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Phosphorylation and concomitant structural changes in human 2-Cys peroxiredoxin isotype I differentially regulate its peroxidase and molecular chaperone functions.
FEBS Lett. 2006 Jan 09; 580(1):351-5.FL

Abstract

The H2O2-catabolizing peroxidase activity of human peroxiredoxin I (hPrxI) was previously shown to be regulated by phosphorylation of Thr90. Here, we show that hPrxI forms multiple oligomers with distinct secondary structures. HPrxI is a dual function protein, since it can behave either as a peroxidase or as a molecular chaperone. The effects of phosphorylation of hPrxI on its protein structure and dual functions were determined using site-directed mutagenesis, in which the phosphorylation site was substituted with aspartate to mimic the phosphorylated status of the protein (T90D-hPrxI). Phosphorylation of the protein induces significant changes in its protein structure from low molecular weight (MW) protein species to high MW protein complexes as well as its dual functions. In contrast to the wild type (WT)- and T90A-hPrxI, the T90D-hPrxI exhibited a markedly reduced peroxidase activity, but showed about sixfold higher chaperone activity than WT-hPrxI.

Links

Publisher Full Text
linkinghub.elsevier.com
doi.org

Authors+Show Affiliations

Jang HH
Environmental Biotechnology National Core Research Center, Gyeongsang National University, Jinju 660-701, Republic of Korea.
Kim SY
No affiliation info available
Park SK
No affiliation info available
Jeon HS
No affiliation info available
Lee YM
No affiliation info available
Jung JH
No affiliation info available
Lee SY
No affiliation info available
Chae HB
No affiliation info available
Jung YJ
No affiliation info available
Lee KO
No affiliation info available
Lim CO
No affiliation info available
Chung WS
No affiliation info available
Bahk JD
No affiliation info available
Yun DJ
No affiliation info available
Cho MJ
No affiliation info available
Lee SY
No affiliation info available

MeSH

Amino Acid SubstitutionHumansHydrogen PeroxideIsoenzymesMolecular ChaperonesPeroxidasesPeroxiredoxinsPhosphorylationPoint MutationProtein Structure, TertiaryStructure-Activity Relationship

Pub Type(s)

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

Language

eng

PubMed ID

16376335

Citation

Jang, Ho Hee, et al. "Phosphorylation and Concomitant Structural Changes in Human 2-Cys Peroxiredoxin Isotype I Differentially Regulate Its Peroxidase and Molecular Chaperone Functions." FEBS Letters, vol. 580, no. 1, 2006, pp. 351-5.
Jang HH, Kim SY, Park SK, et al. Phosphorylation and concomitant structural changes in human 2-Cys peroxiredoxin isotype I differentially regulate its peroxidase and molecular chaperone functions. FEBS Lett. 2006;580(1):351-5.
Jang, H. H., Kim, S. Y., Park, S. K., Jeon, H. S., Lee, Y. M., Jung, J. H., Lee, S. Y., Chae, H. B., Jung, Y. J., Lee, K. O., Lim, C. O., Chung, W. S., Bahk, J. D., Yun, D. J., Cho, M. J., & Lee, S. Y. (2006). Phosphorylation and concomitant structural changes in human 2-Cys peroxiredoxin isotype I differentially regulate its peroxidase and molecular chaperone functions. FEBS Letters, 580(1), 351-5.
Jang HH, et al. Phosphorylation and Concomitant Structural Changes in Human 2-Cys Peroxiredoxin Isotype I Differentially Regulate Its Peroxidase and Molecular Chaperone Functions. FEBS Lett. 2006 Jan 9;580(1):351-5. PubMed PMID: 16376335.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Phosphorylation and concomitant structural changes in human 2-Cys peroxiredoxin isotype I differentially regulate its peroxidase and molecular chaperone functions. AU - Jang,Ho Hee, AU - Kim,Sun Young, AU - Park,Soo Kwon, AU - Jeon,Hye Sook, AU - Lee,Young Mee, AU - Jung,Ji Hyun, AU - Lee,Sun Yong, AU - Chae,Ho Byoung, AU - Jung,Young Jun, AU - Lee,Kyun Oh, AU - Lim,Chae Oh, AU - Chung,Woo Sik, AU - Bahk,Jeong Dong, AU - Yun,Dae-Jin, AU - Cho,Moo Je, AU - Lee,Sang Yeol, Y1 - 2005/12/19/ PY - 2005/11/15/received PY - 2005/12/08/accepted PY - 2005/12/27/pubmed PY - 2006/2/16/medline PY - 2005/12/27/entrez SP - 351 EP - 5 JF - FEBS letters JO - FEBS Lett VL - 580 IS - 1 N2 - The H2O2-catabolizing peroxidase activity of human peroxiredoxin I (hPrxI) was previously shown to be regulated by phosphorylation of Thr90. Here, we show that hPrxI forms multiple oligomers with distinct secondary structures. HPrxI is a dual function protein, since it can behave either as a peroxidase or as a molecular chaperone. The effects of phosphorylation of hPrxI on its protein structure and dual functions were determined using site-directed mutagenesis, in which the phosphorylation site was substituted with aspartate to mimic the phosphorylated status of the protein (T90D-hPrxI). Phosphorylation of the protein induces significant changes in its protein structure from low molecular weight (MW) protein species to high MW protein complexes as well as its dual functions. In contrast to the wild type (WT)- and T90A-hPrxI, the T90D-hPrxI exhibited a markedly reduced peroxidase activity, but showed about sixfold higher chaperone activity than WT-hPrxI. SN - 0014-5793 UR - https://www.unboundmedicine.com/medline/citation/16376335/Phosphorylation_and_concomitant_structural_changes_in_human_2_Cys_peroxiredoxin_isotype_I_differentially_regulate_its_peroxidase_and_molecular_chaperone_functions_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0014-5793(05)01491-2 DB - PRIME DP - Unbound Medicine ER -