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First published online February 13, 2009
Journal of Experimental Biology 212, 668-672 (2009)
Published by The Company of Biologists 2009
doi: 10.1242/jeb.022681
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Characterization of amphioxus nebulin and its similarity to human nebulin

Akira Hanashima1, Kaoru Kubokawa2 and Sumiko Kimura1,*

1 Department of Biology, Graduate School of Science, Chiba University, Chiba 263-8522, Japan
2 Center for Advanced Marine Research, Ocean Research Institute, University of Tokyo, Tokyo 164-8639, Japan

* Author for correspondence (e-mail: sumiko{at}faculty.chiba-u.jp)

Accepted 2 December 2008

Identification of a large molecule in muscle is important but difficult to approach by protein chemistry. In this study we isolated nebulin cDNA from the striated muscle of amphioxus, and characterized the C-terminal regions of nebulins from other chordates. Although the sequence homology with that of human is only 26%, the C-terminal region of amphioxus nebulin has similar structural motifs of 35 amino acid nebulin repeats and an SH3 domain. Using in situ indirect immunofluorescence analysis with a specific antibody raised to the bacterially produced recombinant peptide, we identified that this nebulin fragment is located in the Z-line of the sarcomere, similar to human nebulin. Pull-down and co-sedimentation assays in vitro showed that the C-terminal region binds to actin, {alpha}-actinin and connectin (titin). These results suggest that the C-terminal region of amphioxus nebulin plays a similar role in maintaining striated muscle structure to that of human nebulin. This is the first report of the exact location of nebulin in amphioxus muscle.

Key words: {alpha}-actinin, actin, chordate, connectin, muscle


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© The Company of Biologists Ltd 2009