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학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
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논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 발행연도
- 2016.8
- 수록면
- 594 - 602 (9page)
- DOI
- molcells.2016.0042
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초록· 키워드
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Alkyl hydroperoxide reductase subunit C from Pseudomonas aeruginosa PAO1 (PaAhpC) is a member of the 2-Cys peroxiredoxin family. Here, we examined the peroxidase and molecular chaperone functions of PaAhpC using a site-directed mutagenesis approach by substitution of Ser and Thr residues with Cys at positions 78 and 105 located between two catalytic cysteines. Substitution of Ser with Cys at position 78 enhanced the chaperone activity of the mutant (S78C-PaAhpC) by approximately 9-fold compared with that of the wild-type protein (WT-PaAhpC). This increased activity may have been associated with the proportionate increase in the high-molecular-weight (HMW) fraction and enhanced hydrophobicity of S78C-PaAhpC. Homology modeling revealed that mutation of Ser78 to Cys78 resulted in a more compact decameric structure than that observed in WT-PaAhpC and decreased the atomic distance between the two neighboring sulfur atoms of Cys78 in the dimer-dimer interface of S78C-PaAhpC, which could be responsible for the enhanced hydrophobic interaction at the dimer-dimer interface. Furthermore, complementation assays showed that S78C-PaAhpC exhibited greatly improved the heat tolerance, resulting in enhanced survival under thermal stress. Thus, addition of Cys at position 78 in PaAhpC modulated the functional shifting of this protein from a peroxidase to a chaperone.
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참고문헌 (32)
참고문헌 신청
안병철 / 2010 / A New Antioxidant with Dual Functions as a Peroxidase and Chaperone in Pseudomonas aeruginosa / Molecules and Cells 29(2):145~151
An, B. C. / 2011 / Functional switching of a novel prokaryotic 2-Cys peroxiredoxin(PpPrx)under oxidative stress / Cell Stress Chap 16:317~328
An, B. C. / 2015 / An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone / FEBS Lett 589:2831~2840
Angelucci, F. / 2013 / Switching between the alternative structures and functions of a 2-Cys peroxiredoxin, by site-directed mutagenesis / J. Mol. Biol 425:4556~4568
Bhatt, I. / 2011 / Plant peroxiredoxin : catalytic mechanisms, functional significance and future perspectives / Biotechnol. Adv 29:850~859
An, B. C. / 2011 / Functional switching of a novel prokaryotic 2-Cys peroxiredoxin(PpPrx)under oxidative stress / Cell Stress Chap 16:317~328
An, B. C. / 2015 / An additional cysteine in a typical 2-Cys peroxiredoxin of Pseudomonas promotes functional switching between peroxidase and molecular chaperone / FEBS Lett 589:2831~2840
Angelucci, F. / 2013 / Switching between the alternative structures and functions of a 2-Cys peroxiredoxin, by site-directed mutagenesis / J. Mol. Biol 425:4556~4568
Bhatt, I. / 2011 / Plant peroxiredoxin : catalytic mechanisms, functional significance and future perspectives / Biotechnol. Adv 29:850~859
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