|
|
|
|
|
|
|
||||
| Home Help Feedback Subscriptions Archive Search Table of Contents | ||||
|
Fig. 5. Identification of a signal domain that is necessary and sufficient for
inter- and/or intracellular movement of the protein. (A) Diagram of the
deletion mutants of CPC. The N-terminal domain is shown in red, the Myb domain
in blue. (B-D) CLSM images showing GFP fluorescence (green) and PI
fluorescence (red) in the root epidermis of 5-day-old seedlings. (B) Like
full-length CPC fused to GFP, 1-79G moved from hairless cells to root hair
cells (file of hair cells is indicated by an asterisk) and accumulated in the
nuclei of both cell types. (C) In contrast to 1-79G, 1-75G remained
distributed throughout the cytoplasm of the hairless cells. (D) A partial
defect in CPC movement in 10-83G was indicated by the occurrence of the GFP
signal only in a fraction of hair cells, with 1-79G and 10-83G accumulated in
nuclei. (E) Diagrammatic representation of a signal domain (residues 1 to 79,
as indicated by the yellow and green bar) that is necessary and sufficient for
CPC cell-to-cell movement. The domain, amino acid residues 1 to 79, contains
the N terminus and a part of the Myb domain. The regions whose deletions
conferred defects in the intercellular movement of CPC:GFP were tentatively
designated S1 and S2 (as indicated by the yellow bars). As the behavior of
1-75G shows (C), S2 also is required for the nuclear accumulation of CPC.
Scale bar: 50 µm.
|
