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.
Viruses infecting marine picoplancton encode functional potassium ion channels / F. Siotto, C. Martin, O. Rauh, J.L. Van Etten, I. Schroeder, A. Moroni, G. Thiel. - In: VIROLOGY. - ISSN 0042-6822. - 466-467(2014), pp. 103-111. [10.1016/j.virol.2014.05.002]
Viruses infecting marine picoplancton encode functional potassium ion channels
I. Schroeder;A. Moroni;
2014
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.File | Dimensione | Formato | |
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