期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 17, 期 8, 页码 932-U37出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1858
关键词
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资金
- Howard Hughes Medical Institute
- US National Science Foundation
- US National Institutes of Health (NIH) [GM082848]
- NIH [GM53085, T32GM00879807]
- State University of New York
- Columbia University
- Nanoscale Science and Engineering Initiative of the National Science Foundation under US National Science Foundation [CHE-0641523]
- New York State Office of Science, Technology, and Academic Research
DNA-binding proteins survey genomes for targets using facilitated diffusion, which typically includes a one-dimensional (1D) scanning component for sampling local regions. Eukaryotic proteins must accomplish this task while navigating through chromatin. Yet it is unknown whether nucleosomes disrupt 1D scanning or eukaryotic DNA-binding factors can circumnavigate nucleosomes without falling off DNA. Here we use single-molecule microscopy in conjunction with nanofabricated curtains of DNA to show that the postreplicative mismatch repair protein complex Mlh1-Pms1 diffuses in 1D along DNA via a hopping/stepping mechanism and readily bypasses nucleosomes. This is the first experimental demonstration that a passively diffusing protein can traverse stationary obstacles. In contrast, Msh2-Msh6, a mismatch repair protein complex that slides while maintaining continuous contact with DNA, experiences a boundary upon encountering nucleosomes. These differences reveal important mechanistic constraints affecting intranuclear trafficking of DNA-binding proteins.
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