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Subfunctionalization of the calcineurin gene family in paramecium tetraurelia
Author(s) -
Welker Jordan,
Herring Kelsie,
Van Houten Jason,
Barrington William,
Fraga Dean
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.954.4
Subject(s) - biology , paramecium , subfunctionalization , gene isoform , genetics , gene , calcineurin , gene duplication , gene silencing , microbiology and biotechnology , phenotype , gene family , rna interference , genome , rna , transplantation , medicine , surgery
Calcineurin is a serine/threonine protein phosphatase known to play a role in the motor function of cilia. A typical eukaryotic organism has between two and four copies of the gene for calcineurin, however Paramecium tetraurelia has 14 copies of this gene grouped into 7 isoforms or ohnologs. This multiplicity of the gene for calcineurin is suspected to be the result of whole genome duplication events during the course of evolution of Paramecium . We hypothesized that each isoform plays a different role in Paramecium rather than simply being redundant copies, as previously proposed. To test this hypothesis we utilized RNAi to systematically silence the 7 isoforms of the calcineurin catalytic subunit. The silenced cells were tested for abnormalities in various cilia mediated swimming behavior. We found that CaNA‐2, CaNA‐4, CaNA‐5, and CaNA‐6 decreased time spent swimming backwards. Previous work has shown that silencing of CaNA‐3 and CANA‐7 causes Paramecium to swim backwards for extended amounts of time, and that silencing of CaNA‐1 shows no phenotype in wild type. Forward swimming speed was also measured and found to show variations from wild type. We present our hypotheses that these duplicated genes have been maintained due to subfunctionalization processes and are not being retained strictly for redundancy.