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

J. Biol. Chem., Vol. 279, Issue 9, 7447-7455, February 27, 2004

This Article Full Text Full Text (PDF) All Versions of this Article: 279/9/7447    most recent M305412200v1 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 Nakadai, T. Articles by Tamura, T.-a. Search for Related Content PubMed PubMed Citation Articles by Nakadai, T. Articles by Tamura, T.-a. Social Bookmarking                      What's this?

Specific Interaction with Transcription Factor IIA and Localization of the Mammalian TATA-binding Protein-like Protein (TLP/TRF2/TLF)^*

Tomoyoshi Nakadai, Miho Shimada, Daisuke Shima, Hiroshi Handa, and Taka-aki Tamura¶

From the Department of Biology, Faculty of Science, Chiba University, 1-33 Yayoicho, Inage-ku, Chiba 263-8522, Japan and the Graduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan

TBP-like protein (TLP) is structurally similar to the TATA-binding protein (TBP) and is thought to have a transcriptional regulation function. Although TLP has been found to form a complex with transcription factor IIA (TFIIA), the in vivo functions of TFIIA for TLP are not clear. In this study, we analyzed the interaction between TLP and TFIIA. We determined the biophysical properties for the interaction of TLP with TFIIA. Dissociation constants of TFIIA versus TLP and TFIIA versus TBP were 1.5 and 10 nM, respectively. Moreover, the dissociation rate constant of TLP and TFIIA (1.2 x 10^–4/M·s was significantly lower than that of TBP (2.1 x 10^–3/M·s). These results indicate that TLP has a higher affinity to TFIIA than does TBP and that the TLP-TFIIA complex is much more stable than is the TBP-TFIIA complex. We found that TLP forms a dimer and a trimer and that these multimerizations are inhibited by TFIIA. Moreover, TLP mutimers were more stable than a TBP dimer. We determined the amounts of TLPs in the nucleus and cytoplasm of NIH3T3 cells and found that the molecular number of TLP in the nucleus was only 4% of that in the cytoplasm. Immunostaining of cells also revealed cytoplasmic localization of TLP. We established cells that stably express mutant TLP lacking TFIIA binding ability and identified the amino acids of TLP required for TFIIA binding (Ala-32, Leu-33, Asn-37, Arg-52, Lys-53, Lys-78, and Arg-86). Interestingly, the level of TFIIA binding defective mutant TLPs in the nucleus was much higher than that of the wild-type TLP and TFIIA-interactable mutant TLPs. Immunostaining analyses showed consistent results. These results suggest that the TFIIA binding ability of TLP is required for characteristic cytoplasmic localization of TLP. TFIIA may regulate the intracellular molecular state and the function of TLP through its property of binding to TLP.

Received for publication, May 23, 2003 , and in revised form, August 15, 2003.

^* This work was supported in part by CREST Japan Science and Technology Corporation. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^¶ To whom correspondence should be addressed. Tel.: 81-43-290-2823; Fax: 81-43-290-2824; E-mail: ttamura{at}faculty.chiba-u.jp.

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

This article has been cited by other articles:

				J. H. Reina and N. Hernandez On a roll for new TRF targets Genes & Dev., November 15, 2007; 21(22): 2855 - 2860. [Full Text] [PDF]

				S. Shiraishi, C. Zhou, T. Aoki, N. Sato, T. Chiba, K. Tanaka, S. Yoshida, Y. Nabeshima, Y.-i. Nabeshima, and T.-a. Tamura TBP-interacting Protein 120B (TIP120B)/Cullin-associated and Neddylation-dissociated 2 (CAND2) Inhibits SCF-dependent Ubiquitination of Myogenin and Accelerates Myogenic Differentiation J. Biol. Chem., March 23, 2007; 282(12): 9017 - 9028. [Abstract] [Full Text] [PDF]

				P. Somboonthum, H. Ohta, S. Yamada, M. Onishi, A. Ike, Y. Nishimune, and M. Nozaki cAMP-responsive element in TATA-less core promoter is essential for haploid-specific gene expression in mouse testis Nucleic Acids Res., June 10, 2005; 33(10): 3401 - 3411. [Abstract] [Full Text] [PDF]

				J. A. Chong, M. M. Moran, M. Teichmann, J. S. Kaczmarek, R. Roeder, and D. E. Clapham TATA-Binding Protein (TBP)-Like Factor (TLF) Is a Functional Regulator of Transcription: Reciprocal Regulation of the Neurofibromatosis Type 1 and c-fos Genes by TLF/TRF2 and TBP Mol. Cell. Biol., April 1, 2005; 25(7): 2632 - 2643. [Abstract] [Full Text] [PDF]

				P. Kieffer-Kwon, I. Martianov, and I. Davidson Cell-specific Nucleolar Localization of TBP-related Factor 2 Mol. Biol. Cell, October 1, 2004; 15(10): 4356 - 4368. [Abstract] [Full Text] [PDF]