Abstract:Carboxyl-terminal repeat domain (CTD) of RNA polymerase Ⅱ largest subunit Rpb1 is essential for transcription regulation. Carboxyl-terminal repeat domain kinase (CTDK-I) is composed of CTK1, CTK2 and CTK3, acting on RNA polymerase Ⅱ carboxyl-terminal repeat domain and phosphorylating CTD heptapeptide repeat (YSPTSPS) for regulating transcription and translation. The specific protein CTK3 binds to cyclin CTK2 to form a heterodimer, controlling CTK1 activity by binding to CTK1. Structural and functional study of CTK1, a homologous protein of cyclin dependent kinase (CDK), may provide a new idea for the research of CDK family, and analysis of the regulatory mechanism of activation of CTK1 by CTK2-CTK3 complex may offer an innovative method for developing cell cycle protein inhibitors. This article reviews the functional characteristics of CTDK-I and the structures and interactions of its subunits and provides a useful guide for the studies of CTDK-I complex in the future.