Abstract:
:We investigate the mechanistic nature of the Snf2 family protein HARP, mutations of which are responsible for Schimke immuno-osseous dysplasia. Using a single-molecule magnetic tweezers assay, we construct RPA-stabilized DNA bubbles within torsionally constrained DNA to investigate the annealing action of HARP on a physiologically relevant substrate. We find that HARP closes RPA-stabilized bubbles in a slow reaction, taking on the order of tens of minutes for ∼600 bp of DNA to be re-annealed. The data indicate that DNA re-anneals through the removal of RPA, which is observed as clear steps in the bubble-closing traces. The dependence of the closing rate on both ionic strength and HARP concentration indicates that removal of RPA occurs via an association-dissociation mechanism where HARP does not remain associated with the DNA. The enzyme exhibits classical Michaelis-Menten kinetics and acts cooperatively with a Hill coefficient of 3 ± 1. Our work also allows the determination of some important features of RPA-bubble structures at low supercoiling, including the existence of multiple bubbles and that RPA molecules are mis-registered on the two strands.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Burnham DR,Nijholt B,De Vlaminck I,Quan J,Yusufzai T,Dekker Cdoi
10.1093/nar/gkx147subject
Has Abstractpub_date
2017-05-05 00:00:00pages
4687-4695issue
8eissn
0305-1048issn
1362-4962pii
3057348journal_volume
45pub_type
杂志文章abstract::We have examined the transcript levels of the Saccharomyces cerevisiae DNA repair gene RAD18 in UV irradiated cells, in the mitotic cell cycle, and during meiosis. Levels of RAD18 mRNA increased upon UV irradiation, but remained constant during the mitotic cell cycle. During meiosis, RAD18 mRNA levels rose about 4 fol...
journal_title:Nucleic acids research
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