Open AccessThe remarkable solubility-enhancing power of Escherichia coli maltose-binding protein
Author(s) -
David S. Waugh
Publication year - 2016
Publication title -
postępy biochemii
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.244
H-Index - 15
ISSN - 0032-5422
DOI - 10.18388/pb.2016_41
Subject(s) - maltose binding protein , escherichia coli , inclusion bodies , solubility , chemistry , fusion protein , biochemistry , recombinant dna , protein folding , maltose , folding (dsp implementation) , enhancer , organic chemistry , enzyme , gene expression , engineering , electrical engineering , gene
A common problem encountered during the production of recombinant proteins, particularly in bacteria, is their tendency to accumulate in an insoluble and inactive form (i.e., as inclusion bodies). Although sometimes it is possible to convert the aggregated material into native, biologically active protein, this is a time-consuming, costly, and uncertain undertaking. Consequently, a general means of circumventing the formation of inclusion bodies is highly desirable. During the 1990s, it was serendipitously discovered that certain highly soluble proteins have the ability to enhance the solubility of their fusion partners, thereby preventing them from forming insoluble aggregates. In the ensuing years, Escherichia coli maltose-binding protein (MBP) has emerged as one of the most effective solubility enhancers. Moreover, once rendered soluble by fusion to MBP, many proteins are able to fold into their biologically active conformations. This brief review article focuses on our current understanding of what makes MBP such an effective solubility enhancer and how it facilitates the proper folding of its fusion partners.