Mitrocomin from the jellyfish Mitrocoma cellularia with deleted C-terminal tyrosine reveals a higher bioluminescence activity compared to wild type photoprotein

doi:10.1016/j.jphotobiol.2016.06.054

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	Mitrocomin from the jellyfish Mitrocoma cellularia with deleted C-terminal tyrosine reveals a higher bioluminescence activity compared to wild type photoprotein
	Burakova, Ludmila P.1; Natashin, Pavel V.1,2; Markova, Svetlana V.1; Eremeeva, Elena V.1; Malikova, Natalia P.1; Cheng, Chongyun 2; Liu, Zhi-Jie2,3,4 ; Vysotski, Eugene S.1
	2016-09
发表期刊	JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY (IF:3.9[JCR-2023],5.3[5-Year])
ISSN	1011-1344
卷号	162 页码:286-297
发表状态	已发表
DOI	10.1016/j.jphotobiol.2016.06.054
摘要	The full-length cDNA genes encoding five new isoforms of Ca2+-regulated photoprotein mitrocomin from a small tissue sample of the outer bell margin containing photocytes of only one specimen of the luminous jellyfish Mitrocoma cellularia were cloned, sequenced, and characterized after their expression in Escherichia coli and subsequent purification. The analysis of cDNA nucleotide sequences encoding mitrocomin isoforms allowed suggestion that two isoforms might be the products of two allelic genes differing in one amino acid residue (64R/Q) whereas other isotypes appear as a result of transcriptional mutations. In addition, the crystal structure of mitrocomin was determined at 1.30 angstrom resolution which expectedly revealed a high similarity with the structures of other hydromedusan photoproteins. Although mitrocomin isoforms reveal a high degree of identity of amino acid sequences, they vary in specific bioluminescence activities. At that, all isotypes displayed the identical bioluminescence spectra (473-474 nm with no shoulder at 400 nm). Fluorescence spectra of Ca2+-discharged mitrocomins were almost identical to their light emission spectra similar to the case of Ca2+-discharged aequorin, but different from Ca2+-discharged obelins and clytin which fluorescence is red-shifted by 25-30 nm from bioluminescence spectra. The main distinction of mitrocomin from other hydromedusan photoproteins is an additional Tyr at the C-terminus. Using site-directed mutagenesis, we showed that this Tyr is not important for bioluminescence because its deletion even increases specific activity and efficiency of apomitrocomin conversion into active photoprotein, in contrast to C-terminal Pro of other photoproteins. Since genes in a population generally exist as different isoforms, it makes us anticipate the cloning of even more isoforms of mitrocomin and other hydromedusan photoproteins with different bioluminescence properties. (C) 2016 Elsevier B.V. All rights reserved.
收录类别	SCI
语种	英语
资助项目	Ministry of Science and Technology of China[2014CB910400]
WOS研究方向	Biochemistry & Molecular Biology ; Biophysics
WOS类目	Biochemistry & Molecular Biology ; Biophysics
WOS记录号	WOS:000383003800034
出版者	ELSEVIER SCIENCE SA
WOS关键词	GREEN-FLUORESCENT PROTEIN ; MNEMIOPSIS-LEIDYI ; SEQUENCE-ANALYSIS ; CA2+-REGULATED PHOTOPROTEINS ; TRANSCRIPTIONAL FIDELITY ; COELENTERAZINE-BINDING ; MAMMALIAN-CELLS ; MOLECULAR-FORMS ; CDNA CLONING ; APO-OBELIN
原始文献类型	Article
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/1738
专题	iHuman研究所 iHuman研究所_PI研究组_刘志杰组
通讯作者	Liu, Zhi-Jie; Vysotski, Eugene S.
作者单位	1.Russian Acad Sci, Photobiol Lab, Inst Biophys, Siberian Branch, Krasnoyarsk 660036, Russia 2.Chinese Acad Sci, Natl Lab Biomacromol, Inst Biophys, Beijing 100101, Peoples R China 3.Kunming Med Univ, Inst Mol & Clin Med, Kunming 650500, Peoples R China 4.ShanghaiTech Univ, iHuman Inst, Shanghai 201210, Peoples R China
通讯作者单位	iHuman研究所
推荐引用方式 GB/T 7714	Burakova, Ludmila P.,Natashin, Pavel V.,Markova, Svetlana V.,et al. Mitrocomin from the jellyfish Mitrocoma cellularia with deleted C-terminal tyrosine reveals a higher bioluminescence activity compared to wild type photoprotein[J]. JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY,2016,162:286-297.
APA	Burakova, Ludmila P..,Natashin, Pavel V..,Markova, Svetlana V..,Eremeeva, Elena V..,Malikova, Natalia P..,...&Vysotski, Eugene S..(2016).Mitrocomin from the jellyfish Mitrocoma cellularia with deleted C-terminal tyrosine reveals a higher bioluminescence activity compared to wild type photoprotein.JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY,162,286-297.
MLA	Burakova, Ludmila P.,et al."Mitrocomin from the jellyfish Mitrocoma cellularia with deleted C-terminal tyrosine reveals a higher bioluminescence activity compared to wild type photoprotein".JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY B-BIOLOGY 162(2016):286-297.