Tags

Type your tag names separated by a space and hit enter

Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function.
Cell. 2004 May 28; 117(5):625-35.Cell

Abstract

Although a great deal is known biochemically about peroxiredoxins (Prxs), little is known about their real physiological function. We show here that two cytosolic yeast Prxs, cPrxI and II, which display diversity in structure and apparent molecular weights (MW), can act alternatively as peroxidases and molecular chaperones. The peroxidase function predominates in the lower MW forms, whereas the chaperone function predominates in the higher MW complexes. Oxidative stress and heat shock exposure of yeasts causes the protein structures of cPrxI and II to shift from low MW species to high MW complexes. This triggers a peroxidase-to-chaperone functional switch. These in vivo changes are primarily guided by the active peroxidase site residue, Cys(47), which serves as an efficient "H(2)O(2)-sensor" in the cells. The chaperone function of these proteins enhances yeast resistance to heat shock.

Authors+Show Affiliations

Division of Applied Life Sciences, Gyeonsang National University, Chinju, 660-701, South Korea.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

15163410

Citation

Jang, Ho Hee, et al. "Two Enzymes in One; Two Yeast Peroxiredoxins Display Oxidative Stress-dependent Switching From a Peroxidase to a Molecular Chaperone Function." Cell, vol. 117, no. 5, 2004, pp. 625-35.
Jang HH, Lee KO, Chi YH, et al. Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function. Cell. 2004;117(5):625-35.
Jang, H. H., Lee, K. O., Chi, Y. H., Jung, B. G., Park, S. K., Park, J. H., Lee, J. R., Lee, S. S., Moon, J. C., Yun, J. W., Choi, Y. O., Kim, W. Y., Kang, J. S., Cheong, G. W., Yun, D. J., Rhee, S. G., Cho, M. J., & Lee, S. Y. (2004). Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function. Cell, 117(5), 625-35.
Jang HH, et al. Two Enzymes in One; Two Yeast Peroxiredoxins Display Oxidative Stress-dependent Switching From a Peroxidase to a Molecular Chaperone Function. Cell. 2004 May 28;117(5):625-35. PubMed PMID: 15163410.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Two enzymes in one; two yeast peroxiredoxins display oxidative stress-dependent switching from a peroxidase to a molecular chaperone function. AU - Jang,Ho Hee, AU - Lee,Kyun Oh, AU - Chi,Yong Hun, AU - Jung,Bae Gyo, AU - Park,Soo Kwon, AU - Park,Jin Ho, AU - Lee,Jung Ro, AU - Lee,Seung Sik, AU - Moon,Jeong Chan, AU - Yun,Jeong Won, AU - Choi,Yeon Ok, AU - Kim,Woe Yeon, AU - Kang,Ji Seoun, AU - Cheong,Gang-Won, AU - Yun,Dae-Jin, AU - Rhee,Sue Goo, AU - Cho,Moo Je, AU - Lee,Sang Yeol, PY - 2003/04/16/received PY - 2004/03/31/revised PY - 2004/04/06/accepted PY - 2004/5/28/pubmed PY - 2004/6/30/medline PY - 2004/5/28/entrez SP - 625 EP - 35 JF - Cell JO - Cell VL - 117 IS - 5 N2 - Although a great deal is known biochemically about peroxiredoxins (Prxs), little is known about their real physiological function. We show here that two cytosolic yeast Prxs, cPrxI and II, which display diversity in structure and apparent molecular weights (MW), can act alternatively as peroxidases and molecular chaperones. The peroxidase function predominates in the lower MW forms, whereas the chaperone function predominates in the higher MW complexes. Oxidative stress and heat shock exposure of yeasts causes the protein structures of cPrxI and II to shift from low MW species to high MW complexes. This triggers a peroxidase-to-chaperone functional switch. These in vivo changes are primarily guided by the active peroxidase site residue, Cys(47), which serves as an efficient "H(2)O(2)-sensor" in the cells. The chaperone function of these proteins enhances yeast resistance to heat shock. SN - 0092-8674 UR - https://www.unboundmedicine.com/medline/citation/15163410/Two_enzymes_in_one L2 - https://linkinghub.elsevier.com/retrieve/pii/S0092867404004878 DB - PRIME DP - Unbound Medicine ER -