Unrelated solubility-enhancing fusion partners MBP and NusA utilize a similar mode of action.
Biotechnol Bioeng
; 111(12): 2407-11, 2014 Dec.
Article
em En
| MEDLINE
| ID: mdl-24942647
ABSTRACT
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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Fatores de Transcrição
/
Proteínas Recombinantes de Fusão
/
Fatores de Alongamento de Peptídeos
/
Proteínas de Escherichia coli
/
Proteínas Ligantes de Maltose
Idioma:
En
Ano de publicação:
2014
Tipo de documento:
Article