Human SFMBT is a transcriptional repressor protein that selectively binds the N‐terminal tail of histone H3
dc.contributor.author | Wu, Shumin | en_US |
dc.contributor.author | Trievel, Raymond C. | en_US |
dc.contributor.author | Rice, Judd C. | en_US |
dc.date.accessioned | 2016-01-04T20:51:34Z | |
dc.date.available | 2016-01-04T20:51:34Z | |
dc.date.issued | 2007-07-10 | en_US |
dc.identifier.citation | Wu, 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.issn | 0014-5793 | en_US |
dc.identifier.issn | 1873-3468 | en_US |
dc.identifier.uri | https://hdl.handle.net/2027.42/116313 | |
dc.publisher | Wiley Periodicals, Inc. | en_US |
dc.subject.other | SAM | en_US |
dc.subject.other | sterile alpha motif | en_US |
dc.subject.other | L(3)MBT | en_US |
dc.subject.other | lethal (3) malignant brain tumor | en_US |
dc.subject.other | SCML2 | en_US |
dc.subject.other | sex comb on midleg-like 2 | en_US |
dc.subject.other | PcG | en_US |
dc.subject.other | SFMBT | en_US |
dc.subject.other | Polycomb | en_US |
dc.subject.other | Transcription | en_US |
dc.subject.other | Chromatin | en_US |
dc.subject.other | Histone H3 | en_US |
dc.subject.other | polycomb | en_US |
dc.subject.other | SFMBT | en_US |
dc.subject.other | Scm-related gene containing four mbt domains | en_US |
dc.subject.other | dSfmbt | en_US |
dc.subject.other | Drosophila SFMBT | en_US |
dc.subject.other | hSFMBT | en_US |
dc.subject.other | human SFMBT | en_US |
dc.subject.other | MBT | en_US |
dc.subject.other | malignant brain tumor | en_US |
dc.title | Human SFMBT is a transcriptional repressor protein that selectively binds the N‐terminal tail of histone H3 | en_US |
dc.type | Article | en_US |
dc.rights.robots | IndexNoFollow | en_US |
dc.subject.hlbsecondlevel | Biological Chemistry | en_US |
dc.subject.hlbtoplevel | Science | en_US |
dc.description.peerreviewed | Peer Reviewed | en_US |
dc.contributor.affiliationum | University of Michigan, Department of Biological Chemistry, Ann Arbor, MI 48109-0606, United States | en_US |
dc.contributor.affiliationother | University 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 States | en_US |
dc.description.bitstreamurl | http://deepblue.lib.umich.edu/bitstream/2027.42/116313/1/feb2s0014579307006746.pdf | |
dc.identifier.doi | 10.1016/j.febslet.2007.06.025 | en_US |
dc.identifier.source | FEBS Letters | en_US |
dc.identifier.citedreference | W.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.citedreference | J.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.citedreference | T. 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.citedreference | H. 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.citedreference | D. 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.citedreference | E. 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.citedreference | J. 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.citedreference | A. 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.citedreference | J.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.citedreference | J. 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.citedreference | P. Webb, Estrogen receptor activation function 1 works by binding p160 coactivator proteins. Mol. Endocrinol., 12,( 1998 ), 1605 – 1618. | en_US |
dc.identifier.citedreference | H.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.citedreference | S.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.citedreference | J.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.citedreference | S.Y. Huang, W.T. Garrard, Electrophoretic analyses of nucleosomes and other protein–DNA complexes. Methods Enzymol., 170,( 1989 ), 116 – 142. | en_US |
dc.identifier.citedreference | D.A. Jackson, P.R. Cook, Transcription occurs at a nucleoskeleton. Embo J., 4,( 1985 ), 919 – 925. | en_US |
dc.identifier.citedreference | A. Thiru, Structural basis of HP1/PXVXL motif peptide interactions and HP1 localisation to heterochromatin. Embo J., 23,( 2004 ), 489 – 499. | en_US |
dc.identifier.citedreference | D.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.citedreference | D. 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.citedreference | J.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.citedreference | T. 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.citedreference | I. 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.citedreference | W. 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.citedreference | S.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.citedreference | J. 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.citedreference | V.G. Wilson, D. Rangasamy, Intracellular targeting of proteins by sumoylation. Exp. Cell Res., 271,( 2001 ), 57 – 65. | en_US |
dc.identifier.citedreference | R. 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.citedreference | J.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.citedreference | T.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.citedreference | W. 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.citedreference | D.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.citedreference | J.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.citedreference | S. 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.citedreference | M.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.citedreference | J. 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.citedreference | J. 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.citedreference | J.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.citedreference | L. Goodstadt, C.P. Ponting, CHROMA: consensus-based colouring of multiple alignments for publication. Bioinformatics, 17,( 2001 ), 845 – 846. | en_US |
dc.identifier.citedreference | L. 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.citedreference | F. Bantignies, G. Cavalli, Cellular memory and dynamic regulation of polycomb group proteins. Curr. Opin. Cell Biol., 18,( 2006 ), 275 – 283. | en_US |
dc.identifier.citedreference | E.B. Lewis, A gene complex controlling segmentation in Drosophila. Nature, 276,( 1978 ), 565 – 570. | en_US |
dc.identifier.citedreference | Y.B. Schwartz, V. Pirrotta, Polycomb silencing mechanisms and the management of genomic programmes. Nat. Rev. Genet., 8,( 2007 ), 9 – 22. | en_US |
dc.owningcollname | Interdisciplinary and Peer-Reviewed |
Files in this item
Remediation of Harmful Language
The University of Michigan Library aims to describe library materials in a way that respects the people and communities who create, use, and are represented in our collections. Report harmful or offensive language in catalog records, finding aids, or elsewhere in our collections anonymously through our metadata feedback form. More information at Remediation of Harmful Language.
Accessibility
If you are unable to use this file in its current format, please select the Contact Us link and we can modify it to make it more accessible to you.