Biosynthesis of a stable allophycocyanin beta subunit in metabolically engineered Escherichia coli

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	Biosynthesis of a stable allophycocyanin beta subunit in metabolically engineered Escherichia coli
	Chen, Huaxin 1; Lin, Hanzhi 1,2; Li, Fuchao 1; Jiang, Peng 1; Qin, Song 3
刊名	JOURNAL OF BIOSCIENCE AND BIOENGINEERING
	2013-05-01
卷号	115 期号:5 页码:485-489
关键词	Allophycocyanin Biosynthesis Escherichia coli Fluorescence Thermostability
ISSN号	1389-1723
通讯作者	Jiang, P
中文摘要	Allophycocyanin (APC) is widely used as a fluorescent tag for fluorescence detection techniques. In this study, the alpha pcB gene from a thermophilic cyanobacterium strain was cloned and ligated into an expression vector to construct a pathway for the biosynthesis of an allophycocyanin beta subunit (holo-apcBT) in Escherichia coli. Isopropyl beta-D-1-thiogalactopyranoside induction successfully reconstituted holo-apcBT in E. coli. The recombinant holo-apcB showed spectroscopic properties similar to native APC. The stability and spectroscopic properties of this protein were then compared with another recombinant allophycocyanin beta subunit (holo-apcBM) whose apcB gene was cloned from mesophilic cyanobacterium. At high temperatures and during the course of storage, holo-apcBT was significantly more stable than holo-apcBM. In addition, holo-apcBT had an unexpectedly higher extinction coefficient and fluorescence quantum yield than holo-apcBM, suggesting that holo-apcBT would be a promising fluorescent tag and serve as a substitute for native APC. (c) 2012, The Society for Biotechnology, Japan. All rights reserved.
英文摘要	Allophycocyanin (APC) is widely used as a fluorescent tag for fluorescence detection techniques. In this study, the alpha pcB gene from a thermophilic cyanobacterium strain was cloned and ligated into an expression vector to construct a pathway for the biosynthesis of an allophycocyanin beta subunit (holo-apcBT) in Escherichia coli. Isopropyl beta-D-1-thiogalactopyranoside induction successfully reconstituted holo-apcBT in E. coli. The recombinant holo-apcB showed spectroscopic properties similar to native APC. The stability and spectroscopic properties of this protein were then compared with another recombinant allophycocyanin beta subunit (holo-apcBM) whose apcB gene was cloned from mesophilic cyanobacterium. At high temperatures and during the course of storage, holo-apcBT was significantly more stable than holo-apcBM. In addition, holo-apcBT had an unexpectedly higher extinction coefficient and fluorescence quantum yield than holo-apcBM, suggesting that holo-apcBT would be a promising fluorescent tag and serve as a substitute for native APC. (c) 2012, The Society for Biotechnology, Japan. All rights reserved.
学科主题	Biotechnology & Applied Microbiology ; Food Science & Technology
WOS标题词	Science & Technology ; Life Sciences & Biomedicine
类目[WOS]	Biotechnology & Applied Microbiology ; Food Science & Technology
研究领域[WOS]	Biotechnology & Applied Microbiology ; Food Science & Technology
关键词[WOS]	SYNECHOCOCCUS SP PCC-7002 ; C-PHYCOCYANIN ; CYANOBACTERIAL PHYCOBILIPROTEINS ; CPCS-I ; PROTEIN ; LYASE ; BIOGENESIS ; STABILITY ; PEPTIDES ; TRIMER
收录类别	SCI
原文出处	10.1016/j.jbiosc.2012.11.008
语种	英语
WOS记录号	WOS:000320208600004
公开日期	2014-07-17
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/16534]
专题	海洋研究所_实验海洋生物学重点实验室
作者单位	1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100039, Peoples R China 3.Chinese Acad Sci, Yantai Inst Coastal Zone Res, Yantai 264003, Peoples R China
推荐引用方式 GB/T 7714	Chen, Huaxin,Lin, Hanzhi,Li, Fuchao,et al. Biosynthesis of a stable allophycocyanin beta subunit in metabolically engineered Escherichia coli[J]. JOURNAL OF BIOSCIENCE AND BIOENGINEERING,2013,115(5):485-489.
APA	Chen, Huaxin,Lin, Hanzhi,Li, Fuchao,Jiang, Peng,&Qin, Song.(2013).Biosynthesis of a stable allophycocyanin beta subunit in metabolically engineered Escherichia coli.JOURNAL OF BIOSCIENCE AND BIOENGINEERING,115(5),485-489.
MLA	Chen, Huaxin,et al."Biosynthesis of a stable allophycocyanin beta subunit in metabolically engineered Escherichia coli".JOURNAL OF BIOSCIENCE AND BIOENGINEERING 115.5(2013):485-489.