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Vol. 17, Issue 9, 3832-3847, September 2006
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*Department of Pathology and Graduate Division of Biological and Biomedical Sciences, Emory University, Atlanta, GA 30322
Submitted February 17, 2006;
Revised May 11, 2006;
Accepted June 9, 2006
Monitoring Editor: Thomas Pollard
To gain further insight into the molecular architecture, assembly, and maintenance of the sarcomere, we have carried out a molecular analysis of the UNC-96 protein in the muscle of Caenorhabditis elegans. By polarized light microscopy of body wall muscle, unc-96 mutants display reduced myofibrillar organization and characteristic birefringent "needles." By immunofluorescent staining of known myofibril components, unc-96 mutants show major defects in the organization of M-lines and in the localization of a major thick filament component, paramyosin. In unc-96 mutants, the birefringent needles, which contain both UNC-98 and paramyosin, can be suppressed by starvation or by exposure to reduced temperature. UNC-96 is a novel 
47-kDa polypeptide that has no recognizable domains. Antibodies generated to UNC-96 localize the protein to the M-line, a region of the sarcomere in which thick filaments are cross-linked. By genetic and biochemical criteria, UNC-96 interacts with UNC-98, a previously described component of M-lines, and paramyosin. Additionally, UNC-96 copurifies with native thick filaments. A model is presented in which UNC-96 is required in adult muscle to promote thick filament assembly and/or maintenance.
The online version of this contains supplemental material at MBC Online (http://www.molbiolcell.org). This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E06-02-0144) on June 21, 2006.
Address correspondence to: Guy M. Benian (pathgb{at}emory.edu)
Abbreviations used: GFP, green fluorescent protein; GST, glutathione S-transferase; MHC A, myosin heavy chain A; MHC B, myosin heavy chain B; MBP, maltose-binding protein; SEs, standard errors.
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