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Sequence-specific DNA binding by the c-Myc protein.
T K Blackwell1, L Kretzner, E M Blackwood
1Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.
Science (New York, N.Y.)
|November 23, 1990
Summary
Researchers identified a specific DNA sequence, CACGTG, recognized by the c-Myc protein. This finding reveals sequence-specific DNA binding mediated by c-Myc's carboxyl-terminal region, impacting its biological functions.
Area of Science:
- Molecular Biology
- Genetics
- Protein-DNA Interactions
Background:
- The c-Myc protein is known to bind DNA, but its binding has not been sequence-specific.
- The basic helix-loop-helix (bHLH) motif in c-Myc is crucial for DNA binding and dimerization.
- Other bHLH proteins typically bind to DNA sequences containing a CA--TG consensus.
Purpose of the Study:
- To identify the specific DNA sequence recognized by the c-Myc protein.
- To investigate the sequence-specific DNA binding activity of c-Myc's carboxyl-terminal region.
Main Methods:
- Selected and Amplified Binding-Sequence (SAAB) imprinting technique was employed.
- A purified carboxyl-terminal fragment of human c-Myc, containing the bHLH domain, was used for in vitro binding assays.
Main Results:
- The carboxyl-terminal fragment of c-Myc specifically bound to the DNA sequence CACGTG in vitro.
- This binding was sequence-specific, confirming a previously undetected DNA recognition capability of c-Myc.
Conclusions:
- The carboxyl-terminal region of c-Myc mediates sequence-specific DNA binding.
- This specific DNA binding is likely a mechanism through which Myc family proteins carry out their biological functions.