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Tomb Raider Underworld Bigfile 000 Download Link:..We have been studying the role of the lysine-specific histone demethylase LSD1 in nucleosome assembly and the recruitment of linker histones to promoters. These studies have shown that LSD1 can destabilize nucleosomes and chromatin by demethylating H3K4me2/3, removing H3K4me3 from the DNA, and repositioning H2A/H2B dimers to more open DNA regions. We have also made a large library of mutants of LSD1 by scanning mutagenesis of lysine residues and then tested them for their ability to promote nucleosome assembly and chromatin architecture. We have found that each of the catalytic residues in the FAD binding pocket is essential for the function of LSD1 in both chromatin assembly and de-novo nucleosome assembly, and that individual catalytic residues can play additive roles in these processes. Furthermore, demethylase activity is not required for enzymatic function of LSD1, and a FAD analog, which induces local conformational change in LSD1, is sufficient to enhance demethylase activity in vitro and in vivo, and to promote chromatin decondensation. We have also found that both PHD and Tudor domains, which are known to bind methylated lysine residues, can bind H3K4me2/3 and H3K9me3. We have been finding that assembly of the linker histones on DNA, in the presence of LSD1, is cooperative and in some cases relies on the binding of multiple linker histones to DNA. Moreover, that combined binding of the linker histones and LSD1 to DNA can depend on the presence of H3K4me2/3, H3K9me3, or a combination of these marks. We have found that LSD1 can bind to DNA without the presence of the linker histones, but only once the DNA has been exposed to the linker histones. We have also found that LSD1 binds more tightly to DNA in a nucleosomal array than does a nucleosome remodeling factor, suggesting a possible role for LSD1 in the recruitment of linker histones to their target sites. In addition, we have found that deletion of the LSD1 binding domain in the chromodomain of the linker histone H1 results in the loss of the ability of H1 to promote the assembly of

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