Chen, G., Stenlund, A. (February 2000) Two patches of amino acids on the E2 DNA binding domain define the surface for interaction with E1. Journal of Virology, 74 (3). pp. 1506-1512. ISSN 0022-538X
Abstract
The El and Et proteins from bovine papillomavirus bind cooperatively to the viral origin of DNA replication (ori), forming a complex which is essential for initiation of DNA replication. Cooperative binding has two components, in which (i) the DNA binding domains (DBDs) of the two proteins interact with each other and (ii) the E2 transactivation domain interacts with the helicase domain of El. By generating specific point mutations in the DBD of E2, we have defined two patches of amino acids that are involved in the interaction with the El DBD. These same mutations, when introduced into the viral genome, result in severely reduced replication of the viral genome, as well as failure to transform mouse cells in tissue culture. Thus, the interaction between the El and E2 DBDs is important for the establishment of the viral genome as an episome and most likely contributes to the formation of a preinitiation complex on the viral ori.
Item Type: | Paper |
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Uncontrolled Keywords: | PAPILLOMAVIRUS TYPE-1 E1 Papillomavirus Type 1 BOVINE PAPILLOMAVIRUS Bovine Papillomavirus CRYSTAL STRUCTURE Crystal Structure TRANSCRIPTIONAL ACTIVATOR Transcriptional Activator REPLICATION PROTEIN Replication protein COMPLEX FORMATION complex formation ORIGIN BINDING origin binding INITIATOR E1 initiator REQUIRES TRANSACTIVATOR transactivator |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > DNA replication bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > DNA binding protein |
CSHL Authors: | |
Communities: | CSHL labs > Stenlund lab |
Depositing User: | Brian Soldo |
Date: | February 2000 |
Date Deposited: | 14 Mar 2012 16:43 |
Last Modified: | 14 Feb 2017 20:18 |
PMCID: | PMC111486 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/25190 |
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