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Example sentences for: wd-
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In contrast, the AtCOP1 NLS has been identified as a classic bipartite nuclear localization signal, consisting of 21 amino acids in the intermediate region of coiled-coil domain and the WD-40 domain [ [ 17 ] ; Fig 8].
AtCOP1 contains three conserved structural domains: a RING finger at the amino terminus, a coiled-coil domain in the middle, and a carboxyl-terminal WD40 repeat domain [ 9 10 ] . Each of the three conserved domains has been shown to mediate protein-protein interactions [ 11 12 13 ] . The subcellular localization of AtCOP1 is regulated by light in a tissue specific manner [ 14 15 ] . The hypocotyl cell nuclei contain high levels of COP1 in the dark and reduced levels in the light, suggesting that the nucleocytoplasmic partitioning of AtCOP1 is adjusted by a light-responsive mechanism [ 14 16 ] . The activity of AtCOP1 is at least in part regulated by its subcellular localization, as the degradation of HY5 is dependent upon the nuclear accumulation of AtCOP1 in the dark [ 4 ] . AtCOP1 was demonstrated to carry a single, bipartite nuclear localization signal located between the coiled-coil domain and the WD-40 domain (amino acid 294-314) and a cytoplasmic localization signal, which was mapped to a region partially overlapping with the RING finger and the coiled-coil domain (amino acid 67-117) [ 17 ] . Strikingly, AtCOP1 protein forms characteristic nuclear speckles when transiently expressed in onion epidermal cells or stably expressed in transgenic Arabidopsis [ 6 18 ] . The functional role of these speckles is currently unknown; however, a subnuclear localization signal consisting of 58 residues (amino acid 120-177) is required for their formation [ 19 ] .
Because of its role in mediating the degradation of HY5, HYH, and possibly other transcription factors in Arabidopsis [ 4 5 ] and the presence of a RING finger domain and a WD-40 domain, AtCOP1 has been proposed to function as a RING-finger type ubiquitination E3 ligase, by recruiting E2 through its RING-finger domain and binding to the substrates through the WD-40 repeats [ 4 43 ] . This hypothesis is also supported by the findings about other negative regulators of plant photomorphogenesis.
However, the protein sequences of the three major protein-protein interactive domains (RING, Coiled coil, WD-40 repeats) are highly conserved, possibly due to conserved biochemical activity of COP1 in all organisms.
It might be rooted in some sort of primal hunter-gatherer-type urge, the kind that afflicts most men when they enter a Price Club ("Of course we need 24 gallons of WD-40, honey.
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