Juan Inostroza - Academia.edu (original) (raw)

Papers by Juan Inostroza

Research paper thumbnail of Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription

Cell, 1992

We have discovered a protein termed Dr1 that interacts with the TATA-binding protein, TBP. The as... more We have discovered a protein termed Dr1 that interacts with the TATA-binding protein, TBP. The association of Dr1 with TBP results in repression of both basal and activated levels of transcription. The interaction of Dr1 with TBP precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Dr1 activity is associated with a 19 kd protein. A cDNA clone encoding Dr1 was isolated. Dr1 is phosphorylated in vivo and phosphorylation of Dr1 affected its interaction with TBP. Our results suggest a regulatory role for Dr1 in repression of transcription mediated via phosphorylation.

Research paper thumbnail of Glándula pineal humana, factores reguladores de la producción de melatonina: Morfometría, celularidad y células c-Kit

Revista Internacional de …, Jan 1, 2007

Se obtuvieron glándulas pineales humanas de preparaciones anatómicas frescas: a) grupo 1, de 1 a ... more Se obtuvieron glándulas pineales humanas de preparaciones anatómicas frescas: a) grupo 1, de 1 a 6 años, n = 6; b) grupo 2, de 12 a 17 años, n = 3; c) grupo 3, de 20 a 30 años, n = 3, y d) grupo 4, de 35 años de edad, n = 3. Las muestras fijadas en formol (pH, 7,2) durante ...

Research paper thumbnail of Transcriptional Repression by Dr1, a TATA-binding Protein-associated Phosphoprotein and Inhibitor of Classes II and III Gene Expression

Research paper thumbnail of The effect of paraoxon on spermatogenesis in Dugesia gonocephala from the Chilean Altiplano: proliferation and apoptosis

… Science and Pollution …, Jan 1, 2011

Research paper thumbnail of Role of the phosphatase PP4 in the activation of JNK-1 in prostate carcinoma cell lines PC-3 and LNCaP resulting in increased AP-1 and EGR-1 activity

Biological Research, Jan 1, 2005

Research paper thumbnail of The MAP Kinases are Differently Utilized by CD28 and CD2 Adhesion Pathways in Superantigen-Activated Jurkat T cell

Biological Research, Jan 1, 2003

Research paper thumbnail of Apolipoprotein A‐I synthesis during the acclimatization of the carp (Cyprinus carpio)

Journal of …, Jan 1, 1990

Research paper thumbnail of Differential regulation of RNA polymerases I, II, and III by the TBP-binding repressor Dr1

Science, Jan 1, 1994

RNA polymerases I, II, and III each use the TATA-binding protein (TBP). Regulators that target th... more RNA polymerases I, II, and III each use the TATA-binding protein (TBP). Regulators that target this shared factor may therefore provide a means to coordinate the activities of the three nuclear RNA polymerases. The repressor Dr1 binds to TBP and blocks the interaction of TBP with polymerase II- and polymerase III-specific factors. This enables Dr1 to coordinately regulate transcription by RNA polymerases II and III. Under the same conditions, Dr1 does not inhibit polymerase I transcription. By selectively repressing polymerases II and III, Dr1 may shift the physiological balance of transcriptional output in favor of polymerase I.

Research paper thumbnail of Factors involved in specific transcription by mammalian RNA polymerase II. Purification and functional analysis of general transcription factor IIE.

Journal of Biological Chemistry, Jan 1, 1991

Research paper thumbnail of Interaction of the Dr1 inhibitory factor with the TATA binding protein is disrupted by adenovirus E1A

Proceedings of the …, Jan 1, 1994

Research paper thumbnail of Structure-function analysis of the TBP-binding protein Dr1 reveals a mechanism for repression of class II gene transcription.

Research paper thumbnail of Requirement of a corepressor for Dr1-mediated repression of transcription.

Research paper thumbnail of Structure and functional properties of human general transcription factor IIE

Research paper thumbnail of Transcriptional repression by Msx-1 does not require homeodomain DNA-binding sites

… and cellular biology, Jan 1, 1995

This study investigates the transcriptional properties of Msx-1, a murine homeodomain protein whi... more This study investigates the transcriptional properties of Msx-1, a murine homeodomain protein which has been proposed to play a key role in regulating the differentiation and/or proliferation state of specific cell populations during embryogenesis. We show, using basal and activated transcription templates, that Msx-1 is a potent repressor of transcription and can function through both TATA-containing and TATA-less promoters. Moreover, repression in vivo and in vitro occurs in the absence of DNA-binding sites for the Msx-1 homeodomain. Utilizing a series of truncated Msx-1 polypeptides, we show that multiple regions of Msx-1 contribute to repression, and these are rich in alanine, glycine, and proline residues. When fused to a heterologous DNA-binding domain, both N- and C-terminal regions of Msx-1 retain repressor function, which is dependent upon the presence of the heterologous DNA-binding site. Moreover, a polypeptide consisting of the full-length Msx-1 fused to a heterologous DNA-binding domain is a more potent repressor than either the N- or C-terminal regions alone, and this fusion retains the ability to repress transcription in the absence of the heterologous DNA site. We further show that Msx-1 represses transcription in vitro in a purified reconstituted assay system and interacts with protein complexes composed of TBP and TFIIA (DA) and TBP, TFIIA, and TFIIB (DAB) in gel retardation assays, suggesting that the mechanism of repression is mediated through interaction(s) with a component(s) of the core transcription complex. We speculate that the repressor function of Msx-1 is critical for its proposed role in embryogenesis as a regulator of cellular differentiation.

Research paper thumbnail of Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation

Research paper thumbnail of The Transcriptional Co-Activator P/CIP Binds CBP and Mediates Nuclear-Receptor Function

Nature, Jan 1, 1997

The functionally conserved proteins CBP and p300 act in conjunction with other factors to activat... more The functionally conserved proteins CBP and p300 act in conjunction with other factors to activate transcription of DNA. A new factor, p/CIP, has been discovered that is present in the cell as a complex with CBP and is required for transcriptional activity of nuclear receptors and other CBP/p300-dependent transcription factors. The highly related nuclear-receptor co-activator protein NCoA-1 is also specifically required for ligand-dependent activation of genes by nuclear receptors. p/CIP, NCoA-1 and CBP all contain related leucine-rich charged helical interaction motifs that are required for receptor-specific mechanisms of gene activation, and allow the selective inhibition of distinct signal-transduction pathways.

Research paper thumbnail of Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription

Cell, 1992

We have discovered a protein termed Dr1 that interacts with the TATA-binding protein, TBP. The as... more We have discovered a protein termed Dr1 that interacts with the TATA-binding protein, TBP. The association of Dr1 with TBP results in repression of both basal and activated levels of transcription. The interaction of Dr1 with TBP precludes the formation of a transcription-competent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Dr1 activity is associated with a 19 kd protein. A cDNA clone encoding Dr1 was isolated. Dr1 is phosphorylated in vivo and phosphorylation of Dr1 affected its interaction with TBP. Our results suggest a regulatory role for Dr1 in repression of transcription mediated via phosphorylation.

Research paper thumbnail of Glándula pineal humana, factores reguladores de la producción de melatonina: Morfometría, celularidad y células c-Kit

Revista Internacional de …, Jan 1, 2007

Se obtuvieron glándulas pineales humanas de preparaciones anatómicas frescas: a) grupo 1, de 1 a ... more Se obtuvieron glándulas pineales humanas de preparaciones anatómicas frescas: a) grupo 1, de 1 a 6 años, n = 6; b) grupo 2, de 12 a 17 años, n = 3; c) grupo 3, de 20 a 30 años, n = 3, y d) grupo 4, de 35 años de edad, n = 3. Las muestras fijadas en formol (pH, 7,2) durante ...

Research paper thumbnail of Transcriptional Repression by Dr1, a TATA-binding Protein-associated Phosphoprotein and Inhibitor of Classes II and III Gene Expression

Research paper thumbnail of The effect of paraoxon on spermatogenesis in Dugesia gonocephala from the Chilean Altiplano: proliferation and apoptosis

… Science and Pollution …, Jan 1, 2011

Research paper thumbnail of Role of the phosphatase PP4 in the activation of JNK-1 in prostate carcinoma cell lines PC-3 and LNCaP resulting in increased AP-1 and EGR-1 activity

Biological Research, Jan 1, 2005

Research paper thumbnail of The MAP Kinases are Differently Utilized by CD28 and CD2 Adhesion Pathways in Superantigen-Activated Jurkat T cell

Biological Research, Jan 1, 2003

Research paper thumbnail of Apolipoprotein A‐I synthesis during the acclimatization of the carp (Cyprinus carpio)

Journal of …, Jan 1, 1990

Research paper thumbnail of Differential regulation of RNA polymerases I, II, and III by the TBP-binding repressor Dr1

Science, Jan 1, 1994

RNA polymerases I, II, and III each use the TATA-binding protein (TBP). Regulators that target th... more RNA polymerases I, II, and III each use the TATA-binding protein (TBP). Regulators that target this shared factor may therefore provide a means to coordinate the activities of the three nuclear RNA polymerases. The repressor Dr1 binds to TBP and blocks the interaction of TBP with polymerase II- and polymerase III-specific factors. This enables Dr1 to coordinately regulate transcription by RNA polymerases II and III. Under the same conditions, Dr1 does not inhibit polymerase I transcription. By selectively repressing polymerases II and III, Dr1 may shift the physiological balance of transcriptional output in favor of polymerase I.

Research paper thumbnail of Factors involved in specific transcription by mammalian RNA polymerase II. Purification and functional analysis of general transcription factor IIE.

Journal of Biological Chemistry, Jan 1, 1991

Research paper thumbnail of Interaction of the Dr1 inhibitory factor with the TATA binding protein is disrupted by adenovirus E1A

Proceedings of the …, Jan 1, 1994

Research paper thumbnail of Structure-function analysis of the TBP-binding protein Dr1 reveals a mechanism for repression of class II gene transcription.

Research paper thumbnail of Requirement of a corepressor for Dr1-mediated repression of transcription.

Research paper thumbnail of Structure and functional properties of human general transcription factor IIE

Research paper thumbnail of Transcriptional repression by Msx-1 does not require homeodomain DNA-binding sites

… and cellular biology, Jan 1, 1995

This study investigates the transcriptional properties of Msx-1, a murine homeodomain protein whi... more This study investigates the transcriptional properties of Msx-1, a murine homeodomain protein which has been proposed to play a key role in regulating the differentiation and/or proliferation state of specific cell populations during embryogenesis. We show, using basal and activated transcription templates, that Msx-1 is a potent repressor of transcription and can function through both TATA-containing and TATA-less promoters. Moreover, repression in vivo and in vitro occurs in the absence of DNA-binding sites for the Msx-1 homeodomain. Utilizing a series of truncated Msx-1 polypeptides, we show that multiple regions of Msx-1 contribute to repression, and these are rich in alanine, glycine, and proline residues. When fused to a heterologous DNA-binding domain, both N- and C-terminal regions of Msx-1 retain repressor function, which is dependent upon the presence of the heterologous DNA-binding site. Moreover, a polypeptide consisting of the full-length Msx-1 fused to a heterologous DNA-binding domain is a more potent repressor than either the N- or C-terminal regions alone, and this fusion retains the ability to repress transcription in the absence of the heterologous DNA site. We further show that Msx-1 represses transcription in vitro in a purified reconstituted assay system and interacts with protein complexes composed of TBP and TFIIA (DA) and TBP, TFIIA, and TFIIB (DAB) in gel retardation assays, suggesting that the mechanism of repression is mediated through interaction(s) with a component(s) of the core transcription complex. We speculate that the repressor function of Msx-1 is critical for its proposed role in embryogenesis as a regulator of cellular differentiation.

Research paper thumbnail of Determinants of coactivator LXXLL motif specificity in nuclear receptor transcriptional activation

Research paper thumbnail of The Transcriptional Co-Activator P/CIP Binds CBP and Mediates Nuclear-Receptor Function

Nature, Jan 1, 1997

The functionally conserved proteins CBP and p300 act in conjunction with other factors to activat... more The functionally conserved proteins CBP and p300 act in conjunction with other factors to activate transcription of DNA. A new factor, p/CIP, has been discovered that is present in the cell as a complex with CBP and is required for transcriptional activity of nuclear receptors and other CBP/p300-dependent transcription factors. The highly related nuclear-receptor co-activator protein NCoA-1 is also specifically required for ligand-dependent activation of genes by nuclear receptors. p/CIP, NCoA-1 and CBP all contain related leucine-rich charged helical interaction motifs that are required for receptor-specific mechanisms of gene activation, and allow the selective inhibition of distinct signal-transduction pathways.