Crystal Structure of Negative Cofactor 2 Recognizing the TBP-DNA Transcription Complex

Tipo de material: Texto

TextoSeries ; Cell, 106(1), p.71-81, 2001Trabajos contenidos:

Kamada, K
Shu, F
Chen, H
Malik, S
Stelzer, G
Roeder, R.G
Meisterernst, M
Meisterernst, M

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Resumen: The X-ray structure of a ternary complex of Negative Cofactor 2 (NC2), the TATA box binding protein (TBP), and DNA has been determined at 2.6 A° resolution. The N termini of NC2 a and ß resemble histones H2A and H2B, respectively, and form a heterodimer that binds to the bent DNA double helix on the underside of the preformed TBP-DNA complex via electrostatic interactions. NC2ß contributes to inhibition of TATA-dependent transcription through interactions of its C-terminal a helix with a conserved hydrophobic feature on the upper surface of TBP, which in turn positions the penultimate a helix of NC2ß to block recognition of the TBP-DNA complex by transcription factor IIB. Further regulatory implications of the NC2 heterodimer structure are discussed.

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The X-ray structure of a ternary complex of Negative Cofactor 2 (NC2), the TATA box binding protein (TBP), and DNA has been determined at 2.6 A° resolution. The N termini of NC2 a and ß resemble histones H2A and H2B, respectively, and form a heterodimer that binds to the bent DNA double helix on the underside of the preformed TBP-DNA complex via electrostatic interactions. NC2ß contributes to inhibition of TATA-dependent transcription through interactions of its C-terminal a helix with a conserved hydrophobic feature on the upper surface of TBP, which in turn positions the penultimate a helix of NC2ß to block recognition of the TBP-DNA complex by transcription factor IIB. Further regulatory implications of the NC2 heterodimer structure are discussed.

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