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The C-terminal region controls correct folding of genus Trametes pyranose 2-oxidases

Paper ID Volume ID Publish Year Pages File Format Full-Text
25217 43561 2007 7 PDF Available
Title
The C-terminal region controls correct folding of genus Trametes pyranose 2-oxidases
Abstract

The pyranose 2-oxidases from Trametes ochracea and Trametes pubescens share markedly similar amino acid sequences with identity of 93.4%. When expressed from the recombinant plasmids based on the same vector in the Escherichia coli host strain BL21(DE3) at higher growth temperatures, they differ strikingly in the formation of the inclusion bodies. Upon overexpression in the cultures performed at 28 °C, the specific activity of pyranose 2-oxidase from T. pubescens was eight times higher than that from T. ochracea: 93% of pyranose 2-oxidase from T. ochracea and only 15% of that from T. pubescens was present in the form of inclusion bodies. To ascertain the cause of this difference, both cloned genes were shuffled. Site-directed recombination of p2o cDNAs revealed that DNA constructs ending with 3′ end of p2o cDNA from T. pubescens code for proteins that are folded into an active form to the greater extent, regardless of the gene expression level. “In silicio” analysis of physico-chemical properties of the protein sequences of pyranose 2-oxidases revealed that the sequence of amino acid residues 368–430, constituting the small, head domain of pyranose 2-oxidase from T. pubescens, affects positively the enzyme folding at higher cultivation temperatures. The domain differs in six amino acid residues from that of T. ochracea.

Keywords
Pyranose 2-oxidase; Recombinant protein; Inclusion body; Site-directed recombination
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The C-terminal region controls correct folding of genus Trametes pyranose 2-oxidases
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Biotechnology - Volume 130, Issue 3, 30 June 2007, Pages 229–235
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