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Human SFMBT is a transcriptional repressor protein that selectively binds the N‐terminal tail of histone H3

dc.contributor.authorWu, Shuminen_US
dc.contributor.authorTrievel, Raymond C.en_US
dc.contributor.authorRice, Judd C.en_US
dc.date.accessioned2016-01-04T20:51:34Z
dc.date.available2016-01-04T20:51:34Z
dc.date.issued2007-07-10en_US
dc.identifier.citationWu, Shumin; Trievel, Raymond C.; Rice, Judd C. (2007). "Human SFMBT is a transcriptional repressor protein that selectively binds the N‐terminal tail of histone H3." FEBS Letters 581(17): 3289-3296.en_US
dc.identifier.issn0014-5793en_US
dc.identifier.issn1873-3468en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/116313
dc.publisherWiley Periodicals, Inc.en_US
dc.subject.otherSAMen_US
dc.subject.othersterile alpha motifen_US
dc.subject.otherL(3)MBTen_US
dc.subject.otherlethal (3) malignant brain tumoren_US
dc.subject.otherSCML2en_US
dc.subject.othersex comb on midleg-like 2en_US
dc.subject.otherPcGen_US
dc.subject.otherSFMBTen_US
dc.subject.otherPolycomben_US
dc.subject.otherTranscriptionen_US
dc.subject.otherChromatinen_US
dc.subject.otherHistone H3en_US
dc.subject.otherpolycomben_US
dc.subject.otherSFMBTen_US
dc.subject.otherScm-related gene containing four mbt domainsen_US
dc.subject.otherdSfmbten_US
dc.subject.otherDrosophila SFMBTen_US
dc.subject.otherhSFMBTen_US
dc.subject.otherhuman SFMBTen_US
dc.subject.otherMBTen_US
dc.subject.othermalignant brain tumoren_US
dc.titleHuman SFMBT is a transcriptional repressor protein that selectively binds the N‐terminal tail of histone H3en_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumUniversity of Michigan, Department of Biological Chemistry, Ann Arbor, MI 48109-0606, United Statesen_US
dc.contributor.affiliationotherUniversity of Southern California Keck School of Medicine, Department of Biochemistry and Molecular Biology, 1501 San Pablo Street, ZNI 225, MC 2821, Los Angeles, CA 90033, United Statesen_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/116313/1/feb2s0014579307006746.pdf
dc.identifier.doi10.1016/j.febslet.2007.06.025en_US
dc.identifier.sourceFEBS Lettersen_US
dc.identifier.citedreferenceW.K. Wang, V. Tereshko, P. Boccuni, D. MacGrogan, S.D. Nimer, D.J. Patel, Malignant brain tumor repeats: a three-leaved propeller architecture with ligand/peptide binding pockets. Structure, 11,( 2003 ), 775 – 789.en_US
dc.identifier.citedreferenceJ.L. Brown, D. Mucci, M. Whiteley, M.L. Dirksen, J.A. Kassis, The Drosophila Polycomb group gene pleiohomeotic encodes a DNA binding protein with homology to the transcription factor YY1. Mol. Cell, 1,( 1998 ), 1057 – 1064.en_US
dc.identifier.citedreferenceT. Klymenko, A Polycomb group protein complex with sequence-specific DNA-binding and selective methyl-lysine-binding activities. Genes Dev., 20,( 2006 ), 1110 – 1122.en_US
dc.identifier.citedreferenceH. Usui, T. Ichikawa, K. Kobayashi, T. Kumanishi, Cloning of a novel murine gene Sfmbt, Scm-related gene containing four mbt domains, structurally belonging to the Polycomb group of genes. Gene, 248,( 2000 ), 127 – 135.en_US
dc.identifier.citedreferenceD. Bornemann, E. Miller, J. Simon, The Drosophila Polycomb group gene Sex comb on midleg (Scm) encodes a zinc finger protein with similarity to polyhomeotic protein. Development, 122,( 1996 ), 1621 – 1630.en_US
dc.identifier.citedreferenceE. Montini, Identification of SCML2, a second human gene homologous to the Drosophila sex comb on midleg (Scm): a new gene cluster on Xp22. Genomics, 58,( 1999 ), 65 – 72.en_US
dc.identifier.citedreferenceJ. Wismar, The Drosophila melanogaster tumor suppressor gene lethal(3)malignant brain tumor encodes a proline-rich protein with a novel zinc finger. Mech. Dev., 53,( 1995 ), 141 – 154.en_US
dc.identifier.citedreferenceA. Sathyamurthy, M.D. Allen, A.G. Murzin, M. Bycroft, Crystal structure of the malignant brain tumor (MBT) repeats in Sex Comb on Midleg-like 2 (SCML2). J. Biol. Chem., 278,( 2003 ), 46968 – 46973.en_US
dc.identifier.citedreferenceJ.K. Sims, S.I. Houston, T. Magazinnik, J.C. Rice, A trans-tail histone code defined by monomethylated H4 Lys-20 and H3 Lys-9 demarcates distinct regions of silent chromatin. J. Biol. Chem., 281,( 2006 ), 12760 – 12766.en_US
dc.identifier.citedreferenceJ. Zhang, I. Zamir, M.A. Lazar, Differential recognition of liganded and unliganded thyroid hormone receptor by retinoid X receptor regulates transcriptional repression. Mol. Cell Biol., 17,( 1997 ), 6887 – 6897.en_US
dc.identifier.citedreferenceP. Webb, Estrogen receptor activation function 1 works by binding p160 coactivator proteins. Mol. Endocrinol., 12,( 1998 ), 1605 – 1618.en_US
dc.identifier.citedreferenceH.P. Harding, M.A. Lazar, The monomer-binding orphan receptor Rev-Erb represses transcription as a dimer on a novel direct repeat. Mol. Cell Biol., 15,( 1995 ), 4791 – 4802.en_US
dc.identifier.citedreferenceS.M. Rose, W.T. Garrard, Differentiation-dependent chromatin alterations precede and accompany transcription of immunoglobulin light chain genes. J. Biol. Chem., 259,( 1984 ), 8534 – 8544.en_US
dc.identifier.citedreferenceJ.C. Rice, K. Nishioka, K. Sarma, R. Steward, D. Reinberg, C.D. Allis, Mitotic-specific methylation of histone H4 Lys 20 follows increased PR- Set7 expression and its localization to mitotic chromosomes. Genes Dev., 16,( 2002 ), 2225 – 2230.en_US
dc.identifier.citedreferenceS.Y. Huang, W.T. Garrard, Electrophoretic analyses of nucleosomes and other protein–DNA complexes. Methods Enzymol., 170,( 1989 ), 116 – 142.en_US
dc.identifier.citedreferenceD.A. Jackson, P.R. Cook, Transcription occurs at a nucleoskeleton. Embo J., 4,( 1985 ), 919 – 925.en_US
dc.identifier.citedreferenceA. Thiru, Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin. Embo J., 23,( 2004 ), 489 – 499.en_US
dc.identifier.citedreferenceD.Y. Lee, J.P. Northrop, M.H. Kuo, M.R. Stallcup, Histone H3 lysine 9 methyltransferase G9a is a transcriptional coactivator for nuclear receptors. J. Biol. Chem., 281,( 2006 ), 8476 – 8485.en_US
dc.identifier.citedreferenceD. Chen, H. Ma, H. Hong, S.S. Koh, S.M. Huang, B.T. Schurter, D.W. Aswad, M.R. Stallcup, Regulation of transcription by a protein methyltransferase. Science, 284,( 1999 ), 2174 – 2177.en_US
dc.identifier.citedreferenceJ.C. Rice, K.S. Massey-Brown, B.W. Futscher, Aberrant methylation of the BRCA1 CpG island promoter is associated with decreased BRCA1 mRNA in sporadic breast cancer cells. Oncogene, 17,( 1998 ), 1807 – 1812.en_US
dc.identifier.citedreferenceT. Ishizuka, M.A. Lazar, The N-CoR/histone deacetylase 3 complex is required for repression by thyroid hormone receptor. Mol. Cell Biol., 23,( 2003 ), 5122 – 5131.en_US
dc.identifier.citedreferenceI. Zamir, J. Zhang, M.A. Lazar, Stoichiometric and steric principles governing repression by nuclear hormone receptors. Genes Dev., 11,( 1997 ), 835 – 846.en_US
dc.identifier.citedreferenceW. Fischle, Y. Wang, S.A. Jacobs, Y. Kim, C.D. Allis, S. Khorasanizadeh, Molecular basis for the discrimination of repressive methyl-lysine marks in histone H3 by Polycomb and HP1 chromodomains. Genes Dev., 17,( 2003 ), 1870 – 1881.en_US
dc.identifier.citedreferenceS.A. Jacobs, S. Khorasanizadeh, Structure of HP1 chromodomain bound to a lysine 9-methylated histone H3 tail. Science, 295,( 2002 ), 2080 – 2083.en_US
dc.identifier.citedreferenceJ. Min, Y. Zhang, R.M. Xu, Structural basis for specific binding of Polycomb chromodomain to histone H3 methylated at Lys 27. Genes Dev., 17,( 2003 ), 1823 – 1828.en_US
dc.identifier.citedreferenceV.G. Wilson, D. Rangasamy, Intracellular targeting of proteins by sumoylation. Exp. Cell Res., 271,( 2001 ), 57 – 65.en_US
dc.identifier.citedreferenceR. Farbiszewski, W. Rzeczycki, The digestion of basic proteins by extract of Guerin tumor lysosomes. Biochem. Biophys. Res. Commun., 65,( 1975 ), 280 – 285.en_US
dc.identifier.citedreferenceJ.E. Moskaitis, L.C. Shriver, A.T. Campagnoni, The association of myelin basic protein with itself and other proteins. Neurochem. Res., 12,( 1987 ), 409 – 417.en_US
dc.identifier.citedreferenceT.M. Fletcher, J.C. Hansen, Core histone tail domains mediate oligonucleosome folding and nucleosomal DNA organization through distinct molecular mechanisms. J. Biol. Chem., 270,( 1995 ), 25359 – 25362.en_US
dc.identifier.citedreferenceW. An, R.G. Roeder, Direct association of p300 with unmodified H3 and H4 N termini modulates p300-dependent acetylation and transcription of nucleosomal templates. J. Biol. Chem., 278,( 2003 ), 1504 – 1510.en_US
dc.identifier.citedreferenceD.P. Satijn, A.P. Otte, Polycomb group protein complexes: do different complexes regulate distinct target genes?. Biochim. Biophys. Acta, 1447,( 1999 ), 1 – 16.en_US
dc.identifier.citedreferenceJ.A. Simon, J.W. Tamkun, Programming off and on states in chromatin: mechanisms of Polycomb and trithorax group complexes. Curr. Opin. Genet. Dev., 12,( 2002 ), 210 – 218.en_US
dc.identifier.citedreferenceS. Maurer-Stroh, N.J. Dickens, L. Hughes-Davies, T. Kouzarides, F. Eisenhaber, C.P. Ponting, The Tudor domain ‘Royal Family’: Tudor, plant Agenet, Chromo, PWWP and MBT domains. Trends Biochem. Sci., 28,( 2003 ), 69 – 74.en_US
dc.identifier.citedreferenceM.V. Botuyan, J. Lee, I.M. Ward, J.E. Kim, J.R. Thompson, J. Chen, G. Mer, Structural basis for the methylation state-specific recognition of histone H4-K20 by 53BP1 and Crb2 in DNA repair. Cell, 127,( 2006 ), 1361 – 1373.en_US
dc.identifier.citedreferenceJ. Kim, J. Daniel, A. Espejo, A. Lake, M. Krishna, L. Xia, Y. Zhang, M.T. Bedford, Tudor, MBT and chromo domains gauge the degree of lysine methylation. EMBO Rep., 7,( 2006 ), 397 – 403.en_US
dc.identifier.citedreferenceJ. Schultz, F. Milpetz, P. Bork, C.P. Ponting, SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. USA, 95,( 1998 ), 5857 – 5864.en_US
dc.identifier.citedreferenceJ.D. Thompson, T.J. Gibson, F. Plewniak, F. Jeanmougin, D.G. Higgins, The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res., 25,( 1997 ), 4876 – 4882.en_US
dc.identifier.citedreferenceL. Goodstadt, C.P. Ponting, CHROMA: consensus-based colouring of multiple alignments for publication. Bioinformatics, 17,( 2001 ), 845 – 846.en_US
dc.identifier.citedreferenceL. Ringrose, R. Paro, Epigenetic regulation of cellular memory by the Polycomb and Trithorax group proteins. Annu. Rev. Genet., 38,( 2004 ), 413 – 443.en_US
dc.identifier.citedreferenceF. Bantignies, G. Cavalli, Cellular memory and dynamic regulation of polycomb group proteins. Curr. Opin. Cell Biol., 18,( 2006 ), 275 – 283.en_US
dc.identifier.citedreferenceE.B. Lewis, A gene complex controlling segmentation in Drosophila. Nature, 276,( 1978 ), 565 – 570.en_US
dc.identifier.citedreferenceY.B. Schwartz, V. Pirrotta, Polycomb silencing mechanisms and the management of genomic programmes. Nat. Rev. Genet., 8,( 2007 ), 9 – 22.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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