Key result
Biochemical analysis of chicken brain myosin-Va identified three additional low molecular weight proteins (23-, 17-, and 10-kDa) associated with it, including myosin-II essential light chains and DLC8.
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Identifies the specific light chain components of chicken brain myosin-Va, including essential light chains and a dynein light chain.
Class V myosins are a ubiquitously expressed family of actin-based molecular motors. Biochemical studies on myosin-Va from chick brain indicate that this myosin is a two-headed motor with multiple calmodulin light chains associated with the regulatory or neck domain of each heavy chain, a feature consistent with the regulatory effects of Ca(2+) on this myosin. In this study, the identity of three additional low molecular weight proteins of 23-,17-, and 10 kDa associated with myosin-Va is established. The 23- and 17-kDa subunits are both members of the myosin-II essential light chain gene family, encoded by the chicken L23 and L17 light chain genes, respectively. The 10-kDa subunit is a protein originally identified as a light chain (DLC8) of flagellar and axonemal dynein. The 10-kDa subunit is associated with the tail domain of myosin-Va.
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Espíndola et al. (2000) studied this question. Biochemical analysis of chicken brain myosin-Va identified three additional low molecular weight proteins (23-, 17-, and 10-kDa) associated with it, including myosin-II essential light chains and DLC8.
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