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Vol. 10, Issue 5, 1297-1308, May 1999
Institute of Cell Biology, Swiss Federal Institute of Technology,
ETH Hönggerberg, CH-8093 Zürich
Myomesin is a 185-kDa protein located in the M-band of
striated muscle where it interacts with myosin and titin, possibly connecting thick filaments with the third filament system. By using
expression of epitope-tagged myomesin fragments in cultured cardiomyocytes and biochemical binding assays, we could demonstrate that the M-band targeting activity and the myosin-binding site are
located in different domains of the molecule. An N-terminal immunoglobulin-like domain is sufficient for targeting to the M-band,
but solid-phase overlay assays between individual N-terminal domains
and the thick filament protein myosin revealed that the unique head
domain contains the myosin-binding site. When expressed in
cardiomyocytes, the head domains of rat and chicken myomesin showed
species-specific differences in their incorporation pattern. The head
domain of rat myomesin localized to a central area within the A-band,
whereas the head domain of chicken myomesin was diffusely distributed
in the cytoplasm. We therefore conclude that the head domain of
myomesin binds to myosin but that this affinity is not sufficient for
the restriction of the domain to the M-band in vivo. Instead, the
neighboring immunoglobulin-like domain is essential for the precise
incorporation of myomesin into the M-band, possibly because of
interaction with a yet unknown protein of the sarcomere.
Online version of this article contains video material
for Figure 4. Online version available at www.molbiolcell.org.
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