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Flask for undeflected droplets Figure 2 The ow cytometry device used to separate chromosomes at high speed. A buffer with chromosomes enters the device. Lasers cause uorescence that is analyzed with the aid of the photomultiplier tubes. Droplet formation is induced by vibration, and, based on a ow rate of 50 m/sec, appropriate drops are charged. Charged drops are then separated by charged de ection plates and collected. Uncharged droplets pass through. (Reprinted with permission from J. W. Gray, et al.,
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somes, condensing interphase chromosomes, and performing numerous other activities of chromosomes. Dosage compensation has recently been associated with a change in nucleosome structure.The inactivated X chromosome appears to have a different type of histone present. Histone H2A is replaced by a variant called mH2A. The details of this mechanism are under study.
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Nucleosomes apparently play a major role in controlling gene expression; DNA with nucleosomes has a much lower transcription rate than DNA without nucleosomes. It makes sense that the positions of nucleosomes can provide or prevent access to promoters. There are regions of the DNA, known as nucleasehypersensitive sites, that appear to be nucleosome
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Tamarin: Principles of Genetics, Seventh Edition
III. Molecular Genetics
15. The Eukaryotic Chromosome
The McGraw Hill Companies, 2001
Fifteen
The Eukaryotic Chromosome
free. These sites, usually mutiples of a nucleosomal region of about two hundred base pairs, are particularly sensitive to digestion by different nucleases. When these regions are isolated, they usually have sequences that control functions in replication, transcription, or other activities of DNA. For example, numerous promoter regions in Drosophila, mouse, and human DNA are in nuclease-hypersensitive sites. Hence, some speci c DNA sequences are kept free of nucleosomes, and these sequences appear to be recognized by various enzymes such as RNA polymerase. In many other cases, however, nucleosomes do appear to cover promoters and repress transcription. For transcription to occur in these cases, some form of chromatin remodeling must take place. Two general classes of proteins are involved in chromatin remodeling. First are proteins that acetylate the N-terminal tails of the histones, a process that may cause the nucleosomes to bind the DNA less tightly and thus make it available for attachment of transcription factors. These enzymes are called histone acetyl transferases (HATs). Deacetylating enzymes have the reverse effect: They act to repress transcription. Second, a class of ATPdependent proteins such as the SWI/SNF complex in yeast also affect chromatin remodeling. (Some workers called the proteins SWI because they were involved in mating type switching, and others called them SNF for sucrose nonfermenting.) The SWI/SNF complex is a group of eleven proteins involved in transcription activation in many genes, presumably allowing transcription
The eukaryotic chromosome is associated with histone proteins to form nucleosomes. The protein core is wrapped with 1.7 loops of DNA and connected with a length of DNA called a linker.
Figure 15.6 Nucleosome structure. (a) Schematic comparison of the eight histones comprising the nucleosome in salt solution. A dimer consists of one H2A and one H2B histone molecule; a tetramer consists of two H3 and two H4 histones. (b) DNA ts in surface grooves on the more compacted structure found in physiological conditions. (c) The diagram shows the presumed position of the H1 histone, encompassing 166 base pairs of DNA.
Tamarin: Principles of Genetics, Seventh Edition
III. Molecular Genetics
15. The Eukaryotic Chromosome
The McGraw Hill Companies, 2001
The Eukaryotic Chromosome
Table 15.2 Composition of Histones
Fraction H1 H2A H2B H3 H4 Class Very lysine rich Lysine, arginine rich Moderately lysine rich Arginine rich Arginine, glycine rich Number of Amino Acids 213 129 125 135 102 Percentage of Basic Amino Acids 30 23 24 24 27
Nucleosome core particle at 2.8 resolution. Shown are 146 base pairs of DNA (brown and turquoise) and the eight histone protein chains ( purple: H3; green: H4; yellow: H2A; and red: H2B). Note the protein tails (N-terminal ends) of the histone polypeptides extending out of the nucleosome. On the left is the view down the DNA helix, and on the right is the perpendicular view. (From Karolin Luger, et al., Crystal structure of the
nucleosome core particle at 2.8A resolution in Nature, 389:251 260, September 18, 1997, g. 1a p. 252. Reprinted by permission of Macmillan, Ltd.)
factors to access promoters by remodeling chromatin. These proteins are able to reposition a nucleosome on DNA by sliding the nucleosome down the DNA. We thus conclude that although nucleosomes serve as a general, rst-order packing mechanism in eukaryotic DNA, they can be positioned precisely and can attenuate transcription. It is interesting to note that once transcription begins, RNA polymerase apparently moves along nucleosomed DNA by translocation of the histones by 75 to 80 base pairs without disrupting the nucleosome itself. This seems to be accomplished by the RNA polymerase moving the DNA and then re-forming the nucleosome in its wake ( g. 15.8).
RNA polymerase steps around a nucleosome without disrupting it. (1) The RNA polymerase begins at a promoter (P) and heads for the nucleosomed DNA ( lled in), whose border is noted with a line and the letter B. As the polymerase encounters the nucleosome, it begins to unwrap the DNA from the histones (2). The displaced DNA then reencounters the histones (3), about seventy- ve to eighty base pairs upstream from the original point of nucleosome formation. The polymerase continues on its way (4 and 5), and the nucleosome re-forms in its displaced position without disrupting the histones or ever fully losing contact with the core DNA.
(From Vasily M. Studitsky, et al., A histone octamer can step around a transcribing polymerase without leaving the template, Cell, 76: 371 82, January 28, 1994. Copyright 1994 by Cell Press. Reprinted by permission.)
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