Preparation and properties of Clostridium thermocellum lichenase deletion variants and their use for construction of bifunctional hybrid proteins

被引:7
作者
Musiychuk, KA [1 ]
Goldenkova, IV [1 ]
Abdeev, RM [1 ]
Kobets, NS [1 ]
Piruzian, ES [1 ]
机构
[1] Russian Acad Sci, Vavilov Inst Gen Genet, Moscow 117809, Russia
基金
俄罗斯基础研究基金会;
关键词
thermostable lichenase (beta-1,3-1,4-glucanase); green fluorescent protein (GFP); reporter systems; hybrid bifunctional proteins;
D O I
10.1023/A:1002804923384
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Major properties (pH and temperature optimum, stability) of lichenase (beta -1,3-1,4-glucanase) deletion variants from Clostridium thermocellum were comparatively studied. The deletion variant LicBM2 was used to create hybrid bifunctional proteins by fusion with sequences of the green fluorescent protein (GFP) from Aequorea victoria. The data show that in hybrid proteins both GFP and lichenase retain their major properties, namely, GFP remains a fluorescent protein and the lichenase retains activity and high thermostability. Based on the results of this investigation and results that have been obtained earlier, the use of the deletion variants of lichenase and the bifunctional hybrid proteins as reporter proteins is suggested.
引用
收藏
页码:1397 / 1402
页数:6
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