Poly(ADP-ribose) polymerase 1 is inhibited by a histone H2A variant, macroH2A, and contributes to silencing of the inactive X chromosome

Journal of Biological Chemistry

Volumn 282, Issue 17, 2007, Pages 12851-12859

  Nusinow, Dmitri A ^a   Hernández Muñoz, Inmaculada ^b   Fazzio, Thomas G ^a   Shah, Girish M ^c   Kraus, W Lee ^d   Panning, Barbara ^a,e  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b INST MUNIC D INVESTIGACIO MEDICA   (Spain)

^c LAVAL UNIVERSITY   (Canada)

^d Department of Obstetrics Gynecology   (United States)

^e UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHROMOSOMES; DEGRADATION; DNA SEQUENCES; ENZYME ACTIVITY; GENE EXPRESSION; PROTEINS;

CHROMATIN STRUCTURE; DNA DAMAGE; HETEROCHROMATIN; HISTONE;

ENZYME INHIBITION;

HISTONE H2A; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; HISTONE; MACROH2A HISTONE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PARP1 PROTEIN, HUMAN; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CHROMATIN STRUCTURE; CHROMOSOME INACTIVATION; CONTROLLED STUDY; EMBRYO; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; GENE SILENCING; HETEROCHROMATIN; HUMAN; HUMAN CELL; IN VITRO STUDY; IN VIVO STUDY; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN FUNCTION; REPORTER GENE; RNA INTERFERENCE; X CHROMOSOME; CELL LINE; CHROMATIN; CHROMATIN ASSEMBLY AND DISASSEMBLY; ENZYMOLOGY; GENETICS; METABOLISM; PHYSIOLOGY; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; X CHROMOSOME INACTIVATION;

VERTEBRATA;

CELL LINE; CHROMATIN; CHROMATIN ASSEMBLY AND DISASSEMBLY; GENE SILENCING; HISTONES; POLY(ADP-RIBOSE) POLYMERASES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; X CHROMOSOME INACTIVATION;

EID: 34250359929     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M610502200     Document Type: Article

References (35)

1. Kornberg, R. D., and Lorch, Y. (1999) Cell 98, 285-294
2. Jenuwein, T., and Allis, C. D. (2001) Science 293, 1074-1080
3. Kim, M. Y., Mauro, S., Gevry, N., Lis, J. T., and Kraus, W. L. (2004) Cell 119, 803-814
4. Kim, M. Y., Zhang, T., and Kraus, W. L. (2005) Genes Dev. 19, 1951-1967
5. Ame, J. C., Spenlehauer, C., and de Murcia, G. (2004) BioEssays 26, 882-893
6. Rouleau, M., Aubin, R. A., and Poirier, G. G. (2004) J. Cell Sci. 117, 815-825
7. Hassa, P. O., Haenni, S. S., Elser, M., and Hottiger, M. O. (2006) Microbiol. Mol. Biol. Rev. 70, 789-829
8. Tulin, A., Stewart, D., and Spradling, A. C. (2002) Genes Dev. 16, 2108-2119
9. Pehrson, J. R., and Fried, V. A. (1992) Science 257, 1398-1400
10. Martzen, M. R., McCraith, S. M., Spinelli, S. L., Torres, F. M., Fields, S., Grayhack, E. J., and Phizicky, E. M. (1999) Science 286, 1153-1155
11. Karras, G. I., Kustatscher, G., Buhecha, H. R., Allen, M. D., Pugieux, C., Sait, F., Bycroft, M., and Ladurner, A. G. (2005) EMBO J. 24, 1911-1920
12. Kustatscher, G., Hothorn, M., Pugieux, C., Scheffzek, K., and Ladurner, A. G. (2005) Nat. Struct. Mol. Biol. 12, 624-625
13. Costanzi, C., and Pehrson, J. R. (1998) Nature 393, 599-601
14. Chadwick, B. P., and Willard, H. F. (2001) Hum. Mol. Genet. 10, 1101-1113
15. Costanzi, C., and Pehrson, J. R. (2001) J. Biol. Chem. 276, 21776-21784
16. Zhang, R., Poustovoitov, M. V., Ye, X., Santos, H. A., Chen, W., Daganzo, S. M., Erzberger, J. P., Serebriiskii, I. G., Canutescu, A. A., Dunbrack, R. L., Pehrson, J. R., Berger, J. M., Kaufman, P. D., and Adams, P. D. (2005) Dev. Cell 8, 19-30
17. Changolkar, L. N., and Pehrson, J. R. (2006) Mol. Cell. Biol. 26, 4410-4420
18. Hernandez-Munoz, I., Lund, A. H., van der Stoop, P., Boutsma, E., Muijrers, I., Verhoeven, E., Nusinow, D. A., Panning, B., Marahrens, Y., and van Lohuizen, M. (2005) Proc. Natl. Acad. Sci. U. S. A. 102, 7635-7640
19. Agelopoulos, M., and Thanos, D. (2006) EMBO J. 25, 4843-4853
20. Angelov, D., Molla, A., Perche, P. Y., Hans, F., Cote, J., Khochbin, S., Bouvet, P., and Dimitrov, S. (2003) Mol. Cell 11, 1033-1041
21. Perche, P. Y., Vourc'h, C., Konecny, L., Souchier, C., Robert-Nicoud, M., Dimitrov, S., and Khochbin, S. (2000) Curr. Biol. 10, 1531-1534
22. Chakravarthy, S., Gundimella, S. K., Caron, C., Perche, P. Y., Pehrson, J. R., Khochbin, S., and Luger, K. (2005) Mol. Cell. Biol. 25, 7616-7624
23. Doyen, C. M., An, W., Angelov, D., Bondarenko, V., Mietton, F., Studitsky, V. M., Hamiche, A., Roeder, R. G., Bouvet, P., and Dimitrov, S. (2006) Mol. Cell. Biol. 26, 1156-1164
24. Chu, F., Nusinow, D. A., Chalkley, R. J., Plath, K., Panning, B., and Burlingame, A. L. (2006) Mol. Cell. Proteomics 5, 194-203
25. Pasini, D., Bracken, A. P., Jensen, M. R., Lazzerini Denchi, E., and Helin, K. (2004) EMBO J. 23, 4061-4071
26. Plath, K., Fang, J., Mlynarczyk-Evans, S. K., Cao, R., Worringer, K. A., Wang, H., de la Cruz, C. C., Otte, A. P., Panning, B., and Zhang, Y. (2003) Science 300, 131-135
27. Brummelkamp, T. R., Bernards, R., and Agami, R. (2002) Science 296, 550-553
28. Sui, G., Soohoo, C., Affar el, B., Gay, F., Shi, Y., and Forrester, W. C. (2002) Proc. Natl. Acad. Sci. U. S. A. 99, 5515-5520
29. Shah, R. G., Ghodgaonkar, M. M., Affar el, B., and Shah, G. M. (2005) Biochem. Biophys. Res. Commun. 331, 167-174
30. Chadwick, B. P., Valley, C. M., and Willard, H. F. (2001) Nucleic Acids Res. 29, 2699-2705
31. Csankovszki, G., Nagy, A., and Jaenisch, R. (2001) J. Cell Biol. 153, 773-784
32. Ouararhni, K., Hadj-Slimane, R., Ait-Si-Ali, S., Robin, P., Mietton, F., Harel-Bellan, A., Dimitrov, S., and Hamiche, A. (2006) Genes Dev. 20, 3324-3336
33. Menissier de Murcia, J., Ricoul, M., Tartier, L., Niedergang, C., Huber, A., Dantzer, F., Schreiber, V., Ame, J. C., Dierich, A., LeMeur, M., Sabatier, L., Chambon, P., and de Murcia, G. (2003) EMBO J. 22, 2255-2263
34. D'Amours, D., Desnoyers, S., D'Silva, I., and Poirier, G. G. (1999) Biochem. J. 342, 249-268
35. Aguiar, R. C., Takeyama, K., He, C., Kreinbrink, K., and Shipp, M. (2005) J. Biol. Chem. 280, 33756-33765