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Related Experiment Videos

Max: functional domains and interaction with c-Myc.

G J Kato1, W M Lee, L L Chen

  • 1Department of Pediatrics, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.

Genes & Development
|January 1, 1992
PubMed
Summary
This summary is machine-generated.

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The Max protein interacts with c-Myc, binding DNA in dimeric structures. Max may act as a cofactor for c-Myc or function as a transcriptional repressor.

Area of Science:

  • Molecular Biology
  • Oncology
  • Genetics

Background:

  • The c-Myc proto-oncogene product is a DNA-binding protein implicated in various cancers.
  • The Max gene was cloned due to its protein's interaction with c-Myc.

Purpose of the Study:

  • To investigate the DNA-binding properties and functional characteristics of the Max protein, both alone and in complex with c-Myc.
  • To elucidate the role of Max in transcriptional regulation.

Main Methods:

  • Bacterial production of Max, c-Myc, and truncated c-Myc proteins.
  • DNA-binding assays using specific DNA sequences.
  • Chemical and photo-cross-linking analysis to determine binding structures.
  • Fusion protein experiments in cultured cells to map functional domains.

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Main Results:

  • A truncated c-Myc protein (basic, helix-loop-helix, leucine zipper) binds DNA (GGGCAC(G/A)TGCCC).
  • Max protein, alone or with c-Myc, binds the same DNA sequence.
  • Max and c-Myc/Max complexes bind DNA primarily as dimers.
  • Max interacts with c-Myc intracellularly, dependent on helix-loop-helix and leucine zipper motifs.
  • A nuclear localization domain in Max is mapped to its carboxy-terminal region.
  • Max lacks a functional transcriptional activation domain in Chinese hamster ovary cells.

Conclusions:

  • Max protein forms dimeric complexes with itself or c-Myc for DNA binding.
  • Max protein may function as a cofactor for c-Myc in transcriptional activation.
  • Max protein may act as a transcriptional repressor independently.