Monothiol glutaredoxins and A-type proteins: partners in Fe-S cluster trafficking
| Autor: | Michael K. Johnson, Angela-Nadia Albetel, Sajini Randeniya, Caryn E. Outten, Nicolas Rouhier, Bo Zhang, Daphne T. Mapolelo, Haoran Li, Jérémy Couturier |
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| Přispěvatelé: | Dept Chem, Georgia State University, University System of Georgia (USG)-University System of Georgia (USG), Ctr Metalloenzyme Studies, Dept Chem & Biochem, University of South Carolina [Columbia], Interactions Arbres-Microorganismes (IAM), Université de Lorraine (UL)-Institut National de la Recherche Agronomique (INRA), National Institute of Health [GM62524, GM100069], Agence Nationale de la Recherche [2010BLAN1616], Institut National de la Recherche Agronomique (INRA)-Université de Lorraine (UL) |
| Jazyk: | angličtina |
| Rok vydání: | 2013 |
| Předmět: |
Scaffold protein
SCAFFOLD PROTEINS 2FE-2S CLUSTER STRUCTURAL BASIS Stereochemistry Iron [SDV]Life Sciences [q-bio] Saccharomyces cerevisiae Iron–sulfur cluster Article Inorganic Chemistry SACCHAROMYCES-CEREVISIAE 03 medical and health sciences chemistry.chemical_compound Protein structure Bacterial Proteins FUNCTIONAL-CHARACTERIZATION Glutaredoxin Cluster (physics) AZOTOBACTER-VINELANDII (NIF)ISCA Sulfhydryl Compounds Protein Structure Quaternary Glutaredoxins 030304 developmental biology Azotobacter vinelandii 0303 health sciences biology 030302 biochemistry & molecular biology LIGATED 2FE-2S IRON-SULFUR CLUSTER Biological Transport biology.organism_classification Crystallography chemistry ESCHERICHIA-COLI Protein Multimerization SUBCELLULAR-LOCALIZATION Sulfur Biogenesis |
| Zdroj: | Dalton Transactions Dalton Transactions, Royal Society of Chemistry, 2013, 42 (9), pp.3107-3115. ⟨10.1039/c2dt32263c⟩ |
| ISSN: | 1477-9226 1477-9234 |
| DOI: | 10.1039/c2dt32263c⟩ |
| Popis: | Monothiol glutaredoxins (Grxs) are proposed to function in Fe-S cluster storage and delivery, based on their ability to exist as apo monomeric forms and dimeric forms containing a subunit-bridging [Fe(2)S(2)](2+) cluster, and to accept [Fe(2)S(2)](2+) clusters from primary scaffold proteins. In addition yeast cytosolic monothiol Grxs interact with Fra2 (Fe repressor of activation-2), to form a heterodimeric complex with a bound [Fe(2)S(2)](2+) cluster that plays a key role in iron sensing and regulation of iron homeostasis. In this work, we report on in vitro UV-visible CD studies of cluster transfer between homodimeric monothiol Grxs and members of the ubiquitous A-type class of Fe-S cluster carrier proteins ((Nif)IscA and SufA). The results reveal rapid, unidirectional, intact and quantitative cluster transfer from the [Fe(2)S(2)](2+) cluster-bound forms of A. thaliana GrxS14, S. cerevisiae Grx3, and A. vinelandii Grx-nif homodimers to A. vinelandii(Nif)IscA and from A. thaliana GrxS14 to A. thaliana SufA1. Coupled with in vivo evidence for interaction between monothiol Grxs and A-type Fe-S cluster carrier proteins, the results indicate that these two classes of proteins work together in cellular Fe-S cluster trafficking. However, cluster transfer is reversed in the presence of Fra2, since the [Fe(2)S(2)](2+) cluster-bound heterodimeric Grx3-Fra2 complex can be formed by intact [Fe(2)S(2)](2+) cluster transfer from (Nif)IscA. The significance of these results for Fe-S cluster biogenesis or repair and the cellular regulation of the Fe-S cluster status are discussed. |
| Databáze: | OpenAIRE |
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