| Literature DB >> 23545501 |
Y Paul Chang1, Meng Xu, Ana Carolina Dantas Machado, Xian Jessica Yu, Remo Rohs, Xiaojiang S Chen.
Abstract
The DNA tumor virus Simian virus 40 (SV40) is a model system for studying eukaryotic replication. SV40 large tumor antigen (LTag) is the initiator/helicase that is essential for genome replication. LTag recognizes and assembles at the viral replication origin. We determined the structure of two multidomain LTag subunits bound to origin DNA. The structure reveals that the origin binding domains (OBDs) and Zn and AAA+ domains are involved in origin recognition and assembly. Notably, the OBDs recognize the origin in an unexpected manner. The histidine residues of the AAA+ domains insert into a narrow minor groove region with enhanced negative electrostatic potential. Computational analysis indicates that this region is intrinsically narrow, demonstrating the role of DNA shape readout in origin recognition. Our results provide important insights into the assembly of the LTag initiator/helicase at the replication origin and suggest that histidine contacts with the minor groove serve as a mechanism of DNA shape readout.Entities:
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Year: 2013 PMID： 23545501 PMCID： PMC3748285 DOI： 10.1016/j.celrep.2013.03.002
Source DB: PubMed Journal: Cell Rep Impact factor: 9.423