Light-induced nuclear export reveals rapid dynamics of epigenetic modifications

Nature Chemical Biology

Volumn 12, Issue 6, 2016, Pages 399-401

  Yumerefendi, Hayretin ^a   Lerner, Andrew Michael ^a   Zimmerman, Seth Parker ^a   Hahn, Klaus ^a,b   Bear, James E ^a,b   Strahl, Brian D ^a,b   Kuhlman, Brian ^a,b  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

HISTONE H2B; PHOTOTROPIN; PHOTOTROPIN 1; UNCLASSIFIED DRUG; BRE1 PROTEIN, S CEREVISIAE; FLAVOPROTEIN; HISTONE; NUCLEAR EXPORT SIGNAL; SACCHAROMYCES CEREVISIAE PROTEIN; UBIQUITIN;

ARTICLE; CELLULAR DISTRIBUTION; CHROMATIN ASSEMBLY AND DISASSEMBLY; EMBEDDING; EPIGENETICS; GENETIC TRANSCRIPTION; HISTONE MODIFICATION; LIGHT INDUCIBLE NUCLEAR EXPORTER; NUCLEAR EXPORT SIGNAL; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN METABOLISM; UBIQUITINATION; CELL NUCLEUS; CHEMISTRY; CYTOLOGY; GENETIC EPIGENESIS; GENETICS; LIGHT; METABOLISM; PROTEIN DOMAIN; PROTEIN TRANSPORT; RADIATION RESPONSE; SACCHAROMYCES CEREVISIAE;

CELL NUCLEUS; EPIGENESIS, GENETIC; FLAVOPROTEINS; HISTONES; LIGHT; NUCLEAR EXPORT SIGNALS; PHOTOTROPINS; PROTEIN DOMAINS; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; UBIQUITIN; UBIQUITINATION;

EID: 84964329325     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.2068     Document Type: Article

References (23)

1. Tischer, D., Weiner, O.D. Nat. Rev. Mol. Cell Biol. 15, 551-558 (2014).
2. Yang, X., Jost, A.P.-T., Weiner, O.D., Tang, C. Mol. Biol. Cell 24, 2419-2430 (2013).
3. Gautier, A. et al. J. Am. Chem. Soc. 132, 4086-4088 (2010).
4. Yumerefendi, H. et al. PLoS One 10, e0128443 (2015).
5. Niopek, D. et al. Nat. Comm. 5, 4404 (2014).
6. Harper, S.M., Neil, L.C., Gardner, K.H. Science 301, 1541-1544 (2003).
7. Zayner, J.P., Antoniou, C., Sosnick, T.R. J. Mol. Biol. 419, 61-74 (2012).
8. Hutten, S., Kehlenbach, R.H. Trends Cell Biol. 17, 193-201 (2007).
9. Güttler, T. et al. Nat. Struct. Mol. Biol. 17, 1367-1376 (2010).
10. Hodel, M.R., Corbett, A.H., Hodel, A.E. J. Biol. Chem. 276, 1317-1325 (2001).
11. Guntas, G. et al. Proc. Natl. Acad. Sci. USA 112, 112-117 (2015).
12. Hodel, A.E. et al. J. Biol. Chem. 281, 23545-23556 (2006).
13. Xiao, T. et al. Mol. Cell. Biol. 25, 637-651 (2005).
14. Fuchs, G., Hollander, D., Voichek, Y., Ast, G., Oren, M. Genome Res. 24, 1572-1583 (2014).
15. Henry, K.W. et al. Genes Dev. 17, 2648-2663 (2003).
16. Kosugi, S., Hasebe, M., Tomita, M., Yanagawa, H. Proc. Natl. Acad. Sci. USA 106, 10171-10176 (2009).
17. Sun, Z.-W., Allis, C.D. Nature 418, 104-108 (2002).
18. Briggs, S.D. et al. Nature 418, 498 (2002).
19. Huang, F. et al. J. Biol. Chem. http://dx.doi.org/10.1074/jbc.M115.693085 (2015).
20. Katan-Khaykovich, Y., Struhl, K. EMBO J. 24, 2138-2149 (2005).
21. Cai, L., Makhov, A.M., Schafer, D.A., Bear, J.E. Cell 134, 828-842 (2008).
22. Hallett, R.A., Zimmerman, S.P., Yumerefendi, H., Bear, J.E., Kuhlman, B. ACS Synth. Biol. 5, 53-64 (2016).
23. Gietz, R.D., Schiestl, R.H. Nat. Protoc. 2, 35-37 (2007).