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The Myb oncogene product induces DNA-bending
P Saikumar1, J L Gabriel, E P Reddy
1Fels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, PA.
Oncogene
|April 1, 1994
Summary
The Myb protein, a transcription regulator, bends DNA upon binding. This DNA bending, mediated by the Myb protein
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- The Myb protein family, including viral (v-Myb) and cellular (c-Myb) oncogenes, are transcription factors that regulate gene expression.
- Myb proteins possess distinct DNA-binding and trans-regulatory domains crucial for their function.
- The DNA-binding domain features three imperfectly conserved 50-52 amino acid repeats at the N-terminus.
Purpose of the Study:
- To investigate the structural changes in DNA induced by Myb protein binding.
- To determine if Myb protein binding causes DNA bending and characterize the bending orientation.
- To analyze the role of different Myb protein domains in DNA bending.
Main Methods:
- Circular permutation assays to detect DNA bending induced by Myb protein.
- Phasing analysis to confirm DNA bending and determine bend orientation.
- Molecular modeling to analyze the Myb-DNA complex structure.
Main Results:
- Myb protein binding induces a conformational change, specifically bending the DNA at the binding site.
- Both DNA-binding domains and full-length Myb proteins induce DNA bending with a consistent orientation.
- The transactivating region of Myb protein influences the magnitude of the DNA bend angle.
Conclusions:
- Myb proteins, like other transcriptional regulators, bend DNA upon binding.
- This DNA bending facilitates the interaction of regulatory elements, contributing to transcriptional regulation.
- The DNA-binding domain is sufficient to induce bending, while the transactivating domain modulates the bend angle.