A conserved acidic patch in the Myb domain is required for activation of an endogenous target gene and for chromatin binding.

Journal Article (Journal Article)

The c-Myb protein is a transcriptional regulator initially identified by homology to the v-Myb oncoprotein, and has since been implicated in human cancer. The most highly conserved portion of the c-Myb protein is the DNA-binding domain which consists of three imperfect repeats. Many other proteins contain one or more Myb-related domains, including a number of proteins that do not bind directly to DNA. We performed a phylogenetic analysis of diverse classes of Myb-related domains and discovered a highly conserved patch of acidic residues common to all Myb-related domains. These acidic residues are positioned in the first of three alpha-helices within each of the three repeats that comprise the c-Myb DNA-binding domain. Interestingly, these conserved acidic residues are present on a surface of the protein which is distinct from that which binds to DNA. Alanine mutagenesis revealed that the acidic patch of the third c-Myb repeat is essential for transcriptional activity, but neither for nuclear localization nor DNA-binding. Instead, these acidic residues are required for efficient chromatin binding and interaction with the histone H4 N-terminal tail.

Full Text

Duke Authors

Cited Authors

  • Ko, ER; Ko, D; Chen, C; Lipsick, JS

Published Date

  • October 7, 2008

Published In

Volume / Issue

  • 7 /

Start / End Page

  • 77 -

PubMed ID

  • 18840288

Pubmed Central ID

  • PMC2572630

Electronic International Standard Serial Number (EISSN)

  • 1476-4598

Digital Object Identifier (DOI)

  • 10.1186/1476-4598-7-77


  • eng

Conference Location

  • England