An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone.
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.
Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup 580-185, Republic of Korea.
Byung Chull
BC
An
Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup 580-185, Republic of Korea.
Seung Sik
SS
Lee
Department of Biochemistry, College of Natural Sciences, Kangwon National University, Chuncheon 200-701, Republic of Korea.
Hyun Suk
HS
Jung
Division of Mass Spectrometry Research, Korea Basic Science Institute, 162 Yeongudanjiro, Ochang 363-883, Republic of Korea.
Jin Young
JY
Kim
Division of Applied Life Science (Brain Korea 21 Program), Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Republic of Korea.
Yuno
Y
Lee
Division of Applied Life Science (Brain Korea 21 Program), Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Republic of Korea.
Keun Woo
KW
Lee
Division of Applied Life Science (Brain Korea 21 Program), Gyeongsang National University, 501 Jinju-daero, Jinju 660-701, Republic of Korea.
Sang Yeol
SY
Lee
Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup 580-185, Republic of Korea.
Bhumi Nath
BN
Tripathi
Advanced Radiation Technology Institute, Korea Atomic Energy Research Institute, 29 Geumgu-gil, Jeongeup 580-185, Republic of Korea. Electronic address: bychung@kaeri.re.kr.
Byung Yeoup
BY
Chung
D000595:Amino Acid Sequence; D017124:Conserved Sequence; D003545:Cysteine; D004220:Disulfides / Q000737:chemistry; D057927:Hydrophobic and Hydrophilic Interactions; D018832:Molecular Chaperones / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D054464:Peroxiredoxins / Q000737:chemistry* / Q000378:metabolism*; D055503:Protein Multimerization; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D016958:Pseudomonas putida / Q000201:enzymology*; D013045:Species Specificity
D004220:Disulfides; D018832:Molecular Chaperones; D054464:Peroxiredoxins; D003545:Cysteine
Chaperone; Cysteine; Peroxidase; Peroxiredoxin; Pseudomonas