A Caltech Library Service

Investigating the redox properties of human DNA primase

O'Brien, Elizabeth and Holt, Marilyn and Ehlinger, Aaron and Chazin, Walter J. and Barton, Jacqueline K. (2015) Investigating the redox properties of human DNA primase. Abstracts of Papers of the American Chemical Society, 249 . BIOL-126. ISSN 0065-7727.

Full text is not posted in this repository. Consult Related URLs below.

Use this Persistent URL to link to this item:


Human DNA primase is a heterodimeric, DNA- dependent RNA polymerase that initiates replication on single- stranded DNA. Primase has been shown previously to contain a [4Fe4S] cluster cofactor in the C terminal domain of its large subunit (p58C) . Here we measure the redox activity of the [4Fe4S] domain of primase (p58C) using electrochem. on a DNA- modified gold electrode. P58C is found to be electrochem. active on duplex DNA substrates with a single- stranded DNA overhang. Binding of p58C to the DNA substrate, moreover, is found to be dependent both on oxidn. state of the [4Fe4S] cluster and on the presence of nucleotide triphosphates (NTPs) . Through these studies, we are exploring how DNA charge transport may be exploited by DNA primase in order to execute the multistep, coordinated process of replication initiation.

Item Type:Article
Related URLs:
URLURL TypeDescription Website
Chazin, Walter J.0000-0002-2180-0790
Barton, Jacqueline K.0000-0001-9883-1600
Additional Information:© 2015 American Chemical Society.
Record Number:CaltechAUTHORS:20150424-080637938
Persistent URL:
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:56934
Deposited By: Tony Diaz
Deposited On:24 Apr 2015 16:15
Last Modified:09 Mar 2020 13:18

Repository Staff Only: item control page