An insight into fusion technology aiding efficient recombinant protein production for functional proteomics.

Abstract:

:Advancements in peptide fusion technologies to maximize the protein production has taken a big leap to fulfill the demands of post-genomics era targeting elucidation of structure/function of the proteome and its therapeutic applications, by over-expression in heterologous expression systems. Despite being most preferred protein expression system armed with variety of cardinal fusion tags, expression of the functionally active recombinant protein in E. coli remains plagued. The present review critically analyses the aptness of well-characterized fusion tags utilized for over-expression of recombinant proteins with improved solubility and their compatibility with downstream purification procedures. The combinatorial tandem affinity strategies have shown to provide more versatile options. Solubility decreasing fusion tags have proved to facilitate the overproduction of antimicrobial peptides. Efficient removal of fusion tags prior to final usage is of utmost importance and has been summarized discussing the efficiency of various enzymatic and chemical methods of tag removal. Unfortunately, no single fusion tag works as a magic bullet to completely fulfill the requirements of protein expression and purification in active form. The information provided might help in selection and development of a successful protocol for efficient recombinant protein production for functional proteomics.

journal_name

Arch Biochem Biophys

authors

Yadav DK,Yadav N,Yadav S,Haque S,Tuteja N

doi

10.1016/j.abb.2016.10.012

subject

Has Abstract

pub_date

2016-12-15 00:00:00

pages

57-77

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(16)30424-6

journal_volume

612

pub_type

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