Evidence map›Paper›PMID 26370081›Full record

ArticleThe Journal of biological chemistry2015

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

Kondalarao Bankapalli, SreeDivya Saladi, Sahezeel S Awadia, Arvind Vittal Goswami, Madhuja Samaddar, Patrick D'Silva

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
6.9field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 86 citations in OpenAlex.

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  11. Adaptation ofMicroorganisms · 2023
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  12. Quiescence inAnnual review of genetics · 2022
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  13. RNA-Seq Based Transcriptome Analysis ofJournal of fungi (Basel, Switzerland) · 2022
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  14. Article
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  17. Article
  18. Transcriptional Analysis ofJournal of fungi (Basel, Switzerland) · 2021
    Article
  19. Article
  20. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Kondalarao BankapalliFrom the Department of Biochemistry, Indian Institute of Science, Bangalore, Karnataka 560012, India.
SreeDivya SaladiFrom the Department of Biochemistry, Indian Institute of Science, Bangalore, Karnataka 560012, India.
Sahezeel S AwadiaFrom the Department of Biochemistry, Indian Institute of Science, Bangalore, Karnataka 560012, India.
Arvind Vittal GoswamiFrom the Department of Biochemistry, Indian Institute of Science, Bangalore, Karnataka 560012, India.
Madhuja SamaddarFrom the Department of Biochemistry, Indian Institute of Science, Bangalore, Karnataka 560012, India.
Patrick D'SilvaFrom the Department of Biochemistry, Indian Institute of Science, Bangalore, Karnataka 560012, India patrick@biochem.iisc.ernet.in.
Indian Institute of Science Bangalore · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methylglyoxal (MG) is a reactive metabolic intermediate generated during various cellular biochemical reactions, including glycolysis. The accumulation of MG indiscriminately modifies proteins, including important cellular antioxidant machinery, leading to severe oxidative stress, which is implicated in multiple neurodegenerative disorders, aging, and cardiac disorders. Although cells possess efficient glyoxalase systems for detoxification, their functions are largely dependent on the glutathione cofactor, the availability of which is self-limiting under oxidative stress. Thus, higher organisms require alternate modes of reducing the MG-mediated toxicity and maintaining redox balance. In this report, we demonstrate that Hsp31 protein, a member of the ThiJ/DJ-1/PfpI family in Saccharomyces cerevisiae, plays an indispensable role in regulating redox homeostasis. Our results show that Hsp31 possesses robust glutathione-independent methylglyoxalase activity and suppresses MG-mediated toxicity and ROS levels as compared with another paralog, Hsp34. On the other hand, glyoxalase-defective mutants of Hsp31 were found highly compromised in regulating the ROS levels. Additionally, Hsp31 maintains cellular glutathione and NADPH levels, thus conferring protection against oxidative stress, and Hsp31 relocalizes to mitochondria to provide cytoprotection to the organelle under oxidative stress conditions. Importantly, human DJ-1, which is implicated in the familial form of Parkinson disease, complements the function of Hsp31 by suppressing methylglyoxal and oxidative stress, thus signifying the importance of these proteins in the maintenance of ROS homeostasis across phylogeny.

Indexed as

Heat-Shock ProteinsHumansLactoylglutathione LyaseMitochondriaMitochondrial ProteinsMutationNADPOxidative StressProtein TransportPyruvaldehydeReactive Oxygen SpeciesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHeat-Shock ProteinsHSP31 protein, S cerevisiaeLactoylglutathione LyaseMitochondrial ProteinsNADPPyruvaldehydeReactive Oxygen SpeciesSaccharomyces cerevisiae Proteinsheat shock protein (HSP)mitochondriamitochondrial transportmolecular chaperoneoxidative stressParkinson diseaseprotein foldingyeast genetics

Identifiers

PMID26370081
PMCPMC4646309
OpenAlexW2249632748

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.