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First published online October 14, 2004
doi: 10.1242/10.1242/dev.01439

Development 131, 5215-5220 (2004)
Published by The Company of Biologists 2004
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New insights into plant development in New England

Liam Dolan1 and Jane A. Langdale2,*

1 John Innes Centre, Colney, Norwich NR4 7UH, UK
2 Department of Plant Sciences, University of Oxford, South Parks Rd, Oxford OX1 3RB, UK



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  		Fig. 1. Summary of genetic interactions occurring at the boundary between valve-valve margin and replum in the developing fruit. The colour of each protein indicates the region in which it is expressed. ALC, ALCATRAZ; FUL, FRUITFULL; IND, INDEHISCENT; RPL, REPLUMLESS; SHP, SHATTERPROOF.

 


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  		Fig. 2. Cell distribution on the abaxial surface (underside) of an Arabidopsis cotyledon (seed leaf). Stomata are pores that are surrounded by a pair of kidney-shaped guard cells – the pores appear as black voids in this image. The epidermal surface between stomata is occupied by pavement cells with undulating edges. Scale bar: 50 {lambda}m.

 


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  		Fig. 3. A model of the functional relationships among COP9 signalosome subunit 5B (CSN), CONSTITUTIVELY PHOTOMORPHOGENIC1 (COP1) and DDB1 DET1 COP10 complex (CDD) complexes, in ubiquitin (Ub)-mediated proteolysis. In darkness, CSN, COP1 and CDD complexes work together to promote the ubiquitination of photomorphogenesis-promoting transcription factors such as HY5. The CSN directly interacts with and stabilizes the CDD complex. The CDD complex has the ability to enhance E2 activity. COP10 interacts with the Ring finger domain of COP1. HY5 interacts with the WD40 repeat domain of COP1 and is ubiquitinated by the ubiquitin E3 ligase activity of COP1. Polyubiquitinated HY5 is presumably recognized and degraded by the 26S proteasome. The CSN might regulate the function of the 26S proteasome, CDD complex and COP1 E3 ligase activity. DDB1, DAMAGED DNA BINDING PROTEIN 1B; DET1, DEETIOLATED 1.

 




© The Company of Biologists Ltd 2004