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논문 기본 정보
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- 학술저널
- 저자정보
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- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제25권 제4호
- 발행연도
- 2015.1
- 수록면
- 503 - 510 (8page)
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The iLOV protein belongs to a family of blue-light photoreceptor proteins containing a lightoxygen- voltage sensing domain with a noncovalently bound flavin mononucleotide (FMN) as its chromophore. Owing to advantages such as its small size, oxygen-independent nature, and pH stability, iLOV is an ideal candidate over other reporter fluorescent proteins such as GFP and DsRed. Here, for the first time, we describe the feasibility of applying LOV domain-based fluorescent iLOV as a metal sensor by measuring the fluorescence quenching of a protein with respect to the concentration of metal ions. In the present study, we demonstrated the inherent copper sensing property of the iLOV protein and identified the possible amino acids responsible for metal binding. The fluorescence quenching upon exposure to Cu2+ was highly sensitive and exhibited reversibility upon the addition of the metal chelator EDTA. The copper binding constant was found to be 4.72 ± 0.84 μM. In addition, Cu2+-bound iLOV showed high fluorescence quenching at near physiological pH. Further computational analysis yielded a better insight into understanding the possible amino acids responsible for Cu2+ binding with the iLOV protein.
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참고문헌 (23)
참고문헌 신청
Ayyadurai N / / Bioconjugation of l-3,4-dihydroxyphenylalanine-containing protein with a polysaccharide / Bioconjug. Chem 22 : 551 ~ 555
Ayyadurai N / 2011 / Development of a selective, sensitive, and reversible biosensor by the genetic incorporation of a metal-binding site into green fluorescent protein / Ang
Balint EE / 2013 / Fluorescence of a histidine-modified enhanced green fluorescent protein (EGFP) effectively quenched by copper(II) ions / J. Fluoresc 23 : 273 ~ 281
Chapman S / 2008 / The photoreversible fluorescent protein iLOV outperforms GFP as a reporter of plant virus infection / Proc. Natl. Acad. Sci. USA 105 : 20038 ~ 20043
Christie JM / / Structural tuning of the fluorescent protein iLOV for improved photostability / J. Biol. Chem 287 : 22295 ~ 22304
Ayyadurai N / 2011 / Development of a selective, sensitive, and reversible biosensor by the genetic incorporation of a metal-binding site into green fluorescent protein / Ang
Balint EE / 2013 / Fluorescence of a histidine-modified enhanced green fluorescent protein (EGFP) effectively quenched by copper(II) ions / J. Fluoresc 23 : 273 ~ 281
Chapman S / 2008 / The photoreversible fluorescent protein iLOV outperforms GFP as a reporter of plant virus infection / Proc. Natl. Acad. Sci. USA 105 : 20038 ~ 20043
Christie JM / / Structural tuning of the fluorescent protein iLOV for improved photostability / J. Biol. Chem 287 : 22295 ~ 22304
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