Transcriptional intermediary factor-2

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues

Reexamination Certificate

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C530S300000

Reexamination Certificate

active

06861508

ABSTRACT:
The present invention concerns a nuclear receptor (NR) transcriptional mediator. More specifically, isolated nucleic acid molecules are provided encoding transcriptional intermediary factor-2 (TIF2). Recombinant methods for making TIF2 polypeptides are also provided as are TIF2 antibodies. Screening methods are also provided for identifying agonists and antagonists of the activation function AF-2 of nuclear receptors, for identifying agonists and antagonists of the AD1 activation domain activity of TIF2, and for identifying agonists and antagonists of the AD2 activation domain activity of TIF2.

REFERENCES:
patent: 5508164 (1996-04-01), Kausch et al.
patent: 6268173 (2001-07-01), Chambon et al.
patent: WO 9612823 (1996-05-01), None
patent: WO 9802455 (1998-01-01), None
Berry, M., et al., “Role of the two activating domains of the oestrogen receptor in the cell-type and promoter-context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen,”EMBO J. 9:2811-2818, Oxford University Press (1990).
Bocquel, M.T., et al., “The contribution of the N- and C-terminal regions of steroid receptors to activation of transcription is both receptor and cell-specific,”Nucl. Acids Res. 17:2581-2595, Oxford University Press (1989).
Bourguet, W., et al., “Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-α,”Nature 375:377-382, Nature Publishing Group (Jun. 1995).
Cavailles, V., et al., “Interaction of proteins with transcriptionally active estrogen receptors,”Proc. Natl. Acad. Sci. USA 91:10009-10013, National Academy of Sciences (1994).
Cavailles, V., et al., “Nuclear factor RIP140 modulates transcriptional activation by the estrogen receptor,”EMBO J. 14:3741-3751, Oxford University Press (Aug. 1995).
Danielian, P.S., et al., “Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors,”EMBO J. 11:1025-1033, Oxford University Press (1992).
Durand, B., et al., “Activation function 2 (AF-2) of retinoic acid receptor and 9-cis retinoic acid receptor: presence of a conserved autonomous constitutive activating domain and influence of the nature of the response element of AF-2 activity,”EMBO J. 13:5370-5382, Oxford University Press (1994).
George, D.G., et al., in:Macromolecular Sequencing and Synthesis. Selected Methods and Applications,Schlesinger, D.H., ed., Alan R. Liss, Inc., New York, pp. 127-149 (1988).
Glass, C.K., et al., “Nuclear receptor coactivators,”Curr. Opin. Cell Biol. 9:222-232, Current Biology Ltd. (Apr. 1997).
Halachmi, S., et al., “Estrogen Receptor-Associated Proteins: Possible Mediators of Hormone-Induced Transcription,”Science 264:1455-1458, American Association for the Advancement of Science (1994).
Hanstein, B., et al., “p300 is a component of an estrogen receptor coactivator complex,”Proc. Natl. Acad. Sci. USA 93:11540-11545, National Academy of Sciences (Oct. 1996).
Heery, D.M. et al., “A signature motif in transcriptional co-activators mediates binding to nuclear receptors,”Nature 387:733-736, Nature Publishing Group (Jun. 1997).
Hong, H., et al., “GRIP1, a novel mouse protein that serves as a transcriptional coactivator in yeast for the hormone binding domains of steroid receptors,”Proc. Natl. Acad. Sci. USA 93:4948-4952, National Academy of Sciences (May 1996).
Hong, H., et al., “GRIP1, a Transcriptional Coactivator for the AF-2 Transactivation Domain of Steroid, Thyroid, Retinoid, and Vitamin D Receptors,”Mol. Cell. Biol. 17:2735-2744, American Society for Microbiology (May 1997).
Jacq, X., et al., “Human TAFII30 Is Present in a Distinct TFIID Complex and Is Required for Transcriptional Activation by the Estrogen Receptor,”Cell 79:107-117, Cell Press (1994).
Kamei, Y., et al., “CBP Integrator Complex Mediates Transcriptional Activation and AP-1 Inhibition by Nuclear Receptors,”Cell 85:403-414, Cell Press (May 1996).
Kastner, P., et al., “Structure, localization and transcriptional properties of two classes of retinoic acid receptor α fusion proteins in acute promyelocytic leukemia (APL): structural similarities with a new family of oncoproteins,”EMBO J. 11:629-642, Oxford University Press (1992).
Kurokawa, R., et al., “Polarity-specific activities of retinoic acid receptors determined by a co-repressor,”Nature 377:451-454, Nature Publishing Group (Oct. 1995).
Le Douarin, B., et al., “The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18,”EMBO J. 14:2020-2033, Oxford University Press (May 1995).
Le Douarin, B., et al., “A possible involvement of TIF1α and TIFβ in the epigenetic control of transcription by nuclear receptors,”EMBO J. 15:6701-6715, Oxford University Press (Dec. 1996).
Lee, J.W., et al., “Two Classes of Proteins Dependent on Either the Presence or Absence of Thyroid Hormone for Interaction with the Thyroid Hormone Receptor,”Mol. Endocrinol. 9:243-254, The Endocrine Society (Feb. 1995).
Lee, J.W., et al., “Interaction of thyroid-hormone receptor with a conserved transcriptional mediator,”Nature 374:91-94, Nature Publishing Group (Mar. 1995).
Mengus, G., et al., “Cloning and characterization of hTAFII18, hTAFII20 and hTAFII28: three subunits of the human transcription factor TFIID,”EMBO J. 14:1520-1531 (Apr. 1995).
Metzger, D., et al., “Promoter specificity of the two transcriptional activation functions of the human oestrogen receptor in yeast,”Nucl. Acids Res. 20:2813-2817, Oxford University Press (1992).
Meyer, M.-E., et al., “Steroid Hormone Receptors Compete for Factors That Mediate Their Enhancer Function,”Cell 57:433-422, Cell Press (1989).
Meyer, M.-E., et al., “Agonistic and antagonistic activities of RU486 on the functions of the human progesterone receptor,”EMBO J. 9:3923-3932, Oxford University Press (1990).
Onate, S.A., et al., “Sequence and Characterization of a Coactivator for the Steroid Hormone Receptor Superfamily,”Science 270:1354-1357, American Association for the Advancement of Science (Nov. 1995).
Pierrat, B., et al., “Functional analysis of the human estrogen receptor using a phenotypic transctivation assay in yeast,”Gene 119:237-245, Elsevier Science B.V. (1992).
Pierrat, B., et al., “A highly conserved region in the hormone-binding domain of the human estrogen receptor functions as an efficient transactivation domain in yeast,”Gene 143:193-200, Elsevier Science B.V. (1994).
Renaud, J.-P., et al., “Crystal structure of the RAR-γ ligand-binding domain bound to all-trans retinoic acid,”Nature 378681-689, Nature Publishing Group (Dec. 1995).
Tasset, D., et al., “Distinct Classes of Transcriptional Activating Domains Function by Different Mechanisms,”Cell 62:1177-1187, Cell Press (1990).
Torchia, J., et al., “The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function,”Nature 387:677-684, Nature Publishing Group (Jun. 1997).
Voegel, J.J., et al., “TIF2, a 16 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors,”EMBO J. 15:3667-3675, Oxford University Press (Jul. 1996).
vom Baur, E., et al., “Differential ligand-dependent interactions between the AF-2 activating domain of nuclear receptors and the putative transcriptional intermediary factors mSUG1 and TIF1,”EMBO J. 15:110-124, Oxford University Press (Jan. 1996).
Wagner, R.L., et al., “A structural role for hormone in the thyroid hormone receptor,”Nature 378:690-697, Nature Publishing Group (Dec. 1995).
Wurtz, J.-M., et al., “A canonical structure for the ligand-binding domain of nuclear recept

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