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Viruses infecting marine picoplancton encode functional potassium ion channels.

Siotto, Fenja and Martin, Corinna and Rauh, Oliver and Van Etten, James L. and Schroeder, Indra and Moroni, Anna and Thiel, Gerhard (2014):
Viruses infecting marine picoplancton encode functional potassium ion channels.
In: Virology, pp. 103-11, 466-467, ISSN 1096-0341,
[Article]

Abstract

Phycodnaviruses are dsDNA viruses, which infect algae. Their large genomes encode many gene products, like small K(+) channels, with homologs in prokaryotes and eukaryotes. Screening for K(+) channels revealed their abundance in viruses from fresh-water habitats. Recent sequencing of viruses from marine algae or from salt water in Antarctica revealed sequences with the predicted characteristics of K(+) channels but with some unexpected features. Two genes encode either 78 or 79 amino acid proteins, which are the smallest known K(+) channels. Also of interest is an unusual sequence in the canonical α-helixes in K(+) channels. Structural prediction algorithms indicate that the new channels have the conserved α-helix folds but the algorithms failed to identify the expected transmembrane domains flanking the K(+) channel pores. In spite of these unexpected properties electophysiological studies confirmed that the new proteins are functional K(+) channels.

Item Type: Article
Erschienen: 2014
Creators: Siotto, Fenja and Martin, Corinna and Rauh, Oliver and Van Etten, James L. and Schroeder, Indra and Moroni, Anna and Thiel, Gerhard
Title: Viruses infecting marine picoplancton encode functional potassium ion channels.
Language: English
Abstract:

Phycodnaviruses are dsDNA viruses, which infect algae. Their large genomes encode many gene products, like small K(+) channels, with homologs in prokaryotes and eukaryotes. Screening for K(+) channels revealed their abundance in viruses from fresh-water habitats. Recent sequencing of viruses from marine algae or from salt water in Antarctica revealed sequences with the predicted characteristics of K(+) channels but with some unexpected features. Two genes encode either 78 or 79 amino acid proteins, which are the smallest known K(+) channels. Also of interest is an unusual sequence in the canonical α-helixes in K(+) channels. Structural prediction algorithms indicate that the new channels have the conserved α-helix folds but the algorithms failed to identify the expected transmembrane domains flanking the K(+) channel pores. In spite of these unexpected properties electophysiological studies confirmed that the new proteins are functional K(+) channels.

Journal or Publication Title: Virology
Volume: 466-467
Divisions: 10 Department of Biology
10 Department of Biology > Plant Membrane Biophysics
Date Deposited: 11 Dec 2014 10:02
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