ArticleGenes and environment : the official journal of the Japanese Environmental Mutagen Society2018
Structure analysis of yeast glutaredoxin Grx6 protein produced in
Article in Genes and environment : the official journal of the Japanese Environmental Mutagen Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed, 7 citations in OpenAlex.
- Mössbauer-based molecular-level decomposition of the Saccharomyces cerevisiae ironome, and preliminary characterization of isolated nuclei.Metallomics : integrated biometal science · 2022Article
- A comprehensive mechanistic model of iron metabolism in Saccharomyces cerevisiae.Metallomics : integrated biometal science · 2019Article
- Comparison of structures amongGenes and environment : the official journal of the Japanese Environmental Mutagen Society · 2018Review
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9 authors at 6 institutions in 3 countries.
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Abstract
backgroundGrx6 is a yeast Golgi/endoplasmic reticulum protein involved in iron-sulfur binding that belongs to monothiol glutaredoxin-protein family. Grx6 has been biochemically characterized previously. Grx6 contains a conserved cysteine residue (Cys-136). Depending on the active-site sequences, Grxs can be classified to classic dithiol Grxs with a CXXC motif known as classes II and monothiol Grxs with a CXXS motif known as classes I, and Grx6 belongs to the class I with a CSYS motif.
resultsOur results showed how the loop between the N-terminal and C-terminal can affect the stability. When Grx6 was incubated with FeSO
conclusionsIn this paper, we used a combination of spectroscopic and proteomic techniques to analyse the sequence and to determine the affected mutations and deletions in the stability of Grx6. Our results have increased the knowledge about the differences between monomer and dimer structures in cellular processes and proteins whose roles and functions depend on YCA1 in yeast.
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