期刊
MOLECULAR CELL
卷 35, 期 5, 页码 694-703出版社
CELL PRESS
DOI: 10.1016/j.molcel.2009.07.003
关键词
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资金
- National Institutes of Health (NIH) [GM 065367]
- National Science Foundation [0822613]
- Direct For Mathematical & Physical Scien
- Division Of Physics [0822613] Funding Source: National Science Foundation
An encounter between a DNA-translocating enzyme and a DNA-bound protein must occur frequently in the cell, but little is known about its outcome. Here we developed a multicolor single-molecule fluorescence approach to simultaneously monitor single-stranded DNA (ssDNA) translocation by a helicase, and the fate of another protein bound to the same DNA. Distance-dependent fluorescence quenching by the iron-sulfur cluster of the archaeal XPD (Rad3) helicase was used as a calibrated proximity signal. Despite the similar equilibrium DNA-binding properties, the two cognate ssDNA-binding proteins RPA1 and RPA2 differentially affected XPD translocation. RPA1 competed with XPD for ssDNA access. In contrast, RPA2 did not interfere with XPD-ssDNA binding but markedly slowed down XPD translocation. Mechanistic models of bypassing DNA-bound proteins by the Rad3 family helicases and their biological implications are discussed.
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