Preventing protein aggregation by its hyper-acidic fusion cognates in Escherichia coli.

Abstract:

:Preventing protein aggregation is crucial for various protein studies, and has a large potential for remedy of protein misfolding or aggregates-linked diseases. In this study, we demonstrated the hyper-acidic protein fusion partners, which were previously reported to enhance the soluble expression of aggregation-prone proteins, could also significantly prevent aggregation (or improve the solubility) of disease-associated and amyloid/fibril-forming polypeptides such as TEL-SAM and Aβ42 in Escherichia coli cells. Further and most importantly, the solubility of all poorly soluble target proteins examined was greatly elevated by their corresponding highly soluble hyper-acidic fusion cognates when they were co-expressed, in despite of a concomitant compromise of the cognates' solubility. The extent of such a solubility enhancement appeared to be in parallel with the ratio of the levels of co-expressed hyper-acidic fusion cognate and target protein. The hyper-acidic fusion cognates might function as intermolecular solubilizing effectors to prevent aggregation of the target proteins, and a plausible model for interpreting these results is also proposed.

journal_name

Protein Expr Purif

authors

Zou Z,Fan Y,Zhang C

doi

10.1016/j.pep.2011.06.004

subject

Has Abstract

pub_date

2011-11-01 00:00:00

pages

138-44

issue

1

eissn

1046-5928

issn

1096-0279

pii

S1046-5928(11)00151-3

journal_volume

80

pub_type

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