However, such a model would not easily explain why far more abundant hydrophobic binding proteins do not outcompete SRP, why SRP cannot bind those same sequences post-translationally, and how SRP can rapidly find these transient and rare species to prevent aggregation.
Sequence-specific nucleic acid binding proteins do not recognize one sequence out of all possibilities; rather, they bind to many sequences with a range of affinities.
What is surprising is that osmotin and adiponectin, the receptor binding proteins, do not share sequence similarity even if both have a similar internal beta-barrel domain [5].
Since it has been already reported that methyl-CpG binding proteins do not interact with 5-hmC-containing DNA substrates, these two modifications are likely to play distinct roles in biological systems.
We conclude that DNA methylation and the associated methyl-DNA binding proteins do not appear to play a critical role in determining histone modification patterns on the mammalian inactive X chromosome, either globally or at the level of the promoter.
Although zinc-ion binding proteins do not behave similarly at the level of expression (i.e., they are not all up-regulated or down-regulated: some of them are upregulated, while some are downregulated), it is evident that more attention should be paid to them.
The resulting purified ML protein was able to bind to amylose resin (Figure 5B) and could subsequently be eluted with maltose-containing buffer (Figure 5C), which showed that the covalent attachment of 5-carboxyfluorescein to the C-terminus of the maltose binding protein did not interfere with the protein's biochemical function.
Similarly RNAi knockdown of staufen (stau ), which encodes a double-stranded RNA binding protein, did not result in any overt dendritic defects whereas dendritic branching was reduced in stau mutant larvae (data not shown).
Thus, we conclude that the duplication of known HSPs and HSP-binding proteins did not explain why chrIII was specifically duplicated.
