When bovine myofibrils are incubated with the 20S proteasome their structur
e is rapidly damaged with loss of material, particularly from the Z discs a
nd I bands. After 24 hr of incubation the myofibrils rupture and debris app
ears. Certain myofibrillar proteins, including nebulin, myosin, actin and t
ropomyosin, are hydrolysed during the incubation; others are solubilised (a
lpha-actinin). The 20S proteasome completely and rapidly hydrolyses purifie
d myofibrillar proteins in an energy-independent manner. This shows that th
e 20S proteasome probably plays a role in the postmortem transformation of
muscle and more generally in the hydrolysis of cellular proteins. (C) 1998
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