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Thermostable Lichenase from Clostridium thermocellum as a Host Protein in the Domain Insertion Approachстатья
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 15 февраля 2024 г.
- Авторы: Pavlenko O.S., Gra O.A., Mustafaev O.N., Kabarbaeva K.V., Sadovskaya N.S., Tyurin A.A., Fadeev V.S., Goldenkova-Pavlova I.V.
- Журнал: Biochemistry (Moscow)
- Том: 84
- Номер: 8
- Год издания: 2019
- Издательство: Pleiades Publishing, Ltd
- Местоположение издательства: Road Town, United Kingdom
- Первая страница: 931
- Последняя страница: 940
- DOI: 10.1134/s0006297919080091
- Аннотация: Clostridium thermocellum lichenase (endo-β-1,3;1,4-glucan-D-glycosyl hydrolase, EC 3.2.1.73 (P29716)) has been tested for the insertion of two model fluorescent proteins (EGFP and TagRFP) into two regions of this enzyme. Functional folding of the resulting proteins was confirmed by retention of lichenase activity and EGFP and TagRFP fluorescence. These results convincingly demonstrate that (i) the two experimentally selected lichenase loop regions may serve as the areas for domain insertion without disturbing enzyme folding in vivo; (ii) lichenase permits not only single but also tandem insertions of large protein domains. High specific activity, outstanding thermostability, and efficient in vitro refolding of thermostable lichenase make it an attractive new host protein for the insertional fusion of domains in the engineering of multifunctional proteins.
- Добавил в систему: Садовская Наталия Сергеевна