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Sequence comparison and environmental adaptation of a bacterial endonuclease

Paper ID Volume ID Publish Year Pages File Format Full-Text
15450 1414 2007 10 PDF Available
Title
Sequence comparison and environmental adaptation of a bacterial endonuclease
Abstract

The periplasmic/extracellular bacterial enzyme endonuclease I was chosen as a model system to identify features that might be responsible for temperature- and salt adaptation. A statistical study of amino acid sequence properties belonging to endonuclease I enzymes from three mesophilic habitats (non-marine, brackish water and marine), and three marine temperature groups (psychrophile, intermediate and mesophile) has been conducted. Ten new endonuclease I genes have been sequenced in order to increase the sample size. A bioinformatical method of property dependent statistical analysis of alignments has been applied. To our knowledge this is the first time these methods have been used in order to investigate environmental adaptation of enzymes. Adaptation to low temperature seems to involve increased surface isoelectric point and hydrophobicity in contrast to salt adaptation in which the isoelectric point and hydrophobicity at the surface decreases. Redistribution of charge and hydrophobicity might be the most important signature for cold adaptation and salt adaptation of this enzyme class. The results indicate that general trends of adaptation are possible to elucidate from the amino acid sequences. Also in this paper a new scale of stratified B-factors, derived from the Protein Data Bank, is presented.

Keywords
Cold adaptation; Halophilic enzymes; Sequence analysis; Endonuclease I; Amino acid property
First Page Preview
Sequence comparison and environmental adaptation of a bacterial endonuclease
Publisher
Database: Elsevier - ScienceDirect
Journal: Computational Biology and Chemistry - Volume 31, Issue 3, June 2007, Pages 163–172
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering