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Volumn 22, Issue 22, 2002, Pages 7868-7876

Role for the mortality factors MORF4, MRGX, and MRG15 in transcriptional repression via associations with Pf1, mSin3A, and transducin-like enhancer of split

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE DEACETYLASE; LUCIFERASE; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR; TRANSDUCIN; ZINC FINGER PROTEIN;

EID: 0036841723     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.22.22.7868-7876.2002     Document Type: Article
Times cited : (81)

References (49)
  • 1
    • 0034254857 scopus 로고    scopus 로고
    • NuRD and SIN3 histone deacetylase complexes in development
    • Ahringer, J. 2000. NuRD and SIN3 histone deacetylase complexes in development. Trends Genet. 16:351-356.
    • (2000) Trends Genet. , vol.16 , pp. 351-356
    • Ahringer, J.1
  • 2
    • 0034699391 scopus 로고    scopus 로고
    • Chromodomains are protein-RNA interaction modules
    • Akhtar, A., D. Zink, and P. B. Becker. 2000. Chromodomains are protein-RNA interaction modules . Nature 407:405-409.
    • (2000) Nature , vol.407 , pp. 405-409
    • Akhtar, A.1    Zink, D.2    Becker, P.B.3
  • 4
    • 0032940072 scopus 로고    scopus 로고
    • Histone deacetylases: Transcriptional repression with SINers and NuRDs
    • Ayer, D. E. 1999. Histone deacetylases: Transcriptional repression with SINers and NuRDs. Trends Cell Biol. 9:193-198.
    • (1999) Trends Cell Biol. , vol.9 , pp. 193-198
    • Ayer, D.E.1
  • 6
    • 0028905563 scopus 로고
    • Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3
    • Ayer, D. E., Q. A. Lawrence, and R. N. Eisenman. 1995. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell 80:767-776.
    • (1995) Cell , vol.80 , pp. 767-776
    • Ayer, D.E.1    Lawrence, Q.A.2    Eisenman, R.N.3
  • 8
    • 0035925659 scopus 로고    scopus 로고
    • Conservation of the MORF4 related gene family: Identification of a new chromo domain subfamily and novel protein motif
    • Bertram, M. J., and O. M. Pereira-Smith. 2001. Conservation of the MORF4 related gene family: Identification of a new chromo domain subfamily and novel protein motif. Gene 266:111-121.
    • (2001) Gene , vol.266 , pp. 111-121
    • Bertram, M.J.1    Pereira-Smith, O.M.2
  • 9
    • 0035883746 scopus 로고    scopus 로고
    • The Swi5 activator recruits the Mediator complex to the HO promoter without RNA polymerase II
    • Bhoite, L. T., Y. Yu, and D. J. Stillman. 2001. The Swi5 activator recruits the Mediator complex to the HO promoter without RNA polymerase II. Genes Dev. 15:2457-2469.
    • (2001) Genes Dev. , vol.15 , pp. 2457-2469
    • Bhoite, L.T.1    Yu, Y.2    Stillman, D.J.3
  • 10
    • 0033579566 scopus 로고    scopus 로고
    • Mlx, a novel max-like BHLHZip protein that interacts with the max network of transcription factors
    • Billin, A. N., A. L. Eilers, C. Queva, and D. E. Ayer. 1999. Mlx, a novel max-like BHLHZip protein that interacts with the max network of transcription factors. J. Biol. Chem. 274:36344-36350.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36344-36350
    • Billin, A.N.1    Eilers, A.L.2    Queva, C.3    Ayer, D.E.4
  • 11
    • 0035312290 scopus 로고    scopus 로고
    • All Tcf HMG box transcription factors interact with Groucho-related co-repressors
    • Brantjes, H., J. Roose, M. van De Wetering, and H. Clevers. 2001. All Tcf HMG box transcription factors interact with Groucho-related co-repressors. Nucleic Acids Res. 29:1410-1419.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1410-1419
    • Brantjes, H.1    Roose, J.2    Van De Wetering, M.3    Clevers, H.4
  • 12
    • 0032484989 scopus 로고    scopus 로고
    • Retinoblastoma protein recruits histone deacetylase to repress transcription
    • Brehm, A., E. A. Miska, D. J. McCance, J. L. Reid, A. J. Bannister, and T. Kouzarides. 1998. Retinoblastoma protein recruits histone deacetylase to repress transcription. Nature 391:597-601.
    • (1998) Nature , vol.391 , pp. 597-601
    • Brehm, A.1    Miska, E.A.2    McCance, D.J.3    Reid, J.L.4    Bannister, A.J.5    Kouzarides, T.6
  • 14
    • 0034673929 scopus 로고    scopus 로고
    • Groucho/TLE family proteins and transcriptional repression
    • Chen, G., and A. J. Courey. 2000. Groucho/TLE family proteins and transcriptional repression. Gene 249:1-16.
    • (2000) Gene , vol.249 , pp. 1-16
    • Chen, G.1    Courey, A.J.2
  • 15
    • 0033200392 scopus 로고    scopus 로고
    • A functional interaction between the histone deacetylase Rpd3 and the corepressor groucho in Drosophila development
    • Chen, G., J. Fernandez, S. Mische, and A. J. Courey. 1999. A functional interaction between the histone deacetylase Rpd3 and the corepressor groucho in Drosophila development. Genes Dev. 13:2218-2230.
    • (1999) Genes Dev. , vol.13 , pp. 2218-2230
    • Chen, G.1    Fernandez, J.2    Mische, S.3    Courey, A.J.4
  • 16
    • 0031785159 scopus 로고    scopus 로고
    • A role for Groucho tetramerization in transcriptional repression
    • Chen, G., P. H. Nguyen, and A. J. Courey. 1998. A role for Groucho tetramerization in transcriptional repression. Mol. Cell. Biol. 18:7259-7268.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7259-7268
    • Chen, G.1    Nguyen, P.H.2    Courey, A.J.3
  • 17
    • 0000782017 scopus 로고    scopus 로고
    • The homeodomain protein NK-3 recruits Groucho and a histone deacetylase complex to repress transcription
    • Choi, C. Y., Y. H. Kim, H. J. Kwon, and Y. Kim. 1999. The homeodomain protein NK-3 recruits Groucho and a histone deacetylase complex to repress transcription. J. Biol. Chem. 274:33194-33197.
    • (1999) J. Biol. Chem. , vol.274 , pp. 33194-33197
    • Choi, C.Y.1    Kim, Y.H.2    Kwon, H.J.3    Kim, Y.4
  • 18
    • 0035499392 scopus 로고    scopus 로고
    • Transcriptional repression: The long and the short of it
    • Courey, A. J., and S. Jia. 2001. Transcriptional repression: The long and the short of it. Genes Dev. 15:2786-2796.
    • (2001) Genes Dev. , vol.15 , pp. 2786-2796
    • Courey, A.J.1    Jia, S.2
  • 19
    • 0035576879 scopus 로고    scopus 로고
    • Temporal regulation of a paired-like homeodomain repressor/TLE corepressor complex and a related activator is required for pituitary organogenesis
    • Dasen, J. S., J. P. Barbera, T. S. Herman, S. O. Connell, L. Olson, B. Ju, J. Tollkuhn, S. H. Baek, D. W. Rose, and M. G. Rosenfeld. 2001. Temporal regulation of a paired-like homeodomain repressor/TLE corepressor complex and a related activator is required for pituitary organogenesis. Genes Dev. 15:3193-3207.
    • (2001) Genes Dev. , vol.15 , pp. 3193-3207
    • Dasen, J.S.1    Barbera, J.P.2    Herman, T.S.3    Connell, S.O.4    Olson, L.5    Ju, B.6    Tollkuhn, J.7    Baek, S.H.8    Rose, D.W.9    Rosenfeld, M.G.10
  • 20
    • 0032168984 scopus 로고    scopus 로고
    • The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase
    • Ferreira, R., L. Magnaghi-Jaulin, P. Robin, A. Harel-Bellan, and D. Trouche. 1998. The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase. Proc Natl. Acad. Sci. USA 95:10493-10498.
    • (1998) Proc Natl. Acad. Sci. USA , vol.95 , pp. 10493-10498
    • Ferreira, R.1    Magnaghi-Jaulin, L.2    Robin, P.3    Harel-Bellan, A.4    Trouche, D.5
  • 23
    • 0030798245 scopus 로고    scopus 로고
    • Histone acetylation in chromatin structure and transcription
    • Grunstein, M. 1997. Histone acetylation in chromatin structure and transcription. Nature 389:349-352.
    • (1997) Nature , vol.389 , pp. 349-352
    • Grunstein, M.1
  • 24
    • 0031007189 scopus 로고    scopus 로고
    • Histone deacetylase activity is required for full transcriptional repression by mSin3A
    • Hassig, C. A., T. C. Fleischer, A. N. Billin, S. L. Schreiber, and D. E. Ayer. 1997. Histone deacetylase activity is required for full transcriptional repression by mSin3A. Cell 89:341-347.
    • (1997) Cell , vol.89 , pp. 341-347
    • Hassig, C.A.1    Fleischer, T.C.2    Billin, A.N.3    Schreiber, S.L.4    Ayer, D.E.5
  • 25
    • 0031244521 scopus 로고    scopus 로고
    • Nuclear histone acetylases and deacetylases and transcriptional regulation: HATs off to HDACs
    • Hassig, C. A., and S. L. Schreiber. 1997. Nuclear histone acetylases and deacetylases and transcriptional regulation: HATs off to HDACs. Curr. Opin. Chem. Biol. 1:300-308.
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 300-308
    • Hassig, C.A.1    Schreiber, S.L.2
  • 28
    • 0031865050 scopus 로고    scopus 로고
    • Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo
    • Kadosh, D., and K. Struhl. 1998. Targeted recruitment of the Sin3-Rpd3 histone deacetylase complex generates a highly localized domain of repressed chromatin in vivo. Mol. Cell. Biol. 18:5121-5127.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5121-5127
    • Kadosh, D.1    Struhl, K.2
  • 29
    • 0033601106 scopus 로고    scopus 로고
    • Sin meets NuRD and other tails of repression
    • Knoepfler, P. S., and R. N. Eisenman. 1999. Sin meets NuRD and other tails of repression. Cell 99:447-450.
    • (1999) Cell , vol.99 , pp. 447-450
    • Knoepfler, P.S.1    Eisenman, R.N.2
  • 30
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo, M. H., and C. D. Allis. 1998. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 20:615-626.
    • (1998) Bioessays , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 31
    • 0036143859 scopus 로고    scopus 로고
    • Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)
    • Kuzmichev, A., Y. Zhang, H. Erdjument-Bromage, P. Tempst, and D. Reinberg. 2002. Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1). Mol. Cell. Biol. 22:835-848.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 835-848
    • Kuzmichev, A.1    Zhang, Y.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5
  • 33
    • 0030969516 scopus 로고    scopus 로고
    • Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression
    • Laherty, C. D., W. M. Yang, J. M. Sun, J. R. Davie, E. Seto, and R. N. Eisenman. 1997. Histone deacetylases associated with the mSin3 corepressor mediate mad transcriptional repression. Cell 89:349-356.
    • (1997) Cell , vol.89 , pp. 349-356
    • Laherty, C.D.1    Yang, W.M.2    Sun, J.M.3    Davie, J.R.4    Seto, E.5    Eisenman, R.N.6
  • 35
    • 0032849352 scopus 로고    scopus 로고
    • RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins
    • Lai, A., J. M. Lee, W. M. Yang, J. A. DeCaprio, W. G. Kaelin, Jr., E. Seto, and P. E. Branton. 1999. RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins. Mol. Cell. Biol. 19:6632-6641.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6632-6641
    • Lai, A.1    Lee, J.M.2    Yang, W.M.3    DeCaprio, J.A.4    Kaelin W.G., Jr.5    Seto, E.6    Branton, P.E.7
  • 36
    • 0035914347 scopus 로고    scopus 로고
    • MRG15 activates the B-myb promoter through formation of a nuclear complex with the retinoblastoma protein and the novel protein PAM14
    • Leung, J. K., N. Berube, S. Venable, S. Ahmed, N. Timchenko, and O. M. Pereira-Smith. 2001. MRG15 activates the B-myb promoter through formation of a nuclear complex with the retinoblastoma protein and the novel protein PAM14. J. Biol. Chem. 276:39171-39178.
    • (2001) J. Biol. Chem. , vol.276 , pp. 39171-39178
    • Leung, J.K.1    Berube, N.2    Venable, S.3    Ahmed, S.4    Timchenko, N.5    Pereira-Smith, O.M.6
  • 38
    • 0033868471 scopus 로고    scopus 로고
    • Origin and evolution of the regulatory gene male-specific lethal-3
    • Marin, I., and B. S. Baker. 2000. Origin and evolution of the regulatory gene male-specific lethal-3. Mol. Biol. Evol. 17:1240-1250.
    • (2000) Mol. Biol. Evol. , vol.17 , pp. 1240-1250
    • Marin, I.1    Baker, B.S.2
  • 39
    • 0030720332 scopus 로고    scopus 로고
    • The Groucho/transducin-like enhancer of split transcriptional repressors interact with the genetically defined amino-terminal silencing domain of histone H3
    • Palaparti, A., A. Baratz, and S. Stifani. 1997. The Groucho/transducin-like enhancer of split transcriptional repressors interact with the genetically defined amino-terminal silencing domain of histone H3. J. Biol. Chem. 272: 26604-26610.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26604-26610
    • Palaparti, A.1    Baratz, A.2    Stifani, S.3
  • 41
    • 0032560117 scopus 로고    scopus 로고
    • Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3
    • Rundlett, S. E., A. A. Carmen, N. Suka, B. M. Turner, and M. Grunstein. 1998. Transcriptional repression by UME6 involves deacetylation of lysine 5 of histone H4 by RPD3. Nature 392:831-835.
    • (1998) Nature , vol.392 , pp. 831-835
    • Rundlett, S.E.1    Carmen, A.A.2    Suka, N.3    Turner, B.M.4    Grunstein, M.5
  • 42
    • 0028940364 scopus 로고
    • An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3
    • Schreiber-Agus, N., L. Chin, K. Chen, R. Torres, G. Rao, P. Guida, A. I. Skoultchi, and R. A. DePinho. 1995. An amino-terminal domain of Mxi1 mediates anti-Myc oncogenic activity and interacts with a homolog of the yeast transcriptional repressor SIN3. Cell 80:777-786.
    • (1995) Cell , vol.80 , pp. 777-786
    • Schreiber-Agus, N.1    Chin, L.2    Chen, K.3    Torres, R.4    Rao, G.5    Guida, P.6    Skoultchi, A.I.7    DePinho, R.A.8
  • 43
    • 0031172243 scopus 로고    scopus 로고
    • Cell growth inhibition by the Mad/Max complex through recruitment of histone deacetylase activity
    • Sommer, A., S. Hilfenhaus, A. Menkel, E. Kremmer, C. Seiser, P. Loidl, and B. Luscher. 1997. Cell growth inhibition by the Mad/Max complex through recruitment of histone deacetylase activity. Curr. Biol. 7:357-365.
    • (1997) Curr. Biol. , vol.7 , pp. 357-365
    • Sommer, A.1    Hilfenhaus, S.2    Menkel, A.3    Kremmer, E.4    Seiser, C.5    Loidl, P.6    Luscher, B.7
  • 44
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • Vojtek, A. B., S. M. Hollenberg, and J. A. Cooper. 1993. Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell 74:205-214.
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 45
    • 0025096058 scopus 로고
    • The Saccharomyces cerevisiae SIN3 gene, a negative regulator of HO, contains four paired amphipathic helix motifs
    • Wang, H., I. Clark, P. R. Nicholson, I. Herskowitz, and D. J. Stillman. 1990. The Saccharomyces cerevisiae SIN3 gene, a negative regulator of HO, contains four paired amphipathic helix motifs. Mol. Cell. Biol. 10:5927-5936.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5927-5936
    • Wang, H.1    Clark, I.2    Nicholson, P.R.3    Herskowitz, I.4    Stillman, D.J.5
  • 46
    • 0033863507 scopus 로고    scopus 로고
    • Co-repressor complexes and remodelling chromatin for repression
    • Wolffe, A. P., F. D. Urnov, and D. Guschin. 2000. Co-repressor complexes and remodelling chromatin for repression. Biochem. Soc. Trans. 28:379-386.
    • (2000) Biochem. Soc. Trans. , vol.28 , pp. 379-386
    • Wolffe, A.P.1    Urnov, F.D.2    Guschin, D.3
  • 47
    • 0032252209 scopus 로고    scopus 로고
    • NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities
    • Xue, Y., J. Wong, G. T. Moreno, M. K. Young, J. Cote, and W. Wang. 1998. NURD, a novel complex with both ATP-dependent chromatin-remodeling and histone deacetylase activities. Mol. Cell 2:851-861.
    • (1998) Mol. Cell , vol.2 , pp. 851-861
    • Xue, Y.1    Wong, J.2    Moreno, G.T.3    Young, M.K.4    Cote, J.5    Wang, W.6
  • 48
    • 0034967002 scopus 로고    scopus 로고
    • Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex
    • Yochum, G. S., and D. E. Ayer. 2001. Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex. Mol. Cell. Biol. 21:4110-4118.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4110-4118
    • Yochum, G.S.1    Ayer, D.E.2
  • 49
    • 0030916729 scopus 로고    scopus 로고
    • Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex
    • Zhang, Y., R. Iratni, H. Erdjument-Bromage, P. Tempst, and D. Reinberg. 1997. Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Cell 89:357-364.
    • (1997) Cell , vol.89 , pp. 357-364
    • Zhang, Y.1    Iratni, R.2    Erdjument-Bromage, H.3    Tempst, P.4    Reinberg, D.5


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