E1 initiator DNA binding specificity is unmasked by selective inhibition of non-specific DNA binding

Stenlund, A. (February 2003) E1 initiator DNA binding specificity is unmasked by selective inhibition of non-specific DNA binding. Embo Journal, 22 (4). pp. 954-963. ISSN 0261-4189

Abstract

Initiator proteins are critical components of the DNA replication machinery and mark the site of initiation. This activity probably requires highly selective DNA binding; however, many initiators display modest specificity in vitro. We demonstrate that low specificity of the papillomavirus E1 initiator results from the presence of a non-specific DNA-binding activity, involved in melting, which masks the specificity intrinsic to the E1 DNA-binding domain. The viral factor E2 restores specificity through a physical interaction with E1 that suppresses non-specific binding. We propose that this arrangement, where one DNA-binding activity tethers the initiator to ori while another alters DNA structure, is a characteristic of other viral and cellular initiator proteins. This arrangement would provide an explanation for the low selectivity observed for DNA binding by initiator proteins.

Item Type: Paper
Uncontrolled Keywords: DNA binding DNA replication initiator specificity factor ORIGIN RECOGNITION COMPLEX origin recognition complex LARGE T-ANTIGEN large T-antigen BOVINE PAPILLOMAVIRUS bovine papillomavirus E2 PROTEINS TRANSCRIPTION FACTOR transcription factor STRUCTURAL CHANGES REPLICATION replication DOMAIN domain ATP HELICASE helicase
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
organism description > virus > papillomavirus
CSHL Authors:
Communities: CSHL labs > Stenlund lab
Depositing User: Brian Soldo
Date: February 2003
Date Deposited: 15 Mar 2012 14:05
Last Modified: 14 Feb 2017 20:06
PMCID: PMC145451
Related URLs:
URI: https://repository.cshl.edu/id/eprint/25181

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