By B. Thomas (auth.), Brian Thomas, Christopher B. Johnson (eds.)
This quantity offers a finished photo of contemporary advancements in our knowing of the plant photoreceptor phytochrome and the way it regulates plant improvement. The publication contains chapters written via the best specialists within the box describing their hottest paintings and concepts. Emphasis is on biochemistry and molecular biology yet sign transduction mechanisms and reading info by way of the reaction of the entire plant can be lined.
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Additional resources for Phytochrome Properties and Biological Action
Sample text
The relative positions of these start sites are compared with those of pea in Figure 10. Whether light changes the relative abundance of the transcripts detected by S1 nuclease analysis remains to be determined. , 1989a,b), onlya single transcription start site has been detected. , 1987a; Sharrock and Quail, 1989). The negative autoregulation that phytochrome exerts over the expression of its own phyA genes in monocots provides an excellent model system for investigating the molecular basis of phytochrome-controlled gene expression (Colbert, 1988).
In this case, only lesions with global effects on all members of the phy family, such as disrupted chromophore synthesis, would be expected to result in phytochrome-deficient phenotypes. One approach to overcoming this problem is to overexpress a heterologous phytochrome polypeptide in transgenic plants. In this way, it is hoped either that overexpression of the wild-type sequence itself will produce a phenotype, or that overexpression of mutagenized sequences will interfere with endogenous phytochrome function to produce a dominant-negative phenotype (Herskowitz, 1987).
2,6). In addition, the cluster of negatively-charged D and E residues is less extensive than for phyA, with the result that the local net negative charge for phyB and phyC is -3 versus -5 to -7 for the phyA sequences (Fig. 7). , (1988) have shown that E-404 here (E-354 their numbering) is preferentially cleaved by endoproteinase Glu-C in the Pfr form, suggesting that this segment of the polypeptide moves closer to the surface of the molecule upon photoconversion to the active form. It has been proposed that this movement might account for the observation that Pfr is more negatively charged than Pr.