Work

Author response: Stepwise nucleosome translocation by RSC remodeling complexes

Year: 2015
Type: peer-review
Abstract: Cells package their genetic information in a "complex” of proteins and DNA called chromatin. This complex is made of units called nucleosomes, each of which consist of a short stretch of DNA wrapped around proteins known as histones. These nucleosomes restrict access to the DNA wrapped around the histone proteins, and thus serve to regulate whether genes are activated and a variety of other cellular processes. Certain enzymes regulate the structure of chromatin by altering the position and structure of nucleosomes. However, it is not clear exactly how these “chromatin remodeling” enzymes alter the contacts between the DNA and histone proteins to move DNA around the nucleosome. RSC is a chromatin-remodeling enzyme that typically helps to activate genes. Harada et al. used a technique called single molecule fluorescence resonance energy transfer (or single molecule FRET for short) to observe the movement of DNA around the histone proteins. The technique involves placing a green fluorescent dye on the histone proteins and a red fluorescent dye on the DNA. If the red dye is close to the green dye, some of the energy can be transferred from the green dye to the red dye when the green dye is excited by a laser. By looking at the ratio of green and red light emitted, it is possible to tell how far apart they are, and how this changes over time. The experiments show that the RSC enzyme moves the DNA into and out of the nucleosome in small steps. These steps match the expected step size of DNA movements by a section of the enzyme called the ATPase domain. This suggests that the ATPase domain drives the motion of DNA across the entire nucleosome. A future challenge is to better understand how chromatin remodeling enzymes cooperate with other molecules in cells to remodel nucleosomes and chromatin.
Language: English
Open Access status: gold
OpenAlex ID: W2985522835
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