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Unrelated solubility‐enhancing fusion partners MBP and NusA utilize a similar mode of action
Author(s) -
RaranKurussi Sreejith,
Waugh David S.
Publication year - 2014
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.25317
Subject(s) - maltose binding protein , escherichia coli , fusion protein , solubility , chaperone (clinical) , chemistry , fusion , protein folding , recombinant dna , solubilization , biochemistry , folding (dsp implementation) , overproduction , mode of action , biophysics , biology , gene , medicine , linguistics , philosophy , organic chemistry , engineering , pathology , electrical engineering
The tendency of recombinant proteins to accumulate in the form of insoluble aggregates in Escherichia coli is a major hindrance to their overproduction. One of the more effective approaches to circumvent this problem is to use translation fusion partners {solubility‐enhancers (SEs)}. E. coli maltose‐binding protein (MBP) and N‐utilization substance A (NusA) are arguably the most effective solubilizing agents that have been discovered so far. Here, we show that although these two proteins are structurally, functionally, and physicochemically distinct, they influence the solubility and folding of their fusion partners in a very similar manner. These SEs act as “holdases” that prevent the aggregation of their fusion partners. Subsequent folding of the passenger proteins, when it occurs, is either spontaneous or chaperone‐mediated. Biotechnol. Bioeng. 2014;111: 2407–2411. © 2014 Wiley Periodicals, Inc.