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DNA-mediated signaling by the E. coli helicase, DinG

Grodick, Michael A. and Zwang, Theodore J. and Barton, Jacqueline K. (2015) DNA-mediated signaling by the E. coli helicase, DinG. Abstracts of Papers of the American Chemical Society, 249 . INOR-926. ISSN 0065-7727. https://resolver.caltech.edu/CaltechAUTHORS:20150408-100209650

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Abstract

The protein DinG is an ATP-dependent helicase from E. coli that contains a 4Fe-4S cluster. DNA-modified gold electrodes were used to measure the midpoint redox potential of the DNA-bound protein, which was found to be ∼80 mV vs. Using a 20-mer with a 15-mer single-stranded overhang as a helicase substrate on the DNA-modified electrodes, it was shown that enzymic activity via the hydrolysis of ATP increased the intensity of the electrochem. signal intensity. Whether DinG and EndoIII, a base excision repair enzyme also contg. a 4Fe- 4S cluster, use DNA-mediated charge transport (CT) chem. for inter-protein signaling was tested using several techniques. Using a single mol. at. force microscopy assay, it was shown that DinG and EndoIII preferentially redistribute to strands of DNA that contain DNA damage via long-range DNA-mediated CT. To test this signaling within cells, genetics expts. were used that strongly suggest that DinG and EndoIII utilize DNA-mediated signaling to cooperate in redistributing DinG to its target lesion.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://www.acs.org/content/acs/en/meetings/spring-2015.htmlOrganizationConference Website
ORCID:
AuthorORCID
Barton, Jacqueline K.0000-0001-9883-1600
Additional Information:© 2015 American Chemical Society.
Record Number:CaltechAUTHORS:20150408-100209650
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20150408-100209650
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:56475
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:08 Apr 2015 20:45
Last Modified:03 Oct 2019 08:14

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