Words similar to bipartite
Example sentences for: bipartite
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In a typical bipartite NLS, the distance between the two clusters of positively charged amino acids is usually around 10 amino acids.
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 ] .
Both clusters of positively charged amino acids are required and can function as a classic bipartite NLS when placed within the right distance (Fig 7).
There are two proximal breakpoints (BP1 and BP2) that define two classes of PWS/AS deletion [ 14 ] . The common distal breakpoint is termed BP3 and has a bipartite structure [ 15 16 ] . The BP2 and BP3 duplicons span several hundred kb and contain at least seven expressed sequences.
The TOX protein is 526 amino acids with an acidic N-terminal domain, a bipartite nuclear localization signal sequence and a single centrally located HMG-box motif [ 15 ] . Forced expression of TOX in the thymus of transgenic mice leads to changes in the differentiation program of developing T cells.
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