» Articles » PMID: 3622735

Fusion Polypeptides in Gene Cloning: Potential Problems Due to Conformational Alterations at the Junction

Overview
Journal Experientia
Specialty Science
Date 1987 Aug 15
PMID 3622735
Authors
Affiliations
Soon will be listed here.
Abstract

Many eukaryotic genes are cloned in bacterial hosts as fusion polypeptides. Prediction of the secondary structures for some common prokaryotic fusion polypeptides shows that many junction sites correspond to important secondary structures. It is suggested that such structures could affect (hinder, etc.) the conformation or drive the folding of the neighboring eukaryotic counterparts. Thus the prokaryotic junction should be better performed in random coil regions, or short fusion prokaryotic polypeptides should be used.

References
1.
KYTE J, Doolittle R . A simple method for displaying the hydropathic character of a protein. J Mol Biol. 1982; 157(1):105-32. DOI: 10.1016/0022-2836(82)90515-0. View

2.
Williams D, Van Frank R, Muth W, Burnett J . Cytoplasmic inclusion bodies in Escherichia coli producing biosynthetic human insulin proteins. Science. 1982; 215(4533):687-9. DOI: 10.1126/science.7036343. View

3.
Parrilla A, Domenech A, Querol E . A Pascal microcomputer program for prediction of protein secondary structure and hydropathic segments. Comput Appl Biosci. 1986; 2(3):211-5. DOI: 10.1093/bioinformatics/2.3.211. View

4.
Chou P, Fasman G . Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol Relat Areas Mol Biol. 1978; 47:45-148. DOI: 10.1002/9780470122921.ch2. View

5.
Winther M, Allen G, Bomford R, Brown F . Bacterially expressed antigenic peptide from foot-and-mouth disease virus capsid elicits variable immunologic responses in animals. J Immunol. 1986; 136(5):1835-40. View