Abstract：
:c-Myc (Myc) and Max proteins dimerize and bind DNA through basic-helix-loop-helix-leucine zipper motifs (b-HLH-LZ). Using a genetic approach, we demonstrate that binding to Max is essential for Myc transforming activity and that Myc homodimers are inactive. Mutants of Myc and Max that bind efficiently to each other but not to their wild-type partners were generated by either exchanging the HLH-LZ domains or reciprocally modifying LZ dimerization specificities. While transformation defective on their own, complementary mutants restore Myc transforming activity when coexpressed in cells. The HLH-LZ exchange mutants also have dominant negative activity on wild-type Myc function. In addition, wild-type max antagonizes myc function in a dose-dependent manner, presumably through competition of Max-Max and Myc-Max dimers for common target DNA sites. Therefore, Max can function as both suppressor and activator of Myc. A general model for the role of Myc and Max in growth control is discussed.
journal_name
Celljournal_title
Cellauthors
Amati B,Brooks MW,Levy N,Littlewood TD,Evan GI,Land Hdoi
10.1016/0092-8674(93)90663-bsubject
Has Abstractpub_date
1993-01-29 00:00:00pages
233-45issue
2eissn
0092-8674issn
1097-4172pii
0092-8674(93)90663-Bjournal_volume
72pub_type
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