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Structure analysis of yeast glutaredoxin Grx6 protein produced in Escherichia coli.

Identifieur interne : 000C67 ( Main/Exploration ); précédent : 000C66; suivant : 000C68

Structure analysis of yeast glutaredoxin Grx6 protein produced in Escherichia coli.

Auteurs : Mohnad Abdalla [Soudan] ; Wafa Ali Eltayb ; Amr Ahmed El-Arabey ; Raihan Mo ; T I M. Dafaalla [Soudan] ; Hamed I. Hamouda ; Eijaz Ahmed Bhat ; Annoor Awadasseid [République populaire de Chine] ; Hassan Abdellha Ahmed Ali [Soudan]

Source :

RBID : pubmed:30123389

Abstract

Background

Grx6 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.

Results

Our results showed how the loop between the N-terminal and C-terminal can affect the stability. When Grx6 was incubated with FeSO

Conclusions

In 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.


DOI: 10.1186/s41021-018-0103-6
PubMed: 30123389
PubMed Central: PMC6091153


Affiliations:


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


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<b>Background</b>
</p>
<p>Grx6 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.</p>
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<div type="abstract" xml:lang="en">
<p>
<b>Results</b>
</p>
<p>Our results showed how the loop between the N-terminal and C-terminal can affect the stability. When Grx6 was incubated with FeSO</p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>Conclusions</b>
</p>
<p>In 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.</p>
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<AbstractText Label="Background" NlmCategory="UNASSIGNED">Grx6 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.</AbstractText>
<AbstractText Label="Results" NlmCategory="UNASSIGNED">Our results showed how the loop between the N-terminal and C-terminal can affect the stability. When Grx6 was incubated with FeSO
<sub>4</sub>
·7H
<sub>2</sub>
O and (NH
<sub>4</sub>
)
<sub>2</sub>
Fe(SO
<sub>4</sub>
)
<sub>2</sub>
·6H
<sub>2</sub>
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<i>Saccharomyces cerevisiae</i>
Grx6.</AbstractText>
<AbstractText Label="Conclusions" NlmCategory="UNASSIGNED">In 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.</AbstractText>
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<ForeName>Annoor</ForeName>
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<LastName>Ali</LastName>
<ForeName>Hassan Abdellha Ahmed</ForeName>
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<Affiliation>8Faculty of Medicine, Nile Valley University, Atbara, Sudan.</Affiliation>
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<Month>08</Month>
<Day>06</Day>
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<KeywordList Owner="NOTNLM">
<Keyword MajorTopicYN="N">Crystallization</Keyword>
<Keyword MajorTopicYN="N">Fe-S</Keyword>
<Keyword MajorTopicYN="N">Grx6</Keyword>
<Keyword MajorTopicYN="N">Purification</Keyword>
<Keyword MajorTopicYN="N">Saccharomyces cerevisiae</Keyword>
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<CoiStatement>Not applicable Not applicable The authors declare that they have no competing interests. Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.</CoiStatement>
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