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Transcriptional Repression by RING Finger Protein TIF1 That Interacts with the KRAB Repressor Domain of KOX1


Moosmann, P; Georgiev, O; Le Douarin, B; Bourquin, J-P; Schaffner, W (1996). Transcriptional Repression by RING Finger Protein TIF1 That Interacts with the KRAB Repressor Domain of KOX1. Nucleic Acids Research, 24(24):4859-4867.

Abstract

Many of the vertebrate zinc finger factors of the Krüppel type (C2H2 zinc fingers) contain in their N-terminus a conserved sequence referred to as the KRAB (Krüppel-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, TIF1β (also named KAP-1), that specifically interacts with the KRAB domain of the human zinc finger factor KOX1/ZNF10. TIF1β, TIF1α, 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 TIF1α, TIF1β also contains an additional Cys/His cluster (PHD finger) and a bromorelated domain. When tethered to DNA, TIF1β 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 TIF1β is a mediator of the transcriptional repression exerted by the KRAB domain

Abstract

Many of the vertebrate zinc finger factors of the Krüppel type (C2H2 zinc fingers) contain in their N-terminus a conserved sequence referred to as the KRAB (Krüppel-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, TIF1β (also named KAP-1), that specifically interacts with the KRAB domain of the human zinc finger factor KOX1/ZNF10. TIF1β, TIF1α, 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 TIF1α, TIF1β also contains an additional Cys/His cluster (PHD finger) and a bromorelated domain. When tethered to DNA, TIF1β 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 TIF1β is a mediator of the transcriptional repression exerted by the KRAB domain

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Item Type:Journal Article, refereed, original work
Communities & Collections:National licences > 142-005
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Scopus Subject Areas:Life Sciences > Genetics
Language:English
Date:1 December 1996
Deposited On:25 Sep 2018 13:14
Last Modified:15 Apr 2021 14:49
Publisher:Oxford University Press
ISSN:0305-1048
OA Status:Hybrid
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1093/nar/24.24.4859

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