Words similar to protein-protein
- protein-
- protein-bound
- protein-containing
- protein-free
- protein-ligand
- protein-modifying
- protein-normalized
- protein-nucleic
- protein-peptide
- protein-primed
- protein-protein
- protein-restricted
- protein-rich
- protein-rigid
- protein-selected
- protein-sequence
- protein-sequence-based
- protein-specific
- proteinase
- proteinchip
Example sentences for: protein-protein
How can you use “protein-protein” in a sentence? Here are some example sentences to help you improve your vocabulary:
5 target sites like other Fnr-regulated class II promoters [ 16 ] . By analogy to the CAP transcription regulator [ 17 18 ] , the proposed mechanism for Fnr activation of gene expression involves its ability to promote open complex formation by RNA polymerase [ 13 16 19 ] . As suggested by the appearance of DNase I hypersensitive cleavage sites, a change in the DNA conformation occurs upon Fnr binding at the dmsA promoter [ 7 8 ] . The presence of hypersensitive DNase I cleavage sites at other FNR-regulated promoters as well as DNA bending experiments support this conclusion [ 8 20 ] . Furthermore, recent studies propose the protein-protein interaction of σ 70and Fnr at the narG and dmsA promoters [ 7 21 22 23 ] . Finally, for each of the site-directed mutations of the Fnr binding site in this study, the level of dmsA-lacZ expression was not significantly altered in an fnr deletion strain either aerobically or anaerobically, indicating that the Fnr-independent expression from the dmsA promoter was not affected by the sequence alterations (Figure 1).
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 ] .
Protein-protein interactions form scale-free networks, which show the characteristic power-law distribution of the node degrees; simply put, there is a small number of highly connected proteins (hubs), whereas the majority have a small number of partners (the most abundant class are proteins that are involved in just one interaction) [ 13 14 ] . Scale-free networks are highly tolerant to error (elimination of nodes at random) but are vulnerable to attack, i.e. elimination of the hubs [ 15 ] and, indeed, it has been found that the most highly connected proteins in yeast interaction networks tend to be essential [ 13 ] . This might explain the present findings, namely that a small number of yeast protein-protein interaction hubs evolve slowly due to strong purifying selection, whereas, for the great majority of the proteins, there is no discernible connection between the number of interactions and evolutionary rates.
Given that this domain lies in the periphery of the holoenzyme, it is likely to participate in interactions with cofactors, which is compatible with the protein-protein interaction function identified in several proteins with the β-grasp fold [ 80 81 ] .
A total of 1,879 pairs of orthologous proteins, one from S. cerevisiae and one from S. pombe , were identified (see Methods), and for 1,004 of these, there was data on protein-protein interactions of the S. cerevisiae member in the MIPS database [ 5 ] . For these 1,004 orthologous pairs, the number of protein-protein interactions detected for the S. cerevisiae protein was plotted against the calculated substitution rates between orthologs (Figure 1a).