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Unwinding forward and sliding back: an intermittent unwinding mode of the BLM helicase.

Wang S, Qin W, Li JH, Lu Y, Lu KY, Nong DG, Dou SX, Xu CH, Xi XG, Li M - Nucleic Acids Res. (2015)

Bottom Line: Mutational studies revealed that the RQC domain plays an important role in stabilizing the helicase/DNA interaction during both DNA unwinding and backward sliding of BLM.Especially, Lys1125 in the RQC domain, a highly conserved amino acid among RecQ helicases, may be involved in the backward sliding activity.These results may shed new light on the mechanisms for BLM in DNA repair and homologous recombination.

View Article: PubMed Central - PubMed

Affiliation: Beijing National Laboratory for Condensed Matter Physics and CAS Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.

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Mentions: Distributions of the uninterrupted unwinding length and unwinding time of the wild type enzyme were analyzed. Histograms of the unwinding length showed an obvious peak, and the distribution of unwinding time can be described by Supplementary Equation (1) which is characteristic of an exponential rise followed by an exponential decay (Figure 3A). According to the theory of single-molecule enzyme kinetics (47,48), such a distribution implies a two-rate-limiting transition scheme (Scheme 1) for the strand-switching mechanism of BLM,


Unwinding forward and sliding back: an intermittent unwinding mode of the BLM helicase.

Wang S, Qin W, Li JH, Lu Y, Lu KY, Nong DG, Dou SX, Xu CH, Xi XG, Li M - Nucleic Acids Res. (2015)

© Copyright Policy - creative-commons
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4402530&req=5

Mentions: Distributions of the uninterrupted unwinding length and unwinding time of the wild type enzyme were analyzed. Histograms of the unwinding length showed an obvious peak, and the distribution of unwinding time can be described by Supplementary Equation (1) which is characteristic of an exponential rise followed by an exponential decay (Figure 3A). According to the theory of single-molecule enzyme kinetics (47,48), such a distribution implies a two-rate-limiting transition scheme (Scheme 1) for the strand-switching mechanism of BLM,

Bottom Line: Mutational studies revealed that the RQC domain plays an important role in stabilizing the helicase/DNA interaction during both DNA unwinding and backward sliding of BLM.Especially, Lys1125 in the RQC domain, a highly conserved amino acid among RecQ helicases, may be involved in the backward sliding activity.These results may shed new light on the mechanisms for BLM in DNA repair and homologous recombination.

View Article: PubMed Central - PubMed

Affiliation: Beijing National Laboratory for Condensed Matter Physics and CAS Key Laboratory of Soft Matter Physics, Institute of Physics, Chinese Academy of Sciences, Beijing 100190, China.

Show MeSH
Related in: MedlinePlus