HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kim, T. K. Articles by Roeder, R. G. Search for Related Content PubMed PubMed Citation Articles by Kim, T. K. Articles by Roeder, R. G. Social Bookmarking                      What's this?

Volume 272, Number 11, Issue of March 14, 1997 pp. 7540-7545
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

---

Critical Role of the Second Stirrup Region of the TATA-binding Protein for Transcriptional Activation Both in Yeast and Human

(Received for publication, August 22, 1996, and in revised form, January 3, 1997)

From the Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, New York 10021

We previously identified three TATA-binding protein (TBP) point mutations (L114K, L189K, and K211L) that have severe effects on transcriptional activation by acidic activators, but no effect on basal transcription, in a yeast-derived TBP-dependent in vitro transcription system (Kim, T. K., Hashimoto, S., Kelleher, R. J., III, Flanagan, P. M., Kornberg, R. D., Horikoshi, M., and Roeder, R. G. (1994) Nature 369, 252-255). These activation defects were also demonstrated in vivo in yeast cells (Lee, M., and Struhl, K. (1995) Mol. Cell. Biol. 15, 5461-5469). Here, the transcriptional activities of these and other TBP mutations were examined in human by both in vitro and in vivo assays. Mutations L189K and E188K, which lie in the second stirrup region of TBP, show defective activation by acidic activators both in yeast and human. Somewhat surprisingly, mutations L114K and K211L have almost no demonstrable effect on activation by acidic activators in human, in contrast to their severe effects on defective activator responses in yeast. The implications of these results for TBP structure and function are discussed.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				R. P. Darst, A. Dasgupta, C. Zhu, J.-Y. Hsu, A. Vroom, T. Muldrow, and D. T. Auble Mot1 Regulates the DNA Binding Activity of Free TATA-binding Protein in an ATP-dependent Manner J. Biol. Chem., April 4, 2003; 278(15): 13216 - 13226. [Abstract] [Full Text] [PDF]

				T. K. Kim, T. H. Kim, and T. Maniatis Efficient recruitment of TFIIB and CBP-RNA polymerase II holoenzyme by an interferon-beta enhanceosome in vitro PNAS, October 13, 1998; 95(21): 12191 - 12196. [Abstract] [Full Text] [PDF]

				P. Leng, P. E. Carter, and A. J. P. Brown The TATA-Binding Protein (TBP) from the Human Fungal Pathogen Candida albicans Can Complement Defects in Human and Yeast TBPs J. Bacteriol., April 1, 1998; 180(7): 1771 - 1776. [Abstract] [Full Text]