Fz. Liu et al., BETA-FILAGENIN, A NEWLY IDENTIFIED PROTEIN COASSEMBLING WITH MYOSIN AND PARAMYOSIN IN CAENORHABDITIS-ELEGANS, The Journal of cell biology, 140(2), 1998, pp. 347-353
Muscle thick filaments are stable assemblies of myosin and associated
proteins whose dimensions are precisely regulated. The mechanisms unde
rlying 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 f
ilament backbone in the nematode Caenorhabditis elegans. We obtained p
artial peptide sequences from one of the core proteins, beta-filagenin
, and then identified a gene that encodes a novel protein of 201-amino
acid residues from databases using these sequences. beta-Filagenin ha
s a calculated isoelectric point at 10.61 and a high percentage of aro
matic amino acids. Secondary structure algorithms predict that it cons
ists of four beta-strands but no alpha-helices, Western blotting using
an affinity-purified antibody showed that beta-filagenin was associat
ed with the cores. beta-Filagenin was localized by immunofluorescence
microscopy to the A bands of body-wall muscles, but not the pharynx. b
eta-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, beta-filagenin assembled w
ith myosin to form abnormal tubular filaments with a periodicity ident
ical to wild type. These results verify that beta-filagenin is a core
protein that coassembles with either myosin or paramyosin in C. elegan
s to form tubular filaments.