Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF

Katsuhiko Kamada; Jacqueline De Angelis; Robert G. Roeder; Stephen K. Burley

doi:10.1073/pnas.051631098

Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF

Katsuhiko Kamada, Jacqueline De Angelis, Robert G. Roeder, Stephen K. Burley

Research output: Contribution to journal › Article › peer-review

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Abstract

The x-ray structure of a C-terminal fragment of the RAP74 subunit of human transcription factor (TF) IIF has been determined at 1.02-Å resolution. The α/β structure is strikingly similar to the globular domain of linker histone H5 and the DNA-binding domain of hepatocyte nuclear factor 3γ (HNF-3γ), making it a winged-helix protein. The surface electrostatic properties of this compact domain differ significantly from those of bona fide winged-helix transcription factors (HNF-3γ and RFX1) and from the winged-helix domains found within the RAP30 subunit of TFIIF and the β subunit of TFIIE. RAP74 has been shown to interact with the TFIIF-associated C-terminal domain phosphatase FCP1, and a putative phosphatase binding site has been identified within the RAP74 winged-helix domain.

Original language	English (US)
Pages (from-to)	3115-3120
Number of pages	6
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	98
Issue number	6
DOIs	https://doi.org/10.1073/pnas.051631098
State	Published - Mar 13 2001
Externally published	Yes

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title = "Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF",

abstract = "The x-ray structure of a C-terminal fragment of the RAP74 subunit of human transcription factor (TF) IIF has been determined at 1.02-{\AA} resolution. The α/β structure is strikingly similar to the globular domain of linker histone H5 and the DNA-binding domain of hepatocyte nuclear factor 3γ (HNF-3γ), making it a winged-helix protein. The surface electrostatic properties of this compact domain differ significantly from those of bona fide winged-helix transcription factors (HNF-3γ and RFX1) and from the winged-helix domains found within the RAP30 subunit of TFIIF and the β subunit of TFIIE. RAP74 has been shown to interact with the TFIIF-associated C-terminal domain phosphatase FCP1, and a putative phosphatase binding site has been identified within the RAP74 winged-helix domain.",

author = "Katsuhiko Kamada and {De Angelis}, Jacqueline and Roeder, {Robert G.} and Burley, {Stephen K.}",

year = "2001",

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doi = "10.1073/pnas.051631098",

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T1 - Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF

AU - Kamada, Katsuhiko

AU - De Angelis, Jacqueline

AU - Roeder, Robert G.

AU - Burley, Stephen K.

PY - 2001/3/13

Y1 - 2001/3/13

N2 - The x-ray structure of a C-terminal fragment of the RAP74 subunit of human transcription factor (TF) IIF has been determined at 1.02-Å resolution. The α/β structure is strikingly similar to the globular domain of linker histone H5 and the DNA-binding domain of hepatocyte nuclear factor 3γ (HNF-3γ), making it a winged-helix protein. The surface electrostatic properties of this compact domain differ significantly from those of bona fide winged-helix transcription factors (HNF-3γ and RFX1) and from the winged-helix domains found within the RAP30 subunit of TFIIF and the β subunit of TFIIE. RAP74 has been shown to interact with the TFIIF-associated C-terminal domain phosphatase FCP1, and a putative phosphatase binding site has been identified within the RAP74 winged-helix domain.

AB - The x-ray structure of a C-terminal fragment of the RAP74 subunit of human transcription factor (TF) IIF has been determined at 1.02-Å resolution. The α/β structure is strikingly similar to the globular domain of linker histone H5 and the DNA-binding domain of hepatocyte nuclear factor 3γ (HNF-3γ), making it a winged-helix protein. The surface electrostatic properties of this compact domain differ significantly from those of bona fide winged-helix transcription factors (HNF-3γ and RFX1) and from the winged-helix domains found within the RAP30 subunit of TFIIF and the β subunit of TFIIE. RAP74 has been shown to interact with the TFIIF-associated C-terminal domain phosphatase FCP1, and a putative phosphatase binding site has been identified within the RAP74 winged-helix domain.

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JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

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Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF

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