Words similar to bipartite
Example sentences for: bipartite
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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 ] .
In some cases, including P. falciparum and HeLa cells, nuclear staining appeared more intense than cytoplasmic staining [ 2 9 ] . Based on studies with heterologously expressed human PP5-GFP fusion proteins, it has been proposed that nuclear localization requires a stretch of sequence in the C terminus [ 31 ] . However, other sequences or signals are also likely to contribute to nuclear localization of PP5 and its homologs, since rat and mouse PP5, which are identical to human PP5 in this region do not appear to be nuclear in all cell types [ 32 33 ] . In addition P. falciparum PP5 is primarily nuclear [ 9 ] , although it is not well conserved in the relevant C-terminal region but contains a potential bipartite nuclear localization signal not found in other PP5 sequences reported thus far.
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).
This sequence is the likely nuclear localization signal (NLS) for these proteins [ 15 ] , similar to the bipartite NLS found in nucleoplasmin [ 36 ] . The one exception is the Langerhans cell protein-1 (LCP1)/KIAA0737 pair, which lacks the second basic residue of the motif.
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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