The N-terminal domain determines the affinity and specificity of H1 binding to chromatin

Biochemical and Biophysical Research Communications

Volumn 420, Issue 2, 2012, Pages 321-324

  öberg, Christine ^a   Belikov, Sergey ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Chromatin; Histone H1; Histone H1 N terminal domain; Linker histone; Xenopus oocytes

Indexed keywords

HISTONE H1; MESSENGER RNA;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; BINDING SITE; CHROMATIN ASSEMBLY AND DISASSEMBLY; CHROMATIN STRUCTURE; CONTROLLED STUDY; ENZYME SPECIFICITY; HETEROLOGOUS EXPRESSION; IN VIVO STUDY; NONHUMAN; NUCLEOTIDE SEQUENCE; OOCYTE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN INTERACTION; WILD TYPE; XENOPUS;

AMINO ACID SEQUENCE; ANIMALS; CHROMATIN; HISTONES; HUMANS; MOLECULAR SEQUENCE DATA; OOCYTES; PROTEIN STRUCTURE, TERTIARY; SEQUENCE DELETION; XENOPUS LAEVIS;

EUKARYOTA; HELICOBACTER HEILMANNII TYPE 1;

EID: 84859425800     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2012.02.157     Document Type: Article

References (24)

1. Routh A., Sandin S., Rhodes D. Nucleosome repeat length and linker histone stoichiometry determine chromatin fiber structure. Proc. Natl. Acad. Sci. USA 2008, 105:8872-8877.
2. Fan Y., Nikitina T., Morin-Kensicki E.M., Zhao J., Magnuson T.R., Woodcock C.L., Skoultchi A.I. H1 linker histones are essential for mouse development and affect nucleosome spacing in vivo. Mol. Cell. Biol. 2003, 23:4559-4572.
3. Allan J., Hartman P.G., Crane-Robinson C., Aviles F.X. The structure of histone H1 and its location in chromatin. Nature 1980, 288:675-679.
4. Izzo A., Kamieniarz K., Schneider R. The histone H1 family: specific members, specific functions?. Biol. Chem. 2008, 389:333-343.
5. Hendzel M.J., Lever M.A., Crawford E., Th'ng J.P. The C-terminal domain is the primary determinant of histone H1 binding to chromatin in vivo. J. Biol. Chem. 2004, 279:20028-20034.
6. Caterino T.L., Hayes J.J. Structure of the H1 C-terminal domain and function in chromatin condensation. Biochem. Cell. Biol. 2011, 89:35-44.
7. Lee L.Y., Liang X., Hook M., Brown E.L. Identification and characterization of the C3 binding domain of the Staphylococcus aureus extracellular fibrinogen-binding protein (Efb). J. Biol. Chem. 2004, 279:50710-50716.
8. Almouzni G., Wolffe A.P. Replication-coupled chromatin assembly is required for the repression of basal transcription in vivo. Genes Dev. 1993, 7:2033-2047.
9. Hock R., Moorman A., Fischer D., Scheer U. Absence of somatic histone H1 in oocytes and preblastula embryos of Xenopus laevis. Dev. Biol. 1993, 158:510-522.
10. Dimitrov S., Almouzni G., Dasso M., Wolffe A.P. Chromatin transitions during early Xenopus embryogenesis: changes in histone H4 acetylation and in linker histone type. Dev. Biol. 1993, 160:214-227.
11. Belikov S., Astrand C., Wrange O. Mechanism of histone H1-stimulated glucocorticoid receptor DNA binding in vivo. Mol. Cell. Biol. 2007, 27:2398-2410.
12. Zernicka-Goetz M., Pines J., Ryan K., Siemering K.R., Haseloff J., Evans M.J., Gurdon J.B. An indelible lineage marker for Xenopus using a mutated green fluorescent protein. Development 1996, 122:3719-3724.
13. Astrand C., Belikov S., Wrange O. Histone acetylation characterizes chromatin presetting by NF1 and Oct1 and enhances glucocorticoid receptor binding to the MMTV promoter. Exp. Cell Res. 2009, 315:2604-2615.
14. Belikov S., Astrand C., Wrange O. FoxA1 binding directs chromatin structure and the functional response of a glucocorticoid receptor-regulated promoter. Mol. Cell. Biol. 2009, 29:5413-5425.
15. Fyodorov D.V., Kadonaga J.T. Chromatin assembly in vitro with purified recombinant ACF and NAP-1. Methods Enzymol. 2003, 371:499-515.
16. Allan J., Mitchell T., Harborne N., Bohm L., Crane-Robinson C. Roles of H1 domains in determining higher order chromatin structure and H1 location. J. Mol. Biol. 1986, 187:591-601.
17. P. Vyas, D.T. Brown, The N- and C-terminal domains determine the differential nucleosomal binding geometry and affinity of linker histone isotypes H10 and H1C, J. Biol. Chem. (2012), in press.
18. Bohm L., Mitchell T.C. Sequence conservation in the N-terminal domain of histone H1. FEBS Lett. 1985, 193:1-4.
19. Lu X., Hansen J.C. Identification of specific functional subdomains within the linker histone H10 C-terminal domain. J. Biol. Chem. 2004, 279:8701-8707.
20. Lu X., Hamkalo B., Parseghian M.H., Hansen J.C. Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder. Biochemistry 2009, 48:164-172.
21. Stasevich T.J., Mueller F., Brown D.T., McNally J.G. Dissecting the binding mechanism of the linker histone in live cells: an integrated FRAP analysis. EMBO J. 2010, 29:1225-1234.
22. George E.M., Izard T., Anderson S.D., Brown D.T. Nucleosome interaction surface of linker histone H1c is distinct from that of H1(0). J. Biol. Chem. 2010, 285:20891-20896.
23. Th'ng J.P., Sung R., Ye M., Hendzel M.J. H1 family histones in the nucleus, Control of binding and localization by the C-terminal domain. J. Biol. Chem. 2005, 280:27809-27814.
24. Clausell J., Happel N., Hale T.K., Doenecke D., Beato M. Histone H1 subtypes differentially modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNF or NURF. PLoS One 2009, 4:e0007243.