Journal of Biological Chemistry · 1998 · 145 citations · 54 references
Life SciencesBiochemistryMolecular BiologyEnzymologyGene ExpressionTranscriptionRna Polymerase FunctionRna Polymerase Ii TranscriptionRna Polymerase RegulationRna-binding ProteinsRna-protein InteractionsInitiation Factor RecruitmentProtein Phosphatase CatalysisProtein Phosphatase ComplexesRna Polymerase Ii FunctionRna Polymerase Ii RegulationRna Polymerase InitiationSubunit StoichiometryTfiif Function
TFIIF (RAP30/74) is a general initiation factor that also increases the rate of elongation by RNA polymerase II. A two-hybrid screen for RAP74-interacting proteins produced cDNAs encoding FCP1a, a novel, ubiquitously expressed human protein that interacts with the carboxyl-terminal evolutionarily conserved domain of RAP74. Related cDNAs encoding FCP1b lack a carboxyl-terminal RAP74-binding domain of FCP1a. FCP1 is an essential subunit of a RAP74-stimulated phosphatase that processively dephosphorylates the carboxyl-terminal domain of the largest RNA polymerase II subunit. FCP1 is also a stoichiometric component of a human RNA polymerase II holoenzyme complex.
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