Regulation of Cellular Dynamics and Chromosomal Binding Site Preference of Linker Histones H1.0 and H1.X

REFERENCES

• Andrews AJ, Chen X, Zevin A, Stargell LA, Luger K. 2010. The histone chaperone Nap1 promotes nucleosome assembly by eliminating nonnucleosomal histone DNA interactions. Mol Cell 37:834–842. http://dx.doi.org/10.1016/j.molcel.2010.01.037.
   PubMed Web of Science ®Google Scholar
• Nagata K, Kawase H, Handa H, Yano K, Yamasaki M, Ishimi Y, Okuda A, Kikuchi A, Matsumoto K. 1995. Replication factor encoded by a putative oncogene, set, associated with myeloid leukemogenesis. Proc Natl Acad Sci U S A 92:4279–4283. http://dx.doi.org/10.1073/pnas.92.10.4279.
   PubMedGoogle Scholar
• Okuwaki M, Iwamatsu A, Tsujimoto M, Nagata K. 2001. Identification of nucleophosmin/B23, an acidic nucleolar protein, as a stimulatory factor for in vitro replication of adenovirus DNA complexed with viral basic core proteins. J Mol Biol 311:41–55. http://dx.doi.org/10.1006/jmbi.2001.4812.
   PubMed Web of Science ®Google Scholar
• Kato K, Okuwaki M, Nagata K. 2011. Role of template activating factor-I as a chaperone in linker histone dynamics. J Cell Sci 124:3254–3265. http://dx.doi.org/10.1242/jcs.083139.
   PubMed Web of Science ®Google Scholar
• Gadad SS, Senapati P, Syed SH, Rajan RE, Shandilya J, Swaminathan V, Chatterjee S, Colombo E, Dimitrov S, Pelicci PG, Ranga U, Kundu TK. 2011. The multifunctional protein nucleophosmin (NPM1) is a human linker histone H1 chaperone. Biochemistry 50:2780–2789. http://dx.doi.org/10.1021/bi101835j.
   PubMed Web of Science ®Google Scholar
• Shintomi K, Iwabuchi M, Saeki H, Ura K, Kishimoto T, Ohsumi K. 2005. Nucleosome assembly protein-1 is a linker histone chaperone in Xenopus eggs. Proc Natl Acad Sci U S A 102:8210–8215. http://dx.doi.org/10.1073/pnas.0500822102.
   PubMedGoogle Scholar
• Kepert JF, Mazurkiewicz J, Heuvelman GL, Toth KF, Rippe K. 2005. NAP1 modulates binding of linker histone H1 to chromatin and induces an extended chromatin fiber conformation. J Biol Chem 280:34063–34072. http://dx.doi.org/10.1074/jbc.M507322200.
   PubMed Web of Science ®Google Scholar
• Kondili K, Tsolas O, Papamarcaki T. 1996. Selective interaction between parathymosin and histone H1. Eur J Biochem 242:67–74. http://dx.doi.org/10.1111/j.1432-1033.1996.0067r.x.
   PubMedGoogle Scholar
• Karetsou Z, Sandaltzopoulos R, Frangou-Lazaridis M, Lai CY, Tsolas O, Becker PB, Papamarcaki T. 1998. Prothymosin alpha modulates the interaction of histone H1 with chromatin. Nucleic Acids Res 26:3111–3118. http://dx.doi.org/10.1093/nar/26.13.3111.
   PubMed Web of Science ®Google Scholar
• Erard MS, Belenguer P, Caizergues-Ferrer M, Pantaloni A, Amalric F. 1988. A major nucleolar protein, nucleolin, induces chromatin decondensation by binding to histone H1. Eur J Biochem 175:525–530. http://dx.doi.org/10.1111/j.1432-1033.1988.tb14224.x.
   PubMedGoogle Scholar
• Stasevich TJ, Mueller F, Brown DT, McNally JG. 2010. Dissecting the binding mechanism of the linker histone in live cells: an integrated FRAP analysis. EMBO J 29:1225–1234. http://dx.doi.org/10.1038/emboj.2010.24.
   PubMedGoogle Scholar
• Zhou BR, Jiang J, Feng H, Ghirlando R, Xiao TS, Bai Y. 2015. Structural mechanisms of nucleosome recognition by linker histones. Mol Cell 59:628–638. http://dx.doi.org/10.1016/j.molcel.2015.06.025.
   PubMed Web of Science ®Google Scholar
• Lu X, Hamkalo B, Parseghian MH, Hansen JC. 2009. Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder. Biochemistry 48:164–172. http://dx.doi.org/10.1021/bi801636y.
   PubMedGoogle Scholar
• Roque A, Iloro I, Ponte I, Arrondo JLR, Suau P. 2005. DNA-induced secondary structure of the carboxyl-terminal domain of histone H1. J Biol Chem 280:32141–32147. http://dx.doi.org/10.1074/jbc.M505636200.
   PubMed Web of Science ®Google Scholar
• Caterino TL, Fang H, Hayes JJ. 2011. Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered H1 carboxyl-terminal domain. Mol Cell Biol 31:2341–2348. http://dx.doi.org/10.1128/MCB.05145-11.
   PubMed Web of Science ®Google Scholar
• Allan J, Hartman PG, Crane-Robinson C, Aviles FX. 1980. The structure of histone H1 and its location in chromatin. Nature 288:675–679. http://dx.doi.org/10.1038/288675a0.
   PubMed Web of Science ®Google Scholar
• Raghuram N, Carrero G, Th'ng J, Hendzel MJ. 2009. Molecular dynamics of histone H1. Biochem Cell Biol 87:189–206. http://dx.doi.org/10.1139/O08-127.
   PubMedGoogle Scholar
• Sirotkin AM, Edelmann W, Cheng G, Klein-Szanto A, Kucherlapati R, Skoultchi AI. 1995. Mice develop normally without the H1(0) linker histone. Proc Natl Acad Sci U S A 92:6434–6438. http://dx.doi.org/10.1073/pnas.92.14.6434.
   PubMedGoogle Scholar
• Lin Q, Sirotkin A, Skoultchi AI. 2000. Normal spermatogenesis in mice lacking the testis-specific linker histone H1t. Mol Cell Biol 20:2122–2128. http://dx.doi.org/10.1128/MCB.20.6.2122-2128.2000.
   PubMedGoogle Scholar
• Fan Y, Nikitina T, Morin-Kensicki EM, Zhao J, Magnuson TR, Woodcock CL, Skoultchi AI. 2003. H1 linker histones are essential for mouse development and affect nucleosome spacing in vivo. Mol Cell Biol 23:4559–4572. http://dx.doi.org/10.1128/MCB.23.13.4559-4572.2003.
   PubMed Web of Science ®Google Scholar
• Lin Q, Inselman A, Han X, Xu H, Zhang W, Handel MA, Skoultchi AI. 2004. Reductions in linker histone levels are tolerated in developing spermatocytes but cause changes in specific gene expression. J Biol Chem 279:23525–23535. http://dx.doi.org/10.1074/jbc.M400925200.
   PubMedGoogle Scholar
• Sancho M, Diani E, Beato M, Jordan A. 2008. Depletion of human histone H1 variants uncovers specific roles in gene expression and cell growth. PLoS Genet 4:e1000227. http://dx.doi.org/10.1371/journal.pgen.1000227.
   PubMed Web of Science ®Google Scholar
• Clausell J, Happel N, Hale TK, Doenecke D, Beato M. 2009. Histone H1 subtypes differentially modulate chromatin condensation without preventing ATP-dependent remodeling by SWI/SNF or NURF. PLoS One 4:e0007243.
   PubMed Web of Science ®Google Scholar
• Th'ng JP, Sung R, Ye M, Hendzel MJ. 2005. H1 family histones in the nucleus. Control of binding and localization by the C-terminal domain. J Biol Chem 280:27809–27814.
   Google Scholar
• Orrego M, Ponte I, Roque A, Buschati N, Mora X, Suau P. 2007. Differential affinity of mammalian histone H1 somatic subtypes for DNA and chromatin. BMC Biol 5:22. http://dx.doi.org/10.1186/1741-7007-5-22.
   PubMedGoogle Scholar
• Takata H, Matsunaga S, Morimoto A, Ono-Maniwa R, Uchiyama S, Fukui K. 2007. H1.X with different properties from other linker histones is required for mitotic progression. FEBS Lett 581:3783–3788. http://dx.doi.org/10.1016/j.febslet.2007.06.076.
   PubMed Web of Science ®Google Scholar
• Mayor R, Izquierdo-Bouldstridge A, Millan-Arino L, Bustillos A, Sampaio C, Luque N, Jordan A. 2015. Genome distribution of replication-independent histone H1 variants shows H1.0 associated with nucleolar domains and H1X associated with RNA polymerase II-enriched regions. J Biol Chem 290:7474–7491. http://dx.doi.org/10.1074/jbc.M114.617324.
   PubMed Web of Science ®Google Scholar
• Okuwaki M, Kato K, Shimahara H, Tate S, Nagata K. 2005. Assembly and disassembly of nucleosome core particles containing histone variants by human nucleosome assembly protein I. Mol Cell Biol 25:10639–10651. http://dx.doi.org/10.1128/MCB.25.23.10639-10651.2005.
   PubMedGoogle Scholar
• Okuwaki M, Sumi A, Hisaoka M, Saotome-Nakamura A, Akashi S, Nishimura Y, Nagata K. 2012. Function of homo- and hetero-oligomers of human nucleoplasmin/nucleophosmin family proteins NPM1, NPM2 and NPM3 during sperm chromatin remodeling. Nucleic Acids Res 40:4861–4878. http://dx.doi.org/10.1093/nar/gks162.
   PubMedGoogle Scholar
• Nagata K, Saito S, Okuwaki M, Kawase H, Furuya A, Kusano A, Hanai N, Okuda A, Kikuchi A. 1998. Cellular localization and expression of template-activating factor I in different cell types. Exp Cell Res 240:274–281. http://dx.doi.org/10.1006/excr.1997.3930.
   PubMedGoogle Scholar
• Hisaoka M, Ueshima S, Murano K, Nagata K, Okuwaki M. 2010. Regulation of nucleolar chromatin by B23/nucleophosmin jointly depends upon its RNA binding activity and transcription factor UBF. Mol Cell Biol 30:4952–4964. http://dx.doi.org/10.1128/MCB.00299-10.
   PubMedGoogle Scholar
• Murano K, Okuwaki M, Hisaoka M, Nagata K. 2008. Transcription regulation of the rRNA gene by a multifunctional nucleolar protein, B23/nucleophosmin, through its histone chaperone activity. Mol Cell Biol 28:3114–3126. http://dx.doi.org/10.1128/MCB.02078-07.
   PubMed Web of Science ®Google Scholar
• Stoldt S, Wenzel D, Schulze E, Doenecke D, Happel N. 2007. G1 phase-dependent nucleolar accumulation of human histone H1x. Biol Cell 99:541–552. http://dx.doi.org/10.1042/BC20060117.
   PubMedGoogle Scholar
• Catez F, Ueda T, Bustin M. 2006. Determinants of histone H1 mobility and chromatin binding in living cells. Nat Struct Mol Biol 13:305–310. http://dx.doi.org/10.1038/nsmb1077.
   PubMed Web of Science ®Google Scholar
• George EM, Brown DT. 2010. Prothymosin alpha is a component of a linker histone chaperone. FEBS Lett 584:2833–2836. http://dx.doi.org/10.1016/j.febslet.2010.04.065.
   PubMed Web of Science ®Google Scholar
• Oberg C, Belikov S. 2012. The N-terminal domain determines the affinity and specificity of H1 binding to chromatin. Biochem Biophys Res Commun 420:321–324. http://dx.doi.org/10.1016/j.bbrc.2012.02.157.
   PubMedGoogle Scholar
• Little RD, Braaten DC. 1989. Genomic organization of human 5 S rDNA and sequence of one tandem repeat. Genomics 4:376–383. http://dx.doi.org/10.1016/0888-7543(89)90345-5.
   PubMed Web of Science ®Google Scholar
• Pavelitz T, Rusche L, Matera AG, Scharf JM, Weiner AM. 1995. Concerted evolution of the tandem array encoding primate U2 snRNA occurs in situ, without changing the cytological context of the RNU2 locus. EMBO J 14:169–177.
   PubMedGoogle Scholar
• Hori T, Hosokawa M. 2010. DNA methylation and its involvement in carboxylesterase 1A1 (CES1A1) gene expression. Xenobiotica 40:119–128. http://dx.doi.org/10.3109/00498250903431794.
   PubMed Web of Science ®Google Scholar
• Lu X, Hansen JC. 2004. Identification of specific functional subdomains within the linker histone H10 C-terminal domain. J Biol Chem 279:8701–8707. http://dx.doi.org/10.1074/jbc.M311348200.
   PubMedGoogle Scholar
• Brown DT, Izard T, Misteli T. 2006. Mapping the interaction surface of linker histone H1(0) with the nucleosome of native chromatin in vivo. Nat Struct Mol Biol 13:250–255. http://dx.doi.org/10.1038/nsmb1050.
   PubMedGoogle Scholar
• Contreras A, Hale TK, Stenoien DL, Rosen JM, Mancini MA, Herrera RE. 2003. The dynamic mobility of histone H1 is regulated by cyclin/CDK phosphorylation. Mol Cell Biol 23:8626–8636. http://dx.doi.org/10.1128/MCB.23.23.8626-8636.2003.
   PubMed Web of Science ®Google Scholar
• Flanagan TW, Files JK, Casano KR, George EM, Brown DT. 2016. Photobleaching studies reveal that a single amino acid polymorphism is responsible for the differential binding affinities of linker histone subtypes H1.1 and H1.5. Biol Open 5:372–380. http://dx.doi.org/10.1242/bio.016733.
   PubMedGoogle Scholar
• Talasz H, Sapojnikova N, Helliger W, Lindner H, Puschendorf B. 1998. In vitro binding of H1 histone subtypes to nucleosomal organized mouse mammary tumor virus long terminal repeat promotor. J Biol Chem 273:32236–32243. http://dx.doi.org/10.1074/jbc.273.48.32236.
   PubMedGoogle Scholar
• Meergans T, Albig W, Doenecke D. 1997. Varied expression patterns of human H1 histone genes in different cell lines. DNA Cell Biol 16:1041–1049. http://dx.doi.org/10.1089/dna.1997.16.1041.
   PubMedGoogle Scholar
• McArthur M, Thomas JO. 1996. A preference of histone H1 for methylated DNA. EMBO J 15:1705–1714.
   PubMedGoogle Scholar
• Nightingale K, Wolffe AP. 1995. Methylation at CpG sequences does not influence histone H1 binding to a nucleosome including a Xenopus borealis 5 S rRNA gene. J Biol Chem 270:4197–4200. http://dx.doi.org/10.1074/jbc.270.9.4197.
   PubMedGoogle Scholar
• Gilbert N, Thomson I, Boyle S, Allan J, Ramsahoye B, Bickmore WA. 2007. DNA methylation affects nuclear organization, histone modifications, and linker histone binding but not chromatin compaction. J Cell Biol 177:401–411. http://dx.doi.org/10.1083/jcb.200607133.
   PubMedGoogle Scholar