Measurement of the contributions of 1D and 3D pathways to the translocation of a protein along DNA

被引:196
作者
Gowers, DM [1 ]
Wilson, GG [1 ]
Halford, SE [1 ]
机构
[1] Univ Bristol, Sch Med Sci, Dept Biochem, Bristol BS8 1TD, Avon, England
基金
英国惠康基金;
关键词
DNA-protein interaction; recognition sequence; restriction enzyme;
D O I
10.1073/pnas.0505378102
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Proteins that act at specific DNA sequences bind DNA randomly and then translocate to the target site. The translocation is often ascribed to the protein sliding along the DNA while maintaining continuous contact with it. Proteins also can move on DNA by multiple cycles of dissociation/reassociation within the same chain. To distinguish these pathways, a strategy was developed to analyze protein motion between DNA sites. The strategy reveals whether the protein maintains contact with the DNA as it transfers from one site to another by sliding or whether it loses contact by a dissociation/reassociation step. In reactions at low salt, the test protein stayed on the DNA as it traveled between sites, but only when the sites were < 50 by apart. Transfers of > 30 by at in vivo salt, and over distances of > 50 by at any salt, always included at least one dissociation step. Hence, for this enzyme, 1D sliding operates only over short distances at low salt, and 3D dissociation/reassociation is its main mode of translocation.
引用
收藏
页码:15883 / 15888
页数:6
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