):17801-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18997010</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1989 Jul 25;264(21):12249-52</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2663852</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1982 Jun 25;257(12):6686-90</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7045093</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1982 Nov 10;257(21):12526-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6752137</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biochemistry. 1982 Dec 21;21(26):6628-33</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7159551</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1983 Nov 25;258(22):13453-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6358204</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Virol. 1984 Nov;52(2):501-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6387174</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 1985;54:237-71</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3896121</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Exp Cell Res. 1986 Apr;163(2):363-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3514246</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1988 Nov 25;263(33):17205-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">3053703</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mutat Res. 2000 Feb 14;447(2):305-16</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10751614</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
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</country>
</list>
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</noRegion>
</country>
</tree>
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Molecular mechanisms of thioredoxin and glutaredoxin as hydrogen donors for Mammalian s phase ribonucleotide reductase.

Molecular mechanisms of thioredoxin and glutaredoxin as hydrogen donors for Mammalian s phase ribonucleotide reductase.

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