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Max: functionaldomains andinteraction withc-Myc. Gregory J. KatoW M LeeL L Chen1992 год

Max: functional domains and interaction with c-Myc.
статья из журнала

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Аннотация: The product of the c-myc proto-oncogene is a DNA-binding protein, the deregulated expression of which is associated with a variety of malignant neoplasms. The cDNA for the max gene was recently cloned as a result of the ability of its protein product to interact with the c-Myc protein. We studied bacterially produced Max, c-Myc, and a series of truncated c-Myc proteins. Full-length c-Myc alone cannot bind DNA. However, a truncated c-Myc protein comprising the basic, helix-loop-helix, and leucine zipper regions can bind specifically to DNA bearing the sequence GGGCAC(G/A)TGCCC. Max protein, either alone or in a heteromeric complex with full-length c-Myc, binds to the same core sequence. Using a novel combination of chemical and photo-cross-linking analysis, we demonstrate that either Max or a c-Myc/Max heteromeric complex binds to DNA virtually exclusively in a dimeric structure. Using fusion proteins in cultured cells, we establish a number of functional characteristics of Max. First, we show that Max can interact with c-Myc intracellularly in a manner dependent on the integrity of the helix-loop-helix and leucine zipper motifs. Second, a nuclear localization domain that contains the sequence PQSRKKLR is mapped to the carboxy-terminal region of Max. Third, Max lacks a transcriptional activation domain that is functional in Chinese hamster ovary cells when fused to a heterologous DNA-binding domain. These data suggest that Max may serve as a cofactor for c-Myc in transcriptional activation or, by itself, as a transcriptional repressor.
Год издания: 1992
Авторы: Gregory J. Kato, W M Lee, L L Chen, Chi V. Dang
Издательство: Cold Spring Harbor Laboratory Press
Источник: Genes & Development
Ключевые слова: RNA modifications and cancer, Ubiquitin and proteasome pathways, Cancer-related Molecular Pathways
Другие ссылки: Genes & Development (PDF)
Genes & Development (HTML)
PubMed (HTML)