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Escherichia coli-based expression of functional novel DNA-binding histone H1 from Carassius auratus

Paper ID Volume ID Publish Year Pages File Format Full-Text
18236 42715 2007 7 PDF Available
Title
Escherichia coli-based expression of functional novel DNA-binding histone H1 from Carassius auratus
Abstract

Histones are DNA-binding proteins that assist in DNA packaging and protection. Here, we, for the first time, cloned a novel histone H1 cDNA (638 bp) from the goldfish, Carassius auratus. Sequencing revealed that this histone H1 shared 68.1% amino acid identity and 73.9% similarity with that from the rainbow trout, Salmo gairdneri. We successfully expressed a full-length recombinant version (∼20 kDa) and a truncated C-terminal fragment (∼6 kDa; 61 amino acids) of this histone H1 as a partially soluble form using a maltose binding protein (MBP) fusion strategy in an Escherichia coli expression system. Our results revealed that both these recombinant histone H1 versions had DNA binding and protection functions, and MBP fusion system was an effective way to produce biological functional recombinant histone proteins in E. coli. This novel recombinant histone H1 protein and/or its C-terminal peptide could be used as potential mediators for efficacious gene delivery.

Keywords
Histone H1; C-terminal peptide; DNA-binding protein; Carassius auratus; Goldfish; Escherichia coli
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Escherichia coli-based expression of functional novel DNA-binding histone H1 from Carassius auratus
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 40, Issue 6, 2 May 2007, Pages 1484–1490
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us