|
|
|
||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | |||||
| ||||||||||||||||||||
Files in this Data Supplement:
Fig. S1. Time-lapse analysis of the Rlc1-GFP ring contraction in wild-type or chs2Δ cells.
Movie 1. Time-lapse microscopy of myo3Δ carrying an integrated copy of the Rlc1-GFP fusion protein. Images were captured every 4 minutes over a period of 84 minutes. Then, they were mounted as a movie using Image Ready software with a retard of 0.2 seconds between each image.
Movie 2. Time-lapse microscopy of myo3Δ chs2Δ carrying an integrated copy of the Rlc1-GFP fusion protein. Images were captured every 4 minutes over a period of 112 minutes. In the myo3Δchs2Δ strain, ring contraction and final disassembly takes longer than in the myo3Δ strain (Movie 1). Appearance of secondary rings very close to the original ones can be observed in several cells in the double-mutant strain.
Movie 3. Time-lapse confocal microscopy of myo3Δ chs2Δ cells carrying an integrated copy of the Rlc1-GFP fusion protein. Z-series consisting of 25 sections with a step-size of 2 μm were taken every 5. Then, a three-dimensional reconstruction was made. These 3-D images were mounted as a movie using Image Ready software, with a retard of 0.5 seconds between each image. Appearance of abnormal ring structures can be appreciated (see cells marked with an asterisk).
Movie 4. Time-lapse confocal microscopy of myo3Δchs2Δcells carrying an integrated copy of Cdc15-GFP. Z-series consisting of 25 sections with a step-size of 2 μm were taken every 3 minutes. Then, a three-dimensional reconstruction was made. The 3-D images were mounted as a movie using Image Ready software, with a retard of 0.5 seconds between each image. Appearance of similar abnormal ring structures to those in Movie 3 can be appreciated (see cells marked with an asterisk).
| ||||||||||||||||||||