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C. elegans PAT-9 is a nuclear zinc finger protein critical for the assembly of muscle attachments

Qian Liu1, Takako I Jones12, Rebecca A Bachmann1, Mitchell Meghpara1, Lauren Rogowski1, Benjamin D Williams1 and Peter L Jones12*

Author Affiliations

1 Department of Cell and Developmental Biology, University of Illinois at Urbana-Champaign, 601 S. Goodwin Ave, B107 Chemical and Life Sciences Laboratory, Urbana, IL, 61801, USA

2 Present Address: Boston Biomedical Research Institute, 64 Grove St., Watertown, MA, 02472, USA

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Cell & Bioscience 2012, 2:18  doi:10.1186/2045-3701-2-18

Published: 22 May 2012



Caenorhabditis elegans sarcomeres have been studied extensively utilizing both forward and reverse genetic techniques to provide insight into muscle development and the mechanisms behind muscle contraction. A previous genetic screen investigating early muscle development produced 13 independent mutant genes exhibiting a Pat (

aralyzed and
rrested elongation at the
wo-fold length of embryonic development) muscle phenotype. This study reports the identification and characterization of one of those genes, pat-9.


Positional cloning, reverse genetics, and plasmid rescue experiments were used to identify the predicted C. elegans gene T27B1.2 (recently named ztf-19) as the pat-9 gene. Analysis of pat-9 showed it is expressed early in development and within body wall muscle lineages, consistent with a role in muscle development and producing a Pat phenotype. However, unlike most of the other known Pat gene family members, which encode structural components of muscle attachment sites, PAT-9 is an exclusively nuclear protein. Analysis of the predicted PAT-9 amino acid sequence identified one putative nuclear localization domain and three C2H2 zinc finger domains. Both immunocytochemistry and PAT-9::GFP fusion expression confirm that PAT-9 is primarily a nuclear protein and chromatin immunoprecipitation (ChIP) experiments showed that PAT-9 is present on certain gene promoters.


We have shown that the T27B1.2 gene is pat-9. Considering the Pat-9 mutant phenotype shows severely disrupted muscle attachment sites despite PAT-9 being a nuclear zinc finger protein and not a structural component of muscle attachment sites, we propose that PAT-9 likely functions in the regulation of gene expression for some necessary structural or regulatory component(s) of the muscle attachment sites.

Sarcomere; Muscle; Zinc finger; Pat