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  • 1
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    Spermiogenesis deficiency in mice lacking the Trf2 gene (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-16
    Description: The discovery of TATA-binding protein-related factors (TRFs) has suggested alternative mechanisms for gene-specific transcriptional regulation and raised interest in their biological functions. In contrast to recent observations of an embryonic lethal phenotype for TRF2 inactivation in Caenorhabditis elegans and Xenopus laevis, we found that Trf2-deficient mice are viable. However, Trf2-/- mice are sterile because of a severe defect in spermiogenesis. Postmeiotic round spermatids advance at most to step 7 of differentiation but fail to progress to the elongated form, and gene-specific transcription deficiencies were identified. We speculate that mammals may have evolved more specialized TRF2 functions in the testis that involve transcriptional regulation of genes essential for spermiogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, D -- Penttila, T L -- Morris, P L -- Teichmann, M -- Roeder, R G -- New York, N.Y. -- Science. 2001 May 11;292(5519):1153-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11352070" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Cell Differentiation ; Cell Size ; DNA-Binding Proteins/*deficiency/genetics/*physiology ; Female ; *Gene Deletion ; Gene Expression Regulation, Developmental ; Gene Targeting ; Genotype ; Infertility, Male/genetics/pathology ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Organ Size ; RNA, Messenger/genetics/metabolism ; Spermatogenesis/*genetics ; Spermatozoa/metabolism/pathology ; Telomeric Repeat Binding Protein 2 ; Testis/abnormalities/metabolism/pathology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Transcription factor OTF-1 is functionally identical to the DNA replication factor NF-III (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-02
    Description: Octamer transcription factor-1 (OTF-1) and nuclear factor III (NF-III) are sequence-specific DNA binding proteins that activate transcription and DNA replication, respectively. It is shown here that OTF-1 is physically and biologically indistinguishable from NF-III. This conclusion is based on the following observations. First, the two proteins have identical mobilities by SDS-polyacrylamide gel electrophoresis. Second, OTF-1 binds to the adenovirus origin of DNA replication at the same site and with the same affinity as NF-III. Third, OTF-1 can substitute for NF-III in activating the initiation of adenovirus DNA replication in vitro. Fourth, the ability of OTF-1 to stimulate viral DNA replication is dependent on the presence of an intact NF-III binding site within the origin of replication. Fifth, NF-III can substitute for OTF-1 in activating in vitro transcription from the human histone H2b promoter. These data suggest the possibility that NF-III/OTF-1 is a protein that functions in both cellular DNA replication and transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Neill, E A -- Fletcher, C -- Burrow, C R -- Heintz, N -- Roeder, R G -- Kelly, T J -- CA16519/CA/NCI NIH HHS/ -- CA42567/CA/NCI NIH HHS/ -- R0IGM32544/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1210-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3413485" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/physiology ; DNA Replication/*drug effects ; DNA-Binding Proteins/metabolism/*pharmacology ; Electrophoresis, Polyacrylamide Gel ; HeLa Cells ; Histones/genetics ; Host Cell Factor C1 ; Humans ; Molecular Weight ; Nuclear Proteins/metabolism/*pharmacology ; Octamer Transcription Factor-1 ; Promoter Regions, Genetic ; Transcription Factors/metabolism/*pharmacology ; Transcription, Genetic/*drug effects ; Virus Replication/drug effects
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Physical analysis of transcription preinitiation complex assembly on a class II gene promoter (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-09
    Description: Transcription of protein-encoding genes by human RNA polymerase II requires multiple ancillary proteins (transcription factors). Interactions between these proteins and the promoter DNA of a viral class II gene (the major late transcription unit of adenovirus) were investigated by enzymatic and chemical footprinting. The experiments indicated that the assembly of functionally active RNA polymerase II-containing transcription preinitiation complexes requires a complete set of transcription factors, and that both specific protein-DNA and protein-protein interactions are involved. This allows individual steps along the transcription reaction pathway to be tested directly, thus providing a basis for understanding basic transcription initiation mechanisms as well as the regulatory processes that act on them.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van Dyke, M W -- Roeder, R G -- Sawadogo, M -- CA 42567/CA/NCI NIH HHS/ -- GM 38212/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 9;241(4871):1335-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3413495" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviruses, Human/genetics ; Base Sequence ; DNA-Binding Proteins/physiology ; Deoxyribonucleases/metabolism ; Macromolecular Substances ; Molecular Sequence Data ; Nuclear Proteins/physiology ; *Promoter Regions, Genetic ; RNA Polymerase II/*metabolism ; *Regulatory Sequences, Nucleic Acid ; Transcription Factors/*physiology ; *Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation (2008)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2008-05-02
    Description: Numerous post-translational modifications of histones have been described in organisms ranging from yeast to humans. Growing evidence for dynamic regulation of these modifications, position- and modification-specific protein interactions, and biochemical crosstalk between modifications has strengthened the 'histone code' hypothesis, in which histone modifications are integral to choreographing the expression of the genome. One such modification, ubiquitylation of histone H2B (uH2B) on lysine 120 (K120) in humans, and lysine 123 in yeast, has been correlated with enhanced methylation of lysine 79 (K79) of histone H3 (refs 5-8), by K79-specific methyltransferase Dot1 (KMT4). However, the specific function of uH2B in this crosstalk pathway is not understood. Here we demonstrate, using chemically ubiquitylated H2B, a direct stimulation of hDot1L-mediated intranucleosomal methylation of H3 K79. Two traceless orthogonal expressed protein ligation (EPL) reactions were used to ubiquitylate H2B site-specifically. This strategy, using a photolytic ligation auxiliary and a desulphurization reaction, should be generally applicable to the chemical ubiquitylation of other proteins. Reconstitution of our uH2B into chemically defined nucleosomes, followed by biochemical analysis, revealed that uH2B directly activates methylation of H3 K79 by hDot1L. This effect is mediated through the catalytic domain of hDot1L, most likely through allosteric mechanisms. Furthermore, asymmetric incorporation of uH2B into dinucleosomes showed that the enhancement of methylation was limited to nucleosomes bearing uH2B. This work demonstrates a direct biochemical crosstalk between two modifications on separate histone proteins within a nucleosome.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3774535/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3774535/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McGinty, Robert K -- Kim, Jaehoon -- Chatterjee, Champak -- Roeder, Robert G -- Muir, Tom W -- GM07739/GM/NIGMS NIH HHS/ -- R01 GM086868/GM/NIGMS NIH HHS/ -- England -- Nature. 2008 Jun 5;453(7196):812-6. doi: 10.1038/nature06906. Epub 2008 Apr 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Synthetic Protein Chemistry, The Rockefeller University, New York, New York 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18449190" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Animals ; Catalytic Domain ; Histones/chemical synthesis/*metabolism ; Humans ; Lysine/metabolism ; Methylation ; Methyltransferases/genetics/*metabolism ; Nucleosomes/chemistry/*metabolism ; Ubiquitin/*metabolism ; Xenopus
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Published by Nature Publishing Group (NPG)
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  • 5
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    GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis (2009)
    Nature Publishing Group (NPG)
    Details
    Publication Date: 2009-04-21
    Description: The post-translational modifications of histone tails generate a 'histone code' that defines local and global chromatin states. The resultant regulation of gene function is thought to govern cell fate, proliferation and differentiation. Reversible histone modifications such as methylation are under mutual controls to organize chromosomal events. Among the histone modifications, methylation of specific lysine and arginine residues seems to be critical for chromatin configuration and control of gene expression. Methylation of histone H3 lysine 4 (H3K4) changes chromatin into a transcriptionally active state. Reversible modification of proteins by beta-N-acetylglucosamine (O-GlcNAc) in response to serum glucose levels regulates diverse cellular processes. However, the epigenetic impact of protein GlcNAcylation is unknown. Here we report that nuclear GlcNAcylation of a histone lysine methyltransferase (HKMT), MLL5, by O-GlcNAc transferase facilitates retinoic-acid-induced granulopoiesis in human HL60 promyelocytes through methylation of H3K4. MLL5 is biochemically identified in a GlcNAcylation-dependent multi-subunit complex associating with nuclear retinoic acid receptor RARalpha (also known as RARA), serving as a mono- and di-methyl transferase to H3K4. GlcNAcylation at Thr 440 in the MLL5 SET domain evokes its H3K4 HKMT activity and co-activates RARalpha in target gene promoters. Increased nuclear GlcNAcylation by means of O-GlcNAc transferase potentiates retinoic-acid-induced HL60 granulopoiesis and restores the retinoic acid response in the retinoic-acid-resistant HL60-R2 cell line. Thus, nuclear MLL5 GlcNAcylation triggers cell lineage determination of HL60 through activation of its HKMT activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujiki, Ryoji -- Chikanishi, Toshihiro -- Hashiba, Waka -- Ito, Hiroaki -- Takada, Ichiro -- Roeder, Robert G -- Kitagawa, Hirochika -- Kato, Shigeaki -- England -- Nature. 2009 May 21;459(7245):455-9. doi: 10.1038/nature07954. Epub 2009 Apr 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19377461" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylglucosamine/*metabolism ; Cell Lineage ; Cell Nucleus/metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Granulocytes/*cytology/*drug effects ; HL-60 Cells ; Histone-Lysine N-Methyltransferase/chemistry/*metabolism ; Humans ; Leukopoiesis/*drug effects ; Multiprotein Complexes/chemistry/isolation & purification/metabolism ; N-Acetylglucosaminyltransferases/chemistry/*metabolism ; Protein Structure, Tertiary ; Receptors, Retinoic Acid/metabolism ; Threonine/metabolism ; Tretinoin/*pharmacology
    Print ISSN: 0028-0836
    Electronic ISSN: 1476-4687
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
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  • 6
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    Repression of HIV-1 transcription by a cellular protein (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-03-22
    Description: A cellular DNA binding protein, LBP-1, sequentially interacts in a concentration-dependent manner with two sites that surround the transcriptional initiation site of the human immunodeficiency virus type 1 (HIV-1) promoter. Although sequences in the downstream site (site I) were found to enhance transcription, purified LBP-1 specifically repressed transcription in vitro by binding to the upstream site (site II), which overlaps the TATA element. The binding of human TATA binding factor (TFIID) to the promoter before LBP-1 blocked repression, suggesting that repression resulted from an inhibition of TFIID binding to the TATA element. Furthermore, mutations that eliminated binding to site II both prevented repression in vitro and increased HIV-1 transcription in stably transformed cells. These findings suggest that a cellular factor regulates HIV-1 transcription in a manner that is characteristic of bacterial repressors and that this factor could be important in HIV-1 latency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kato, H -- Horikoshi, M -- Roeder, R G -- AI27397/AI/NIAID NIH HHS/ -- CA42567/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1991 Mar 22;251(5000):1476-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry and Molecular Biology, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2006421" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Binding Proteins/genetics ; *Gene Expression Regulation, Viral ; HIV-1/*genetics ; Molecular Sequence Data ; Promoter Regions, Genetic ; Repressor Proteins/*genetics ; Transcription Factor TFIID ; Transcription Factors/metabolism ; Transcription, Genetic
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
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    The leukemogenicity of AML1-ETO is dependent on site-specific lysine acetylation (2011)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2011-07-19
    Description: The chromosomal translocations found in acute myelogenous leukemia (AML) generate oncogenic fusion transcription factors with aberrant transcriptional regulatory properties. Although therapeutic targeting of most leukemia fusion proteins remains elusive, the posttranslational modifications that control their function could be targetable. We found that AML1-ETO, the fusion protein generated by the t(8;21) translocation, is acetylated by the transcriptional coactivator p300 in leukemia cells isolated from t(8;21) AML patients, and that this acetylation is essential for its self-renewal-promoting effects in human cord blood CD34(+) cells and its leukemogenicity in mouse models. Inhibition of p300 abrogates the acetylation of AML1-ETO and impairs its ability to promote leukemic transformation. Thus, lysine acetyltransferases represent a potential therapeutic target in AML.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3251012/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3251012/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Lan -- Gural, Alexander -- Sun, Xiao-Jian -- Zhao, Xinyang -- Perna, Fabiana -- Huang, Gang -- Hatlen, Megan A -- Vu, Ly -- Liu, Fan -- Xu, Haiming -- Asai, Takashi -- Xu, Hao -- Deblasio, Tony -- Menendez, Silvia -- Voza, Francesca -- Jiang, Yanwen -- Cole, Philip A -- Zhang, Jinsong -- Melnick, Ari -- Roeder, Robert G -- Nimer, Stephen D -- GM62437/GM/NIGMS NIH HHS/ -- R01 GM062437/GM/NIGMS NIH HHS/ -- R01 GM062437-12/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2011 Aug 5;333(6043):765-9. doi: 10.1126/science.1201662. Epub 2011 Jul 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Pharmacology and Chemistry Program, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21764752" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Animals ; Cell Line ; Cell Line, Tumor ; *Cell Transformation, Neoplastic ; Core Binding Factor Alpha 2 Subunit/chemistry/*metabolism ; E1A-Associated p300 Protein/antagonists & inhibitors/*metabolism ; Fetal Blood/cytology ; Gene Expression Profiling ; Hematopoietic Stem Cells/*cytology/physiology ; Humans ; Leukemia, Myeloid, Acute/*metabolism/pathology ; Lysine/*metabolism ; Mice ; Mice, Inbred C57BL ; Mutant Proteins/metabolism ; Oncogene Proteins, Fusion/chemistry/*metabolism ; Preleukemia/metabolism/pathology ; Protein Binding ; Protein Interaction Domains and Motifs ; Protein Processing, Post-Translational ; Transcriptional Activation ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 8
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    Biochemistry. Have your PIC! (2013)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2013-11-10
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malik, Sohail -- Roeder, Robert G -- New York, N.Y. -- Science. 2013 Nov 8;342(6159):706-7. doi: 10.1126/science.1246170.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry and Molecular Biology, Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/24202169" target="_blank"〉PubMed〈/a〉
    Keywords: Catalytic Domain ; Cryoelectron Microscopy ; Crystallography ; DNA/*chemistry ; Humans ; *Promoter Regions, Genetic ; Protein Conformation ; RNA Polymerase II/*chemistry ; Transcription Factors, General/*chemistry ; *Transcription Initiation, Genetic
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Human PAD4 regulates histone arginine methylation levels via demethylimination (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-09-04
    Description: Methylation of arginine (Arg) and lysine residues in histones has been correlated with epigenetic forms of gene regulation. Although histone methyltransferases are known, enzymes that demethylate histones have not been identified. Here, we demonstrate that human peptidylarginine deiminase 4 (PAD4) regulates histone Arg methylation by converting methyl-Arg to citrulline and releasing methylamine. PAD4 targets multiple sites in histones H3 and H4, including those sites methylated by coactivators CARM1 (H3 Arg17) and PRMT1 (H4 Arg3). A decrease of histone Arg methylation, with a concomitant increase of citrullination, requires PAD4 activity in human HL-60 granulocytes. Moreover, PAD4 activity is linked with the transcriptional regulation of estrogen-responsive genes in MCF-7 cells. These data suggest that PAD4 mediates gene expression by regulating Arg methylation and citrullination in histones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Yanming -- Wysocka, Joanna -- Sayegh, Joyce -- Lee, Young-Ho -- Perlin, Julie R -- Leonelli, Lauriebeth -- Sonbuchner, Lakshmi S -- McDonald, Charles H -- Cook, Richard G -- Dou, Yali -- Roeder, Robert G -- Clarke, Steven -- Stallcup, Michael R -- Allis, C David -- Coonrod, Scott A -- DK55274/DK/NIDDK NIH HHS/ -- GM R01 26020/GM/NIGMS NIH HHS/ -- GM R01 50659/GM/NIGMS NIH HHS/ -- HD R01 38353/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2004 Oct 8;306(5694):279-83. Epub 2004 Sep 2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetic Medicine, Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15345777" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arginine/*metabolism ; Blotting, Western ; Calcimycin/pharmacology ; Cell Line, Tumor ; Citrulline/metabolism ; Gene Expression Regulation ; Genes, Reporter ; HL-60 Cells ; Histones/*metabolism ; Humans ; Hydrolases/*metabolism ; Ionophores/pharmacology ; Membrane Proteins/genetics ; Methylamines/metabolism ; Methylation ; Molecular Sequence Data ; Presenilin-2 ; Promoter Regions, Genetic ; Protein-Arginine N-Methyltransferases/metabolism ; Recombinant Fusion Proteins/metabolism ; Recombinant Proteins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    E protein silencing by the leukemogenic AML1-ETO fusion protein (2004)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2004-08-31
    Description: The AML1-ETO fusion protein, generated by the t(8;21) chromosomal translocation, is causally involved in nearly 15% of acute myeloid leukemia (AML) cases. This study shows that AML1-ETO, as well as ETO, inhibits transcriptional activation by E proteins through stable interactions that preclude recruitment of p300/CREB-binding protein (CBP) coactivators. These interactions are mediated by a conserved ETO TAF4 homology domain and a 17-amino acid p300/CBP and ETO target motif within AD1 activation domains of E proteins. In t(8;21) leukemic cells, very stable interactions between AML1-ETO and E proteins underlie a t(8;21) translocation-specific silencing of E protein function through an aberrant cofactor exchange mechanism. These studies identify E proteins as AML1-ETO targets whose dysregulation may be important for t(8;21) leukemogenesis, as well as an E protein silencing mechanism that is distinct from that associated with differentiation-inhibitory proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Jinsong -- Kalkum, Markus -- Yamamura, Soichiro -- Chait, Brian T -- Roeder, Robert G -- New York, N.Y. -- Science. 2004 Aug 27;305(5688):1286-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Biochemistry and Molecular Biology, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15333839" target="_blank"〉PubMed〈/a〉
    Keywords: Acute Disease ; Amino Acid Sequence ; Basic Helix-Loop-Helix Transcription Factors ; CREB-Binding Protein ; Cell Line ; Cell Line, Tumor ; Conserved Sequence ; Core Binding Factor Alpha 2 Subunit ; DNA-Binding Proteins/genetics/*metabolism ; *Gene Silencing ; HeLa Cells ; Hematopoietic Stem Cells/physiology ; Humans ; Jurkat Cells ; Leukemia, Myeloid/genetics/*metabolism ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Oncogene Proteins, Fusion/genetics/*metabolism ; Protein Binding ; Protein Structure, Tertiary ; TCF Transcription Factors ; Trans-Activators/metabolism ; Transcription Factor 7-Like 2 Protein ; Transcription Factors/genetics/*metabolism ; Transcriptional Activation ; Translocation, Genetic
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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