Evolution of lysine acetylation in the RNA polymerase II C-terminal domain.

ABSTRACT:

Background

RPB1, the largest subunit of RNA polymerase II, contains a highly modifiable C-terminal domain (CTD) that consists of variations of a consensus heptad repeat sequence (Y1S2P3T4S5P6S7). The consensus CTD repeat motif and tandem organization represent the ancestral state of eukaryotic RPB1, but across eukaryotes CTDs show considerable diversity in repeat organization and sequence content. These differences may reflect lineage-specific CTD functions mediated by protein interactions. Mammalian CTDs contain eight non-consensus repeats with a lysine in the seventh position (K7). Posttranslational acetylation of these sites was recently shown to be required for proper polymerase pausing and regulation of two growth factor-regulated genes.

Results

To investigate the origi

SUBMITTER: Simonti CN 

PROVIDER: S-EPMC4362643 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature