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Identification of human TFIID components and direct interaction between a 250-kDa polypeptide and the TATA box-binding protein (TFIID tau).

作者信息

Takada R, Nakatani Y, Hoffmann A, Kokubo T, Hasegawa S, Roeder R G, Horikoshi M

机构信息

Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.

出版信息

Proc Natl Acad Sci U S A. 1992 Dec 15;89(24):11809-13. doi: 10.1073/pnas.89.24.11809.

Abstract

Previous studies have indicated that human transcription initiation factor TFIID is a large complex that contains a TATA-binding polypeptide (TFIID tau or TBP) and other components that qualitatively alter promoter interactions and are uniquely required for activator-dependent (versus basal) transcription. TFIID tau-specific antibody columns have been employed to identify a number of human TFIID polypeptides that are tightly associated with TFIID tau. These differ in size from polypeptides in known general initiation factors, including the initiator-binding factor (TFII-I) which shares some promoter binding characteristics with TFIID. The largest component (p250) identified in TFIID was shown to interact directly and tightly with TFIID tau, suggesting that it may play a major role in the assembly of the TFIID complex.

摘要
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/d01a/50646/7692fd86ed6d/pnas01098-0171-a.jpg

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