Drosophila H1 regulates the genetic activity of heterochromatin by recruitment of Su(var)3-9

Science

Volumn 340, Issue 6128, 2013, Pages 78-81

  Lu, Xingwu ^a   Wontakal, Sandeep N ^a   Kavi, Harsh ^a   Kim, Byung Ju ^a   Guzzardo, Paloma M ^b   Emelyanov, Alexander V ^a   Xu, Na ^a   Hannon, Gregory J ^b   Zavadil, Jiri ^c,d   Fyodorov, Dmitry V ^a   Skoultchi, Arthur I ^a  

^a ALBERT EINSTEIN COLLEGE OF MEDICINE   (United States)

^b Howard Hughes Medical Institute Cold Spring Harbor Laboratory Cold Spring Harbor   (United States)

^c NEW YORK UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d INTERNATIONAL AGENCY FOR RESEARCH ON CANCER   (France)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H1; HISTONE H3; HISTONE H3 LYSINE 9 METHYLTRANSFERASE SU(VAR)3-9; HISTONE METHYLTRANSFERASE; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; DROSOPHILA PROTEIN; HISTONE; MUSCLE PROTEIN; NAUTILUS PROTEIN, DROSOPHILA; REPRESSOR PROTEIN; SUPPRESSOR OF VARIEGATION 3 9 PROTEIN, DROSOPHILA; SUPPRESSOR OF VARIEGATION 3-9 PROTEIN, DROSOPHILA; TRANSCRIPTION FACTOR;

EUKARYOTE; GENETIC VARIATION; METHYLATION; PROTEIN; RNA;

ANIMAL EXPERIMENT; ARTICLE; CHROMATIN ASSEMBLY AND DISASSEMBLY; CONTROLLED STUDY; DROSOPHILA; GENE EXPRESSION; GENE REPRESSION; GENETIC REGULATION; HETEROCHROMATIN; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA INTERFERENCE; ANIMAL; DROSOPHILA MELANOGASTER; GENE SILENCING; GENETICS; METABOLISM; NUCLEOTIDE REPEAT;

ANIMALS; DROSOPHILA MELANOGASTER; DROSOPHILA PROTEINS; GENE SILENCING; HETEROCHROMATIN; HISTONES; MUSCLE PROTEINS; REPETITIVE SEQUENCES, NUCLEIC ACID; REPRESSOR PROTEINS; RNA INTERFERENCE; TRANSCRIPTION FACTORS;

MLCS; MLOWN;

EID: 84876337753     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.1234654     Document Type: Article

References (25)

1. A. P. Wolffe, Chromatin: Structure and Function (Academic Press, San Diego, 1995).
2. S. C. Elgin, S. I. Grewal, Curr. Biol. 13, R895 (2003).
3. J. C. Eissenberg, G. Reuter, Int. Rev. Cell. Mol. Biol. 273, 1 (2009).
4. X. Lu et al., Genes Dev. 23, 452 (2009).
5. O. Vujatovic et al., Nucleic Acids Res. 40, 5402 (2012).
6. J. S. Khurana, W. Theurkauf, J. Cell Biol. 191, 905 (2010).
7. C. D. Malone, G. J. Hannon, Cell 136, 656 (2009).
8. B. Czech, G. J. Hannon, Nat. Rev. Genet. 12, 19 (2011).
9. M. Ghildiyal, P. D. Zamore, Nat. Rev. Genet. 10, 94 (2009).
10. C. M. Bergman, H. Quesneville, D. Anxolabéhère, M. Ashburner, Genome Biol. 7, R112 (2006).
11. P. Dimitri, Genetica 100, 85 (1997).
12. J. S. Kaminker et al., Genome Biol. 3, RESEARCH0084 (2002).
13. K. J. Livak, Genetics 124, 303 (1990).
14. R. N. Kotelnikov et al., Nucleic Acids Res. 37, 3254 (2009).
15. A. A. Aravin et al., Curr. Biol. 11, 1017 (2001).
16. T. Jenuwein, Trends Cell Biol. 11, 266 (2001).
17. S. Daujat, U. Zeissler, T. Waldmann, N. Happel, R. Schneider, J. Biol. Chem. 280, 38090 (2005).
18. A. L. Nielsen et al., Mol. Cell 7, 729 (2001).
19. P. Trojer et al., J. Biol. Chem. 284, 8395 (2009).
20. A. Ebert, S. Lein, G. Schotta, G. Reuter, Chromosome Res. 14, 377 (2006).
21. T. K. Hale, A. Contreras, A. J. Morrison, R. E. Herrera, Mol. Cell 22, 693 (2006).
22. S. A. Grigoryev, K. S. Spirin, I. A. Krasheninnikov, Nucleic Acids Res. 18, 7397 (1990).
23. R. T. Kamakaka, J. O. Thomas, EMBO J. 9, 3997 (1990).
24. H. Weintraub, Cell 38, 17 (1984).
25. X. Lu, S. Liu, T. B. Kornberg, Genes Dev. 20, 2539 (2006).