کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1925143 1536346 2014 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Role of the disaggregase ClpB in processing of proteins aggregated as inclusion bodies
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Role of the disaggregase ClpB in processing of proteins aggregated as inclusion bodies
چکیده انگلیسی


• Overproduction of aggregation-prone proteins induces the ClpB accumulation.
• ClpB associates with inclusion bodies (IBs) in E. coli cells.
• The loss of ClpB increases the level of IB accumulation in E. coli cells.
• ClpB plays an important role in the IB processing.

Overproduction of heterologous proteins in bacterial systems often results in the formation of insoluble inclusion bodies (IBs), which is a major impediment in biochemical research and biotechnology. In principle, the activity of molecular chaperones could be employed to gain control over the IB formation and to improve the recombinant protein yields, but the potential of each of the major bacterial chaperones (DnaK/J, GroEL/ES, and ClpB) to process IBs has not been fully established yet. We investigated the formation of inclusion bodies (IBs) of two aggregation-prone proteins, VP1LAC and VP1GFP, overproduced in Escherichiacoli in the presence and absence of the chaperone ClpB. We found that both ClpB isoforms, ClpB95 and ClpB80 accumulated in E. coli cells during the production of IBs. The amount of IB proteins increased in the absence of ClpB. ClpB supported the resolubilization and reactivation of the aggregated VP1LAC and VP1GFP in E. coli cells. The IB disaggregation was optimal in the presence of both ClpB95 and ClpB80. Our results indicate an essential role of ClpB in controlling protein aggregation and inclusion body formation in bacteria.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Archives of Biochemistry and Biophysics - Volumes 555–556, August 2014, Pages 23–27
نویسندگان
, , , ,