Nucleic Acids Research, Vol 24, Issue 24 4859-4867, Copyright © 1996 by Oxford University Press
P Moosmann, O Georgiev, B Le Douarin, JP Bourquin and W Schaffner
Many of the vertebrate zinc finger factors of the Kruppel type (C2H2 zinc
fingers) contain in their N-terminus a conserved sequence referred to as
the KRAB (Kruppel-associated box) domain that, when tethered to DNA,
efficiently represses transcription. Using the yeast two-hybrid system, we
have isolated an 835 amino acid RING finger (C3HC4 zinc finger) protein,
TIF1 beta (also named KAP-1), that specifically interacts with the KRAB
domain of the human zinc finger factor KOX1/ZNF10. TIF1 beta, TIF1 alpha,
PML and efp belong to a characteristic subgroup of RING finger proteins
that contain one or two other Cys/His-rich clusters (B boxes) and a
putative coiled-coil in addition to the classical C3HC4 RING finger motif
(RBCC configuration). Like TIF1 alpha, TIF1 beta also contains an
additional Cys/His cluster (PHD finger) and a bromo-related domain. When
tethered to DNA, TIF1 beta can repress transcription in transiently
transfected mammalian cells both from promoter-proximal and remote
(enhancer) positions, similarly to the KRAB domain itself. We propose that
TIF1 beta is a mediator of the transcriptional repression exerted by the
KRAB domain.
ARTICLES
Transcriptional repression by RING finger protein TIF1 beta that interacts with the KRAB repressor domain of KOX1
Institut fur Molekularbiologie der Universitat, Abteilung II, Zurich, Switzerland.
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