Mark Eben Massari

TL;DR: The helix-loop-helix (HLH) family of transcriptional regulatory proteins are key players in a wide array of developmental processes, including neurogenesis, myogenesis, hematopoiesis, and pancreatic development and the structure and functional properties are examined.

TL;DR: Two conserved boxes in the E2A amino-terminal domain are identified that show extensive homology within the transactivation domains of E12, E47, E2-2, HEB, and daughterless, all members of the same class of helix-loop-helix proteins, and are proposed to represent a novel transactivation domain distinct from the previously characterized acidic blob, proline-rich, and glutamine-rich activation motifs.

TL;DR: This work identifies a novel motif, LDFS, present in the vertebrate class I HLH proteins as well as in a yeast HLH protein that is essential for transactivation and provides both genetic and biochemical evidence that the highly conserved LDFs motif stimulates transcription by direct recruitment of the SAGA histone acetyltransferase complex.

TL;DR: Structural and functional analyses of AD1 reveal striking similarities to the acidic class of activators and it is proposed that the unstructured domain may become helical upon interaction with its cellular target molecule.