title: Disruption of Caenorhabditis elegans muscle structure and function caused by mutation of troponin I.
abstract: Caenorhabditis elegans strains mutant for the unc-27 gene show abnormal locomotion and muscle structure. Experiments revealed that unc-27 is one of four C. elegans troponin I genes and that three mutant alleles truncate the protein: recessive and presumed null allele e155 terminates after nine codons; semidominant su142sd eliminates the inhibitory and C-terminal regions; and semidominant su195sd abbreviates the extreme C-terminus. Assays of in vivo muscular performance at high and low loads indicated that su142sd is most deleterious, with e155 least and su195sd intermediate. Microscopy revealed in mutant muscle a prevalent disorder of dense body positioning and a less well defined sarcomeric structure, with small islands of thin filaments interspersed within the overlap region of A bands and even within the H zone. The mutants' rigid paralysis and sarcomeric disarray are consistent with unregulated contraction of the sarcomeres, in which small portions of each myofibril shorten irregularly and independently of one another, thereby distorting the disposition of filaments. The exacerbated deficits of su142sd worms are compatible with involvement in vivo of the N-terminal portion of troponin I in enhancing force production, and the severe impairment associated with su195sd highlights importance of the extreme C-terminus in the protein's inhibitory function.
authors.affiliation: Biology Department, Oberlin College, Oberlin, Ohio 44074-1097, USA.
authors.forename: A K
authors.initials: AK
authors.lastname: Burkeen
authors.forename: S L
authors.initials: SL
authors.lastname: Maday
authors.forename: K K
authors.initials: KK
authors.lastname: Rybicka
authors.forename: J A
authors.initials: JA
authors.lastname: Sulcove
authors.forename: J
authors.initials: J
authors.lastname: Ward
authors.forename: M M
authors.initials: MM
authors.lastname: Huang
authors.forename: R
authors.initials: R
authors.lastname: Barstead
authors.forename: C
authors.initials: C
authors.lastname: Franzini-Armstrong
authors.forename: T StC
authors.initials: TS
authors.lastname: Allen
mesh_terms: D000375:Aging / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D017173:Caenorhabditis elegans; D008969:Molecular Sequence Data; D009069:Movement Disorders / Q000473:pathology* / Q000503:physiopathology*; D018482:Muscle, Skeletal / Q000473:pathology* / Q000503:physiopathology*; D016297:Mutagenesis, Site-Directed; D009154:Mutation; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012518:Sarcomeres / Q000378:metabolism / Q000648:ultrastructure; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D013550:Swimming; D013647:Task Performance and Analysis; D014018:Tissue Distribution; D019210:Troponin I / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D011994:Recombinant Proteins; D019210:Troponin I