Metabolic role for yeast DJ-1 superfamily proteins

Wilson, Mark A.

doi:10.1073/pnas.1405511111

Cited by 15 publications

(7 citation statements)

References 20 publications

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“…S. cerevisiae HSP31 is a relatively recent addition to the list of stress-responsive genes. For years, this gene has received little interest except as a human DJ-1 orthologue, but it has recently been extensively studied in S. cerevisiae (Natkańska et al 2017 ; Aslam et al 2016 ; Aslam and Hazbun 2016 ; Bankapalli et al 2015 ; Amm et al 2015 ; Tsai et al 2015 ; Wilson 2014 ; Miller-Fleming et al 2014 ). HSP31 orthologues from related yeast species have also been investigated (Zhao et al 2014 ; Hasim et al 2014 ).…”

Section: Discussionmentioning

confidence: 99%

Oxidative stress triggers aggregation of GFP-tagged Hsp31p, the budding yeast environmental stress response chaperone, and glyoxalase III

Natkańska

Skoneczna

Skoneczny

2018

Cell Stress and Chaperones

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The Saccharomyces cerevisiae Hsp31p protein belongs to the ubiquitous DJ-1/ThiJ/PfpI family. The most prominent member of this family is human DJ-1; defects of this protein are associated with Parkinson’s disease pathogenesis. Numerous recent findings reported by our group and others have revealed the importance of Hsp31p for survival in the post-diauxic phase of cell growth and under diverse environmental stresses. Hsp31p was shown to possess glutathione-independent glyoxalase III activity and to function as a protein chaperone, suggesting that it has multiple cellular roles. Our previous work also revealed that HSP31 gene expression was controlled by multiple stress-related transcription factors, which mediated HSP31 promoter responses to oxidative, osmotic, and thermal stresses, toxic products of glycolysis, and the diauxic shift. Nevertheless, the exact role of Hsp31p within budding yeast cells remains elusive. Here, we aimed to obtain insights into the function of Hsp31p based on its intracellular localization. We have demonstrated that the Hsp31p-GFP fusion protein is localized to the cytosol under most environmental conditions and that it becomes particulate in response to oxidative stress. However, the particles do not colocalize with other granular subcellular structures present in budding yeast cells. The observed particulate localization does not seem to be important for Hsp31p functionality. Instead, it is likely the result of oxidative damage, as the particle abundance increases when Hsp31p is nonfunctional, when the cellular oxidative stress response is affected, or when cellular maintenance systems that optimize the state of the proteome are compromised.

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Section: Discussionmentioning

confidence: 99%

Oxidative stress triggers aggregation of GFP-tagged Hsp31p, the budding yeast environmental stress response chaperone, and glyoxalase III

Natkańska

Skoneczna

Skoneczny

2018

Cell Stress and Chaperones

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“… 12,14,15 The catalytic triad Cys-His-Glu of Hsp31 is vital for this enzymatic activity and critical for suppressing the elevated level of ROS by MG. 12,15 An overall view has emerged that indicates Hsp31 has important metabolic and regulatory roles in cytoprotective pathways. 16 …”

Section: Role Of Hsp31 In Cellular Stress Response and Proteotoxic Stmentioning

confidence: 99%

Hsp31, a member of the DJ-1 superfamily, is a multitasking stress responder with chaperone activity

Aslam

Hazbun

2016

Prion

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Among different types of protein aggregation, amyloids are a biochemically well characterized state of protein aggregation that are associated with a large number of neurodegenerative diseases including Parkinson's disease, Alzheimer and Creutzfeldt-Jakob disease. Yeast, Saccharomyces cerevisiae is an insightful model to understand the underlying mechanism of protein aggregation. Many yeast molecular chaperones can modulate aggregation and misfolding of proteins including α-Syn and the Sup35 prion. Hsp31 is a homodimeric protein structurally similar to human DJ-1, a Parkinson's disease-linked protein, and both are members of the DJ-1/ThiJ/PfpI superfamily. An emerging view is that Hsp31 and its associated superfamily members each have divergent multitasking functions that have the common theme of responding and managing various types of cellular stress. Hsp31 has several biochemical activities including chaperone and detoxifying enzyme activities that modulate at various points of a stress pathway such as toxicity associated with protein misfolding. However, we have shown the protective role of Hsp31's chaperone activity can operate independent of detoxifying enzyme activities in preventing the early stages of protein aggregate formation and associated cellular toxicities. We provide additional data that collectively supports the multiple functional roles that can be accomplished independent of each other. We present data indicating Hsp31 purified from yeast is more active compared to expression and purification from E. coli suggesting that posttranslational modifications could be important for Hsp31 to be fully active. We also compare the similarities and differences in activities among paralogs of Hsp31 supporting a model in which this protein family has overlapping but diverging roles in responding to various sources of cellular stresses.

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“…The cellular functions of DJ-1 and E. coli hchA have been characterized, and their multifunctional roles in mediating oxidative stress, chaperone-like activity, methylglyoxalase activity, and cytoprotection have been described (10,15,16,19). There has been limited characterization of the cellular functions of Hsp31, but several recent studies have demonstrated that it has glyoxylase activity (20), chaperone activity (21), and a role in autophagy (22).…”

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confidence: 99%

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

Tsai

Aslam

Drendel

et al. 2015

Journal of Biological Chemistry

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Background: Hsp31 is a multifunctional cellular stress response protein.Results: Hsp31 is a stress-inducible chaperone that has substoichiometric activity on a wide spectrum of substrates, including prions and the non-physiological client, ␣-synuclein. Conclusion: Hsp31 protects cells from ␣-synuclein-mediated toxicity via chaperone activity and independently from enzymatic activity and autophagy. Significance: This is the first characterization of the early acting and wide ranging chaperone activity of Hsp31.

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Metabolic role for yeast DJ-1 superfamily proteins

Cited by 15 publications

References 20 publications

Oxidative stress triggers aggregation of GFP-tagged Hsp31p, the budding yeast environmental stress response chaperone, and glyoxalase III

Oxidative stress triggers aggregation of GFP-tagged Hsp31p, the budding yeast environmental stress response chaperone, and glyoxalase III

Hsp31, a member of the DJ-1 superfamily, is a multitasking stress responder with chaperone activity

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

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