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The solubility and stability of recombinant proteins are increased by their fusion to NusA.

Abstract：

:The new bacterial vector pETM60 enables the expression of His-tagged recombinant proteins fused to the C-terminus of NusA through a TEV protease recognition sequence. Three sequences coding for two protein domains (Xklp3A and Tep3Ag) and one membrane-bound viral protein (E8R) could not be expressed in a soluble form in bacteria. Their GST-fusions were mostly soluble but quickly degraded during purification. The same sequences cloned in pETM60 were efficiently purified by metal affinity and recovered soluble after the removal of the fusion partner. The NusA-fused constructs enabled to yield 13-20mg of fusion protein per litre of culture and 2.5-5mg of pure protein per litre of culture. Structural analysis indicated that the purified proteins were monodispersed and correctly folded. NusA has been used to raise antibodies that have been successfully used for Western blot and immunoprecipitation of NusA fusion proteins.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

De Marco V,Stier G,Blandin S,de Marco A

doi

10.1016/j.bbrc.2004.07.189

subject

Has Abstract

pub_date

2004-09-24 00:00:00

pages

766-71

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(04)01693-6

journal_volume

322

pub_type

杂志文章

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