Related Experiment Video
Updated: Aug 4, 2026

Analyzing and Building Nucleic Acid Structures with 3DNA
Published on: April 26, 2013
The Autographa californica nucleopolyhedrovirus IE-1 protein complex has two modes of specific DNA binding
1Department of Microbiology, Oregon State University, Corvallis, Oregon 97331, USA. leisyd@bcc.orst.edu
Abstract:
Missing contact footprinting with formic acid as a modifying reagent was used to examine specific IE-1 binding contacts to double-stranded oligonucleotides that contained either a consensus hr repeat sequence or a sequence from the pe38 promoter, which is down regulated by IE-1. The hr repeat sequences contain two consensus IE-1 binding motifs (IBMs) flanking a central EcoRI site that are oriented in opposite directions with respect to each other. IE-1 was found to contact regions including both IBMs. The bases footprinted in the top strand included the left IBM (IBM-A), whereas bases in the bottom strand were footprinted in a region that included IBM-B and part of IBM-A. When substitution mutations were introduced into either IBM, bases on both strands of the remaining IBM were strongly footprinted. As with the hr IBM-mutant constructs, bases footprinted in the pe38 promoter construct included both strands of the single IBM.
Related Concept Videos
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
RNA Polymerase II Accessory Proteins
Cooperative Binding of Transcription Regulators
Single-Strand DNA Binding Proteins
RNA Polymerase II Accessory Proteins

