Source:http://linkedlifedata.com/resource/pubmed/id/21299470
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2011-6-9
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pubmed:abstractText |
Monothiol glutaredoxins (Grxs) with a noncanonical CGFS active site are found in all kingdoms of life. They include members with a single domain and thioredoxin-Grx fusion proteins. In Saccharomyces cerevisiae, the multidomain Grx3 and Grx4 play an essential role in intracellular iron trafficking. This crucial task is mediated by an essential Fe/S cofactor. This study shows that this unique physiological role cannot be executed by single domain Grxs, because the thioredoxin domain is indispensable for function in vivo. Mutational analysis revealed that a CPxS active site motif is fully compatible with Fe/S cluster binding on Grx4, while a dithiol active site results in cofactor destabilization and a moderate impairment of in vivo function. These requirements for Fe/S cofactor stabilization on Grx4 are virtually the opposite of those previously reported for single domain Grxs. Grx4 functions as iron sensor for the iron-sensing transcription factor Aft1 in S. cerevisiae. We found that Aft1 binds to a conserved binding site at the C-terminus of Grx4. This interaction is essential for the regulation of Aft1. Collectively, our analysis demonstrates that the multidomain monothiol Grxs form a unique protein family distinct from that of the single domain Grxs.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/GRX4 protein, S pombe,
http://linkedlifedata.com/resource/pubmed/chemical/Glutaredoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Grx4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Schizosaccharomyces pombe Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Thioredoxins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1557-7716
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
1
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
19-30
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pubmed:meshHeading |
pubmed-meshheading:21299470-Catalytic Domain,
pubmed-meshheading:21299470-Glutaredoxins,
pubmed-meshheading:21299470-Protein Structure, Tertiary,
pubmed-meshheading:21299470-Saccharomyces cerevisiae,
pubmed-meshheading:21299470-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:21299470-Schizosaccharomyces,
pubmed-meshheading:21299470-Schizosaccharomyces pombe Proteins,
pubmed-meshheading:21299470-Thioredoxins
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pubmed:year |
2011
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pubmed:articleTitle |
The multidomain thioredoxin-monothiol glutaredoxins represent a distinct functional group.
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pubmed:affiliation |
Institut für Zytobiologie und Zytopathologie, Philipps-Universität Marburg, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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