the grouchotlegrg family of transcriptional co-repressorsgrouchotlegrg家族的转录体若.pdf

Protein family review TThhee GGrroouucchhoo//TTLLEE//GGrrgg ffaammiillyy ooff ttrraannssccrriippttiioonnaall ccoo--rreepprreessssoorrss Barbara H Jennings and David Ish-Horowicz Address: Developmental Genetics Laboratory, Cancer Research UK, Lincoln’s Inn Fields, London, WC2A 3PX, UK. Correspondence: David Ish-Horowicz. Email: david.horowicz@.uk Published: 31 January 2008 Genome BBiioollooggyy 2008, 99::205 (doi:10.1186/gb-2008-9-1-205) The electronic version of this article is the complete one and can be found online at /2008/9/1/205 © 2008 BioMed Central Ltd SSuummmmaarryy The Drosophila Groucho (Gro) protein was the founding member of the family of transcriptional co-repressor proteins that now includes the transducin-like enhancer of split (TLE) and Gro- related gene (Grg) proteins in vertebrates. Gro family proteins do not bind DNA directly, but are recruited by a diverse profile of transcription factors, including members of the Hes, Runx, Nkx, LEF1/Tcf, Pax, Six and c-Myc families. The primary structure of Gro proteins includes five identifiable regions, of which the most highly conserved are the amino-terminal glutamine-rich Q domain and the carboxy-terminal WD-repeat domain. The Q domain contains two coiled-coil motifs that facilitate oligomerization into tetramers and binding to some transcription factors. The WD domain folds to form a β-propeller, which mediates protein-protein interactions. Many transcription factors interact with the WD domain via a short peptide motif that falls into either of two classes: WRPW and related tetrapeptides; and the ‘eh1’ motif (FxIxxIL). Gro family proteins are broadly expr