sectin N regulaition of transcription in eukaryoted.ppt

Section N Regulation of transcription in eukaryotes N1 Eukaryotic Transcription Factors Transcription factor domain structure (link) DNA-binding domains Dimerization domains Transcription activation domains Repressor domains Targets for transcriptional regulation (link) Common features of transcription factors bind specifically to some DNA sites: specific motifs in promoters, upstream regulatory elements (UREs) or enhancer regions. Some factors modulate transcription by protein-protein intracation Activate/repress transcription. N1-2: DNA-binding domains The helix-turn-helix domain The zinc finger domain The basic domain Return to menu… 2. Bacteriophage DNA-binding proteins such as the phage λ cro repressor, lac and trp repressors, and cAMP receptor protein, CRP. Examples: (1) TFIIIA, the RNA Pol III transcription factor, with C2H2 zinc finger repeated 9 times. (2) SP1, with 3 copies of C2H2 zinc finger. Usually, three or more C2H2 zinc fingers are required for DNA binding. The basic domain Rich in basic amino acid residues found in a number of DNA-binding proteins generally associated with one or other of two dimerization domains, the leucine zipper or the helix-loop-helix(HLH) motif, resulting in basic leucine zipper (bZIP) or basic HLH proteins. Dimerization of the proteins brings together two basic domains which can then interact with DNA. N1-3: Dimerization domains Leucine zippers The helix-loop-helix domain (HLH) Leucine zipper proteins contain a hydrophobic leucine residue at every seventh position in a region that is often at the C-terminal part of the DNA-binding domain (picture.). These leucines are responsible for dimerization through interaction between the hydrophobic faces of the α-helices. This interaction forms a coiled-coil structure bZIP (basic leucine zipper) transcription factors: contain a basic DNA-binding domain N-terminal to the leucine zipper. The N-terminal basic domai