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文献和实验Purifi cation of Multiprotein Histone Acetyltransferase Complexes
have now been identified and shown to acetylate different sites on histones as well as on non-histone proteins, including transcription regulators. In general, purified recombinant HATs expressed in bacteria or in insect cells are able to acetylate free histones
nucleosomal structure in an ATP-dependent manner. Nucleosomes are reorganized either by remodeler-directed repositioning, disassembly and/or exchange of H2A-H2B dimers for histone variants (Längst and Becker, 2004; Saha et al., 2006). Since the emergence
The Use of Small Noncoding RNAs to Silence Transcription in Human Cells
transcription specifically at the targeted gene promoter (56, 57). In human cells, this activity requires a transcriptional silencing complex that consists of Argonaute 1 (Ago-1) (54, 55), DNA methyltransferase 3A (47, 48, 56
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