ANTHRBIO 201 Chapter Notes - Chapter 12: Aureus, Palindromic Sequence, Lac Operon

• School: U of M
• Department: Anthropology, Biological
• Course: ANTHRBIO 201
• Professor: John Mitani

Document Summary

The fact that the activators are bound to. Shown here is a cartoon for gal4: many also have a dimerization domain that allow proteins to form homodimers, heterodimers and multimers, some have effector-binding domains. Interaction among activators: dimerization (depends on protein), advantage of a dimer binding, 2 monomers bind 1 helical turn apart, 2 cis-acting sequences. Transcriptional activator domains: dna-binding domains, zinc-containing modules, homeodomains (hds) ~60 amino acids, helix-turn-helix structure: bzip and bhlh motifs. A highly basic dna binding motif linked to a protein dimerization motif such as leucine zippers (zip) and helix-loop-helix (hlh) motifs: transcription-activating domains, acidic domains (gal4). Contain many acidic amino acids: glutamine (q)-rich domains (sp1). Contain many glutamine (q) residues: proline-rich domains (ctf). Contain many proline (p) residues: the domains function independently, they are separated physically on the protein, they are folded independently of each other to form distinct 3d structures, they can operate independently of each other.