What controls the unusual melting profiles of small AuNPs/DNA complexes

2019 ◽  
Vol 21 (21) ◽  
pp. 11019-11032 ◽  
Author(s):  
Elia Grueso ◽  
Rosa M. Giráldez-Pérez ◽  
Pilar Perez-Tejeda ◽  
Emilio Roldán ◽  
R. Prado-Gotor

The effect of the addition of low salt concentrations on ds-DNA and ss-DNA conformational changes induced by small N-(2-mercaptopropionyl)glycine gold nanoparticles (AuNPs) is studied in detail by using different techniques. The results are correlated with the unusual melting profiles of the AuNPs/DNA complexes.

Author(s):  
Sharonda J LeBlanc ◽  
Jacob W Gauer ◽  
Pengyu Hao ◽  
Brandon C Case ◽  
Manju M Hingorani ◽  
...  

2019 ◽  
Vol 116 (3) ◽  
pp. 21a
Author(s):  
Sudipta Lahiri ◽  
Bharat Lakhani ◽  
Yan Li ◽  
Manju M. Hingorani ◽  
David L. Beveridge ◽  
...  

2009 ◽  
Vol 96 (3) ◽  
pp. 4a
Author(s):  
Stephan M. Woods ◽  
Katrice E. King ◽  
Avishek Kumar ◽  
Roberta E. Redfern ◽  
Alonzo Ross ◽  
...  

2020 ◽  
Vol 295 (27) ◽  
pp. 9012-9020
Author(s):  
Carel Fijen ◽  
Mariam M. Mahmoud ◽  
Meike Kronenberg ◽  
Rebecca Kaup ◽  
Mattia Fontana ◽  
...  

Eukaryotic DNA polymerase β (Pol β) plays an important role in cellular DNA repair, as it fills short gaps in dsDNA that result from removal of damaged bases. Since defects in DNA repair may lead to cancer and genetic instabilities, Pol β has been extensively studied, especially its mechanisms for substrate binding and a fidelity-related conformational change referred to as “fingers closing.” Here, we applied single-molecule FRET to measure distance changes associated with DNA binding and prechemistry fingers movement of human Pol β. First, using a doubly labeled DNA construct, we show that Pol β bends the gapped DNA substrate less than indicated by previously reported crystal structures. Second, using acceptor-labeled Pol β and donor-labeled DNA, we visualized dynamic fingers closing in single Pol β-DNA complexes upon addition of complementary nucleotides and derived rates of conformational changes. We further found that, while incorrect nucleotides are quickly rejected, they nonetheless stabilize the polymerase-DNA complex, suggesting that Pol β, when bound to a lesion, has a strong commitment to nucleotide incorporation and thus repair. In summary, the observation and quantification of fingers movement in human Pol β reported here provide new insights into the delicate mechanisms of prechemistry nucleotide selection.


2019 ◽  
Vol 116 (3) ◽  
pp. 500a ◽  
Author(s):  
Kim A. Sharp ◽  
Xiang-Jun Lu ◽  
Gino Cingolani ◽  
Stephen C. Harvey

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