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J. Cell Biol.,
Volume 140, Number 2, January 26, 1998 347-353
-Filagenin, a Newly Identified Protein
Coassembling with Myosin and Paramyosin
in Caenorhabditis elegans
* Department of Neurology, Muscle thick filaments are stable assemblies
of myosin and associated proteins whose dimensions
are precisely regulated. The mechanisms underlying the
stability and regulation of the assembly are not understood. As an approach to these problems, we have studied the core proteins that, together with paramyosin,
form the core structure of the thick filament backbone
in the nematode Caenorhabditis elegans. We obtained
partial peptide sequences from one of the core proteins,
Department of Microbiology and Immunology, and § Department of Biochemistry, Baylor College
of Medicine, Houston, Texas 77030
-filagenin, and then identified a gene that encodes a
novel protein of 201-amino acid residues from databases using these sequences. -Filagenin has a calculated isoelectric point at 10.61 and a high percentage of
aromatic amino acids. Secondary structure algorithms
predict that it consists of four -strands but no 
-helices. Western blotting using an affinity-purified antibody showed that -filagenin was associated with the
cores. -Filagenin was localized by immunofluorescence microscopy to the A bands of body-wall muscles,
but not the pharynx. -filagenin assembled with the
myosin homologue paramyosin into the tubular cores
of wild-type nematodes at a periodicity matching the
72-nm repeats of paramyosin, as revealed by immunoelectron microscopy. In CB1214 mutants where
paramyosin is absent, -filagenin assembled with myosin to form abnormal tubular filaments with a periodicity identical to wild type. These results verify that -filagenin is a core protein that coassembles with either myosin or paramyosin in C. elegans to form tubular
filaments.
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