STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) OF 300-316, REGION, FUNCTION (ISOFORM I), MUTAGENESIS OF 29-LYS-ARG-30; GLU-32; ARG-33; 49-LYS-LYS-50; ASP-53; 66-GLU-GLU-67 AND 303-LEU-LEU-304
Categories
Family & Domains, Function, Disease & Variants, Structure
Modification of TFIIF provides one pathway through which efficient Gdown1 loading can occur early in elongation allowing downstream pausing to be regulated.
Gdown1 competes with TFIIF for binding to the RPB1 and RPB5 subunits of Pol II thereby inhibiting an essential function of TFIIF in preinitiation complex assembly.
Data identify GRINL1A as a membrane-associated DYNLL1 binding partner and suggest that additional DYNLL1-binding partners are present near this glutamate channel homolog.
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