Figure 1.
Figure 1. Myo1 is a two-headed myosin and its tail contains two distinct targeting domains. (A) Myo1 heavy chain forms a dimer in yeast. Myo1-C-TAP and myo1-TD2Δ-C-TAP were purified from strains XDY7 and XDY99, respectively (left, silver staining), and observed by rotary-shadowing EM (right). (B) Recombinant myo1-Tail forms a dimer. MBP-myo1-Tail-TD2Δ was purified from E. coli (left, Coomassie blue staining) and observed by rotary-shadowing EM (right). (C) Summary of localization data on Myo1 fragments. mTD1, minimal targeting domain 1; TD2, targeting domain 2; AD, assembly domain. (D) Localization of different Myo1 fragments during the cell cycle. Yeast strains (XDY41, YJL335A, YJL221A, YJL489A, YJL222A; see Table II) were used for observation. Bar, 1 µm.

Myo1 is a two-headed myosin and its tail contains two distinct targeting domains. (A) Myo1 heavy chain forms a dimer in yeast. Myo1-C-TAP and myo1-TD2Δ-C-TAP were purified from strains XDY7 and XDY99, respectively (left, silver staining), and observed by rotary-shadowing EM (right). (B) Recombinant myo1-Tail forms a dimer. MBP-myo1-Tail-TD2Δ was purified from E. coli (left, Coomassie blue staining) and observed by rotary-shadowing EM (right). (C) Summary of localization data on Myo1 fragments. mTD1, minimal targeting domain 1; TD2, targeting domain 2; AD, assembly domain. (D) Localization of different Myo1 fragments during the cell cycle. Yeast strains (XDY41, YJL335A, YJL221A, YJL489A, YJL222A; see Table II) were used for observation. Bar, 1 µm.

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