Site-specific proteolysis of the transcriptional coactivator HCF-1 can regulate its interaction with protein cofactors.

ABSTRACT: Limited proteolytic processing is an important transcriptional regulatory mechanism. In various contexts, proteolysis controls the cytoplasmic-to-nuclear transport of important transcription factors or removes domains to produce factors with altered activities. The transcriptional coactivator host cell factor-1 (HCF-1) is proteolytically processed within a unique domain consisting of 20-aa reiterations. Site-specific cleavage within one or more repeats generates a family of amino- and carboxyl-terminal subunits that remain tightly associated. However, the consequences of HCF-1 processing have been undefined. In this study, it was determined that the HCF-1-processing domain interacts with several proteins including the transcriptional coactivator/corepressor four-and-a-half LIM domain-2 (FH

SUBMITTER: Vogel JL 

PROVIDER: S-EPMC1440766 | biostudies-literature | 2006 May

REPOSITORIES: biostudies-literature