The evolution of the 9aaTAD domain in Sp2 proteins: inactivation with valines and intron reservoirs.

ABSTRACT: The universal nine-amino-acid transactivation domains (9aaTADs) have been identified in numerous transcription activators. Here, we identified the conserved 9aaTAD motif in all nine members of the specificity protein (SP) family. Previously, the Sp1 transcription factor has been defined as a glutamine-rich activator. We showed by amino acid substitutions that the glutamine residues are completely dispensable for 9aaTAD function and are not conserved in the SP family. We described the origin and evolutionary history of 9aaTADs. The 9aaTADs of the ancestral Sp2 gene became inactivated in early chordates. We next discovered that an accumulation of valines in 9aaTADs inactivated their transactivation function and enabled their strict conservation during evolution. Subsequently, in chordates, S

SUBMITTER: Piskacek M 

PROVIDER: S-EPMC11105055 | biostudies-literature | 2020 May

REPOSITORIES: biostudies-literature