pH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature

Abstract Peroxiredoxin 6 (Prdx6), the ubiquitously expressed enzyme belonging to the family of peroxidases, namely, peroxiredoxins, exhibits a unique feature of functional compartmentalization within cells. Whereas, the enzyme localized in cytosol shows glutathione peroxidase activity, its lysosomal...

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Autores principales:	Rimpy Kaur Chowhan, Sunaina Hotumalani, Hamidur Rahaman, Laishram Rajendrakumar Singh
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e31d544a68084e5db1f7144c130cd78b
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spelling	oai:doaj.org-article:e31d544a68084e5db1f7144c130cd78b2021-12-02T16:51:38ZpH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature10.1038/s41598-021-89093-82045-2322https://doaj.org/article/e31d544a68084e5db1f7144c130cd78b2021-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-89093-8https://doaj.org/toc/2045-2322Abstract Peroxiredoxin 6 (Prdx6), the ubiquitously expressed enzyme belonging to the family of peroxidases, namely, peroxiredoxins, exhibits a unique feature of functional compartmentalization within cells. Whereas, the enzyme localized in cytosol shows glutathione peroxidase activity, its lysosomal counterpart performs calcium independent phospholipase A2 (aiPLA2) activity. Like any true moonlighting protein, these two activities of Prdx6 are mutually exclusive of each other as a function of the pH of the cellular compartments. Differential substrate preference at different pH (i.e. peroxidised phospholipids at neutral pH and reduced phospholipids at acidic pH) is considered to be the reason for this behavior. To gain insight into the pH-induced structural–functional interplay we have systematically evaluated conformational variations, thermodynamic stability of the protein and quaternary state of the conformers at both pH 7.0 and 4.0. Our findings suggest that change in pH allows alterations in native states of Prdx6 at pH 7.0 and 4.0 such that the changes make the protein resistant to thermal denaturation at low pH.Rimpy Kaur ChowhanSunaina HotumalaniHamidur RahamanLaishram Rajendrakumar SinghNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-10 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Rimpy Kaur Chowhan Sunaina Hotumalani Hamidur Rahaman Laishram Rajendrakumar Singh pH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature
description	Abstract Peroxiredoxin 6 (Prdx6), the ubiquitously expressed enzyme belonging to the family of peroxidases, namely, peroxiredoxins, exhibits a unique feature of functional compartmentalization within cells. Whereas, the enzyme localized in cytosol shows glutathione peroxidase activity, its lysosomal counterpart performs calcium independent phospholipase A2 (aiPLA2) activity. Like any true moonlighting protein, these two activities of Prdx6 are mutually exclusive of each other as a function of the pH of the cellular compartments. Differential substrate preference at different pH (i.e. peroxidised phospholipids at neutral pH and reduced phospholipids at acidic pH) is considered to be the reason for this behavior. To gain insight into the pH-induced structural–functional interplay we have systematically evaluated conformational variations, thermodynamic stability of the protein and quaternary state of the conformers at both pH 7.0 and 4.0. Our findings suggest that change in pH allows alterations in native states of Prdx6 at pH 7.0 and 4.0 such that the changes make the protein resistant to thermal denaturation at low pH.
format	article
author	Rimpy Kaur Chowhan Sunaina Hotumalani Hamidur Rahaman Laishram Rajendrakumar Singh
author_facet	Rimpy Kaur Chowhan Sunaina Hotumalani Hamidur Rahaman Laishram Rajendrakumar Singh
author_sort	Rimpy Kaur Chowhan
title	pH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature
title_short	pH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature
title_full	pH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature
title_fullStr	pH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature
title_full_unstemmed	pH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature
title_sort	ph induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal ph or high temperature
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/e31d544a68084e5db1f7144c130cd78b
work_keys_str_mv	AT rimpykaurchowhan phinducedconformationalalterationinhumanperoxiredoxin6mightberesponsibleforitsresistanceagainstlysosomalphorhightemperature AT sunainahotumalani phinducedconformationalalterationinhumanperoxiredoxin6mightberesponsibleforitsresistanceagainstlysosomalphorhightemperature AT hamidurrahaman phinducedconformationalalterationinhumanperoxiredoxin6mightberesponsibleforitsresistanceagainstlysosomalphorhightemperature AT laishramrajendrakumarsingh phinducedconformationalalterationinhumanperoxiredoxin6mightberesponsibleforitsresistanceagainstlysosomalphorhightemperature
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pH induced conformational alteration in human peroxiredoxin 6 might be responsible for its resistance against lysosomal pH or high temperature

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