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Many types of myosin have been found and characterized to date, and already nearly 20 classes have been identified. However, these myosin motors can be classified more simply into two groups according to their head-structure, i.e. double- or single-headed myosins. Why do some myosin motors possess a double-headed structure? One obvious possible reason would be that the two heads improve the motor's processivity and sliding performance. Previously, to investigate the possibility that the double-headed myosins simultaneously interact with parallel arrayed two actin filaments in the presence of Mg-ATP, we developed an in vitro assay system using actin bundles formed by inert polymers. Using that system, we show here that skeletal muscle heavy meromyosin (HMM), a double-headed myosin derivative, but not subfragment-1 (S-1), a single-headed one, was able to contract or elongate actin bundles in a concentration-dependent manner. Similar elongation or contraction of actin bundles can also be induced by other double-headed myosin species isolated in the native state from Dictyostelium, from green algae Chara or from chicken brain. The results of this study confirm that double-headed myosin motors can induce sliding movements among neighboring actin filaments. The double-headed structure of myosins may also be important for generating tension or elongation in actin bundles or gels, and for organizing polarity-sorted actin networks, not just for improving their motor processivity or activity.