Literature DB >> 17395014

Saccharomyces cerevisiae Hsp31p, a stress response protein conferring protection against reactive oxygen species.

Adrianna Skoneczna1, Arkadiusz Miciałkiewicz, Marek Skoneczny.   

Abstract

The Saccharomyces cerevisiae HSP31 (YDR533c) gene encodes a protein that belongs to the DJ-1/PfpI family and its function is unknown. Homologs to Hsp31p polypeptide can be found in organisms from all systematic groups of eukaryotes and prokaryotes, and the functions of the vast majority of them are also hypothetical. One of the homologs is human protein DJ-1. Various amino acid substitutions within this protein correlate with early onset hereditary Parkinson's disease. The deletion of the HSP31 gene displays no apparent phenotype under standard growth conditions, but a thorough functional analysis of S. cerevisiae revealed that its absence makes the cells sensitive to a subset of reactive oxygen species (ROS) generators. HSP31 is induced under conditions of oxidative stress in a YAP1-dependent manner. Similar to other stress response genes, it is also induced in the postdiauxic phase of growth and this induction is YAP1-independent. The patterns of sensitivities to various ROS generators of the hsp31Delta strain and the strain with the deletion of SOD1, another gene defending the cell against ROS, are different. We postulate that Hsp31p protects the cell against oxidative stress and complements other stress protection systems within the cell.

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Year:  2007        PMID: 17395014     DOI: 10.1016/j.freeradbiomed.2007.01.042

Source DB:  PubMed          Journal:  Free Radic Biol Med        ISSN: 0891-5849            Impact factor:   7.376


  27 in total

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5.  Robust glyoxalase activity of Hsp31, a ThiJ/DJ-1/PfpI family member protein, is critical for oxidative stress resistance in Saccharomyces cerevisiae.

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6.  Proteomic analysis of Mrr1p- and Tac1p-associated differential protein expression in azole-resistant clinical isolates of Candida albicans.

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8.  Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process.

Authors:  Chai-Jui Tsai; Kiran Aslam; Holli M Drendel; Josephat M Asiago; Kourtney M Goode; Lake N Paul; Jean-Christophe Rochet; Tony R Hazbun
Journal:  J Biol Chem       Date:  2015-08-25       Impact factor: 5.157

9.  Proteomic response of Rhizoctonia solani GD118 suppressed by Paenibacillus kribbensis PS04.

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Journal:  World J Microbiol Biotechnol       Date:  2014-08-28       Impact factor: 3.312

10.  A glutathione-independent glyoxalase of the DJ-1 superfamily plays an important role in managing metabolically generated methylglyoxal in Candida albicans.

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Journal:  J Biol Chem       Date:  2013-12-03       Impact factor: 5.157

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