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

作者：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^*

来源：FEBS LETTERS, 2015, 589(19): 2831-2840.

DOI：10.1016/j.febslet.2015.07.046

• Chaperone
• Cysteine
• Peroxidase
• Peroxiredoxin
• Pseudomonas

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.

• 出版日期2015-9-14