An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone

•An additional cysteine promotes functional switching in 2-Cys Prx.•An additional cysteine triggers the oligomerization of 2Cys-Prx protein.•An additional cysteine increases chaperone function of 2-Cys Prx. Peroxiredoxins (Prx) have received considerable attention during recent years. This study dem...

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Bibliographic Details
Published in:FEBS letters 2015-09, Vol.589 (19), p.2831-2840
Main Authors: An, Byung Chull, Lee, Seung Sik, Jung, Hyun Suk, Kim, Jin Young, Lee, Yuno, Lee, Keun Woo, Lee, Sang Yeol, Tripathi, Bhumi Nath, Chung, Byung Yeoup
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Chaperone
Conserved Sequence
Cysteine
Disulfides - chemistry
Hydrophobic and Hydrophilic Interactions
Molecular Chaperones - metabolism
Molecular Sequence Data
Molecular Weight
Peroxidase
Peroxiredoxin
Peroxiredoxins - chemistry
Peroxiredoxins - metabolism
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Secondary
Pseudomonas
Pseudomonas aeruginosa - enzymology
Pseudomonas putida - enzymology
Species Specificity
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Summary:•An additional cysteine promotes functional switching in 2-Cys Prx.•An additional cysteine triggers the oligomerization of 2Cys-Prx protein.•An additional cysteine increases chaperone function of 2-Cys Prx. Peroxiredoxins (Prx) have received considerable attention during recent years. This study demonstrates that two typical Pseudomonas-derived 2-Cys Prx proteins, PpPrx and PaPrx can alternatively function as a peroxidase and chaperone. The amino acid sequences of these two Prx proteins exhibit 93% homology, but PpPrx possesses an additional cysteine residue, Cys112, instead of the alanine found in PaPrx. PpPrx predominates with a high molecular weight (HMW) complex and chaperone activity, whereas PaPrx has mainly low molecular weight (LMW) structures and peroxidase activity. Mass spectrometry and structural analyses showed the involvement of Cys112 in the formation of an inter-disulfide bond, the instability of LMW structures, the formation of HMW complexes, and increased hydrophobicity leading to functional switching of Prx proteins between peroxidase and chaperone.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2015.07.046