منابع مشابه
A structural perspective of CTD function.
The C-terminal domain (CTD) of RNA polymerase II (Pol II) integrates nuclear events by binding proteins involved in mRNA biogenesis. CTD-binding proteins recognize a specific CTD phosphorylation pattern, which changes during the transcription cycle, due to the action of CTD-modifying enzymes. Structural and functional studies of CTD-binding and -modifying proteins now reveal some of the mechani...
متن کاملA structural perspective on Mediator function.
Gene transcription by RNA polymerase II requires the multiprotein coactivator complex Mediator. Mediator was identified two decades ago, but its molecular mechanisms remain poorly understood, because structural studies are hampered by its large size, modularity, and flexibility. Here we collect all available structural data on Mediator and discuss their functional implications. Progress was mad...
متن کاملEvolution of function in protein superfamilies, from a structural perspective.
The recent growth in protein databases has revealed the functional diversity of many protein superfamilies. We have assessed the functional variation of homologous enzyme superfamilies containing two or more enzymes, as defined by the CATH protein structure classification, by way of the Enzyme Commission (EC) scheme. Combining sequence and structure information to identify relatives, the majori...
متن کاملStructural Basis of Transcription Activation: The CAP- CTD-DNA Complex
The Escherichia coli catabolite activator protein (CAP) activates transcription at Plac, Pgal, and other promoters through interactions with the RNA polymerase subunit carboxyl-terminal domain ( CTD). We determined the crystal structure of the CAPCTD-DNA complex at a resolution of 3.1 angstroms. CAP makes direct protein-protein interactions with CTD, and CTD makes direct protein-DNA interaction...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Genes & Development
سال: 2005
ISSN: 0890-9369
DOI: 10.1101/gad.1318105