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Figure 6. Role of the P/rds C terminus for self-assembly and localization. Scale bars, 10 μm. A, Confocal micrographs of tadpole ocular cryosections showing BiFC (green; a, d, g), Mab 1G9 labeling of endogenous X. laevis P/rds (white; b, e, h), and Hoechst stained nuclei (blue; a–i). Deletion of the P/rds C-terminal domain from one (Va-HA-P/rdsΔC + Vb-MYC-P/rds) or both (Va-HA-P/rdsΔC + Vb-MYC- P/rdsΔC) transgenically expressed proteins did not prevent self-assembly; substantial BiFC was generated in each instance (a, d, g). In contrast, absence of the C-terminal domain tended to favor IS localization (d, arrowheads) in a dose-dependent manner. B, Confocal micrographs of tadpole ocular cryosections showing, in a–c, BiFC (green), antibody labeling of HA-tagged (red) and MYC-tagged (white) fusion proteins, and Hoechst stained nuclei (blue), or d–f, BiFC (green), HA labeling of Va-HA-P/rdsΔC (red), MabC6 labeling of Vb-MYC-P/rds (white), and Hoechst stained nuclei (blue). Labeling of individual transgenic proteins (e and f vs b and c) showed that loss of C-terminal domains produced a somewhat greater effect on BiFC complex than individual partner distributions. Image published in: Ritter LM et al. (2011) Copyright © 2011. This image is reproduced with permission of the publisher and the copyright holder. This is an Open Access article distributed under the terms of the Creative Commons Attribution License. Larger Image Printer Friendly View

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