Overproduced <Emphasis Type="Italic">Brucella abortus</Emphasis> PdhS-mCherry forms soluble aggregates in <Emphasis Type="Italic">Escherichia coli</Emphasis>, partially associating with mobile foci of IbpA-YFP |
| |
| Authors: | Charles Van der Henst Caroline Charlier Michaël Deghelt Johan Wouters Jean-Yves Matroule Jean-Jacques Letesson Xavier De Bolle |
| |
| Institution: | (1) Molecular Biology Research Unit (URBM), University of Namur (FUNDP), 61 rue de Bruxelles, 5000 Namur, Belgium;(2) Theoretical and Structural Physical Chemistry Unit (UCPTS), University of Namur (FUNDP), 61 rue de Bruxelles, 5000 Namur, Belgium |
| |
| Abstract: | Background When heterologous recombinant proteins are produced in Escherichia coli, they often precipitate to form insoluble aggregates of unfolded polypeptides called inclusion bodies. These structures are
associated with chaperones like IbpA. However, there are reported cases of "non-classical" inclusion bodies in which proteins
are soluble, folded and active. |
| |
| Keywords: | |
| 本文献已被 SpringerLink 等数据库收录！ |
|
