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The zinc-finger protein Kruppel (Kr) [1] is an integral part of the Drosophila segmentation gene cascade [2] and is essential in organogenesis during later embryonic development [3]. In tissue culture, Kr regulates transcription [4-9]. Monomeric Kr can act as a transcriptional activator, whereas Kr dimers formed at high concentrations cause repression [6]. Here we show that Kr-dependent control of transcription involves functional interactions with components of the basal RNA polymerase II transcription machinery, which includes the initiation factors TFIIA, B, E, F, H and I [10,11] as well as the TATA-binding protein (TBP) and TBP-associated factors (TAFs) contained in the multisubunit TFIID [12]. Our results indicate that when acting from a site close to a basal monomeric Kr interacts with TFIIB to activate transcription, whereas an interaction of the Kr dimer with TFIIE beta, a subunit of TFIIE, results in transcriptional repression.

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