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SUMO (small‐ubiquitin‐like modifier) in Tetrahymena thermophila
Author(s) -
Matejka Stephanie Lynn,
Knobbe Amy,
Johnson Jacob,
Weeks Donald P.,
Bailey Cheryl
Publication year - 2010
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.24.1_supplement.843.2
Subject(s) - tetrahymena , flagellum , cilium , chlamydomonas reinhardtii , biology , proteome , microbiology and biotechnology , organelle , basal body , protein targeting , gene , genetics , membrane protein , mutant , membrane
Cilia and flagella organelles serve important roles in a wide variety of organisms. Outside of Chlamydomonas reinhardtii flagella, there is limited understanding of ciliary protein composition and regulation. We investigate SUMO ( S mall u biquitin‐like mo difier) protein modification in the cilia of the single celled protozoan, Tetrahymena thermophila . SUMO is a member of the family of ubiquitin‐like polypeptides that become covalently attached to intracellular target proteins in eukaryotic organisms. Bioinformatics have shown a single SUMO gene in the genome of this organism. Real‐time RT‐PCR of T. thermophila samples has confirmed the expression of this SUMO gene. Additionally, western‐blot analysis of ciliary extracts has shown three SUMOylated proteins of approximately 35kD, 50kD and 135kD. The 135kD SUMOylated protein is preferentially found in ciliary extracts and not in cell body extracts. This implies there are specific SUMOylated target proteins in the cilia. Fractionations of ciliary extracts have been submitted for mass‐spectrometry analysis and reveal proteins not previously found in the T. thermophila ciliary proteome. Supported by NSF and the Nebraska Research Council.