Protein methylation in full length Chlamydomonas flagella
- 26 May 2009
- journal article
- research article
- Published by Wiley in Cell Motility
- Vol. 66 (8), 650-660
- https://doi.org/10.1002/cm.20387
Abstract
Post‐translational protein modification occurs extensively in eukaryotic flagella. Here we examine protein methylation, a protein modification that has only recently been reported to occur in flagella [Schneider MJ, Ulland M, Sloboda RD. 2008 . Mol Biol Cell 19(10):4319–4327.]. The cobalamin (vitamin B12) independent form of the enzyme methionine synthase (MetE), which catalyzes the final step in methionine production, is localized to flagella. Here we demonstrate, using immunogold scanning electron microscopy, that MetE is bound to the outer doublets of the flagellum. Methionine can be converted to S‐adenosyl methionine, which then serves as the methyl donor for protein methylation reactions. Using antibodies that recognize symmetrically or asymmetrically methylated arginine residues, we identify three highly methylated proteins in intact flagella: two symmetrically methylated proteins of about 30 and 40 kDa, and one asymmetrically methylated protein of about 75 kDa. Several other relatively less methylated proteins could also be detected. Fractionation and immunoblot analysis shows that these proteins are components of the flagellar axoneme. Immunogold thin section electron microscopy indicates that the symmetrically methylated proteins are located in the central region of the axoneme, perhaps as components of the central pair complex and the radial spokes, while the asymmetrically methylated proteins are associated with the outer doublets. Cell Motil. Cytoskeleton 2009.This publication has 41 references indexed in Scilit:
- Chapter Two Intraflagellar Transport (IFT)Current Topics in Developmental Biology, 2008
- Making sense of cilia and flagellaThe Journal of cell biology, 2007
- HEF1-Dependent Aurora A Activation Induces Disassembly of the Primary CiliumCell, 2007
- Proteomic analysis of a eukaryotic ciliumThe Journal of cell biology, 2005
- Chlamydomonas Kinesin-II–dependent Intraflagellar Transport (IFT): IFT Particles Contain Proteins Required for Ciliary Assembly in Caenorhabditis elegans Sensory NeuronsThe Journal of cell biology, 1998
- The Mammalian Immediate-early TIS21 Protein and the Leukemia-associated BTG1 Protein Interact with a Protein-arginine -MethyltransferasePublished by Elsevier BV ,1996
- The Chlamydomonas kinesin-like protein FLA10 is involved in motility associated with the flagellar membrane.The Journal of cell biology, 1995
- The transmembrane signaling pathway involved in directed movements of Chlamydomonas flagellar membrane glycoproteins involves the dephosphorylation of a 60-kD phosphoprotein that binds to the major flagellar membrane glycoprotein.The Journal of cell biology, 1994
- A motility in the eukaryotic flagellum unrelated to flagellar beating.Proceedings of the National Academy of Sciences of the United States of America, 1993
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970