GlutaredoxinV1, Main, Exploration, bibRecord, 000708

Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts.

Identifieur interne : 000708 ( Main/Exploration ); précédent : 000707; suivant : 000709

Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts.

Auteurs : Xi Liu [République populaire de Chine] ; Shian Liu ; Yingang Feng ; Jian-Zhong Liu ; Yuling Chen ; Khanh Pham ; Haiteng Deng ; Kendal D. Hirschi ; Xinquan Wang ; Ninghui Cheng

Source :

Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2013.

RBID : pubmed:23690600

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Motifs (genetics), Antiporters (MeSH), Arabidopsis (enzymology), Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), Carrier Proteins (metabolism), Chloroplasts (enzymology), Chromatography, Gel (MeSH), DNA (metabolism), Endonucleases (genetics), Endonucleases (metabolism), Glutaredoxins (metabolism), Magnetic Resonance Spectroscopy (MeSH), Mass Spectrometry (MeSH), Mutation, Missense (genetics), Oxidation-Reduction (MeSH), Protein Folding (MeSH), Protein Structure, Tertiary (MeSH), Reactive Oxygen Species (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Spectrophotometry, Ultraviolet (MeSH), Yeasts (MeSH).
MESH :
- chemical , genetics : Arabidopsis Proteins, Endonucleases.
- chemical , metabolism : Arabidopsis Proteins, Carrier Proteins, DNA, Endonucleases, Glutaredoxins, Reactive Oxygen Species, Saccharomyces cerevisiae Proteins.
- chemical : Antiporters.
- enzymology : Arabidopsis, Chloroplasts.
- genetics : Amino Acid Motifs, Mutation, Missense.
- Chromatography, Gel, Magnetic Resonance Spectroscopy, Mass Spectrometry, Oxidation-Reduction, Protein Folding, Protein Structure, Tertiary, Spectrophotometry, Ultraviolet, Yeasts.

Abstract

Glutaredoxins (Grxs) have been identified across taxa as important mediators in various physiological functions. A chloroplastic monothiol glutaredoxin, AtGRXS16 from Arabidopsis thaliana, comprises two distinct functional domains, an N-terminal domain (NTD) with GlyIleTyr-TyrIleGly (GIY-YIG) endonuclease motif and a C-terminal Grx module, to coordinate redox regulation and DNA cleavage in chloroplasts. Structural determination of AtGRXS16-NTD showed that it possesses a GIY-YIG endonuclease fold, but the critical residues for the nuclease activity are different from typical GIY-YIG endonucleases. AtGRXS16-NTD was able to cleave λDNA and chloroplast genomic DNA, and the nuclease activity was significantly reduced in AtGRXS16. Functional analysis indicated that AtGRXS16-NTD could inhibit the ability of AtGRXS16 to suppress the sensitivity of yeast grx5 cells to oxidative stress; however, the C-terminal Grx domain itself and AtGRXS16 with a Cys123Ser mutation were active in these cells and able to functionally complement a Grx5 deficiency in yeast. Furthermore, the two functional domains were shown to be negatively regulated through the formation of an intramolecular disulfide bond. These findings unravel a manner of regulation for Grxs and provide insights into the mechanistic link between redox regulation and DNA metabolism in chloroplasts.

DOI: 10.1073/pnas.1306899110
PubMed: 23690600
PubMed Central: PMC3677505

Affiliations:

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

to stream Main, to step Corpus: 000736
to stream Main, to step Curation: 000736

Le document en format XML

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<term>Arabidopsis Proteins (genetics)</term>
<term>Arabidopsis Proteins (metabolism)</term>
<term>Carrier Proteins (metabolism)</term>
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<term>Chromatography, Gel (MeSH)</term>
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<term>Endonucleases (metabolism)</term>
<term>Glutaredoxins (metabolism)</term>
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<term>Mutation, Missense (genetics)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Protein Folding (MeSH)</term>
<term>Protein Structure, Tertiary (MeSH)</term>
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<term>Saccharomyces cerevisiae Proteins (metabolism)</term>
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<term>Arabidopsis (enzymologie)</term>
<term>Chloroplastes (enzymologie)</term>
<term>Chromatographie sur gel (MeSH)</term>
<term>Endonucleases (génétique)</term>
<term>Endonucleases (métabolisme)</term>
<term>Espèces réactives de l'oxygène (métabolisme)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Levures (MeSH)</term>
<term>Motifs d'acides aminés (génétique)</term>
<term>Mutation faux-sens (génétique)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Pliage des protéines (MeSH)</term>
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<term>Protéines d'Arabidopsis (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines de transport (métabolisme)</term>
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<term>Spectrophotométrie UV (MeSH)</term>
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<term>Magnetic Resonance Spectroscopy</term>
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<term>Yeasts</term>
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<term>Oxydoréduction</term>
<term>Pliage des protéines</term>
<term>Spectrométrie de masse</term>
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<front><div type="abstract" xml:lang="en">Glutaredoxins (Grxs) have been identified across taxa as important mediators in various physiological functions. A chloroplastic monothiol glutaredoxin, AtGRXS16 from Arabidopsis thaliana, comprises two distinct functional domains, an N-terminal domain (NTD) with GlyIleTyr-TyrIleGly (GIY-YIG) endonuclease motif and a C-terminal Grx module, to coordinate redox regulation and DNA cleavage in chloroplasts. Structural determination of AtGRXS16-NTD showed that it possesses a GIY-YIG endonuclease fold, but the critical residues for the nuclease activity are different from typical GIY-YIG endonucleases. AtGRXS16-NTD was able to cleave λDNA and chloroplast genomic DNA, and the nuclease activity was significantly reduced in AtGRXS16. Functional analysis indicated that AtGRXS16-NTD could inhibit the ability of AtGRXS16 to suppress the sensitivity of yeast grx5 cells to oxidative stress; however, the C-terminal Grx domain itself and AtGRXS16 with a Cys123Ser mutation were active in these cells and able to functionally complement a Grx5 deficiency in yeast. Furthermore, the two functional domains were shown to be negatively regulated through the formation of an intramolecular disulfide bond. These findings unravel a manner of regulation for Grxs and provide insights into the mechanistic link between redox regulation and DNA metabolism in chloroplasts.</div>
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<Abstract><AbstractText>Glutaredoxins (Grxs) have been identified across taxa as important mediators in various physiological functions. A chloroplastic monothiol glutaredoxin, AtGRXS16 from Arabidopsis thaliana, comprises two distinct functional domains, an N-terminal domain (NTD) with GlyIleTyr-TyrIleGly (GIY-YIG) endonuclease motif and a C-terminal Grx module, to coordinate redox regulation and DNA cleavage in chloroplasts. Structural determination of AtGRXS16-NTD showed that it possesses a GIY-YIG endonuclease fold, but the critical residues for the nuclease activity are different from typical GIY-YIG endonucleases. AtGRXS16-NTD was able to cleave λDNA and chloroplast genomic DNA, and the nuclease activity was significantly reduced in AtGRXS16. Functional analysis indicated that AtGRXS16-NTD could inhibit the ability of AtGRXS16 to suppress the sensitivity of yeast grx5 cells to oxidative stress; however, the C-terminal Grx domain itself and AtGRXS16 with a Cys123Ser mutation were active in these cells and able to functionally complement a Grx5 deficiency in yeast. Furthermore, the two functional domains were shown to be negatively regulated through the formation of an intramolecular disulfide bond. These findings unravel a manner of regulation for Grxs and provide insights into the mechanistic link between redox regulation and DNA metabolism in chloroplasts.</AbstractText>
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Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts.

Structural insights into the N-terminal GIY-YIG endonuclease activity of Arabidopsis glutaredoxin AtGRXS16 in chloroplasts.

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