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2015 | OriginalPaper | Buchkapitel

Chemical and Biological Tools for the Preparation of Modified Histone Proteins

verfasst von : Cecil J. Howard, Ruixuan R. Yu, Miranda L. Gardner, John C. Shimko, Jennifer J. Ottesen

Erschienen in: Protein Ligation and Total Synthesis II

Verlag: Springer International Publishing

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Abstract

Eukaryotic chromatin is a complex and dynamic system in which the DNA double helix is organized and protected by interactions with histone proteins. This system is regulated through a large network of dynamic post-translational modifications (PTMs) which ensure proper gene transcription, DNA repair, and other processes involving DNA. Homogenous protein samples with precisely characterized modification sites are necessary to understand better the functions of modified histone proteins. Here, we discuss sets of chemical and biological tools developed for the preparation of modified histones, with a focus on the appropriate choice of tool for a given target. We start with genetic approaches for the creation of modified histones, including the incorporation of genetic mimics of histone modifications, chemical installation of modification analogs, and the use of the expanded genetic code to incorporate modified amino acids. We also cover the chemical ligation techniques which have been invaluable in the generation of complex modified histones indistinguishable from their natural counterparts. We end with a prospectus on future directions.

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Vorheriges Kapitel New Methods for Chemical Protein Synthesis

Davey CA et al (2002) Solvent mediated interactions in the structure of the nucleosome core particle at 1.9 Å resolution. J Mol Biol 319:1097–1113CrossRef

Luger K et al (1997) Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature 389:251–260CrossRef

Lochmann B, Ivanov D (2012) Histone H3 localizes to the centromeric DNA in budding yeast. PLoS Geneti 8:e1002739

Redon C et al (2002) Histone H2A variant H2AX and H2AZ. Curr Opin Genet Dev 12:162–169CrossRef

Ward IM et al (2003) Accumulation of checkpoint protein 53BP1 at DNA breaks involves its binding to phosphorylated histone H2AX. J Biol Chem 278:19579–19582CrossRef

Park YJ et al (2004) A new fluorescence resonance energy transfer approach demonstrates that the histone variant H2AZ stabilizes the histone octamer within the nucleosome. J Biol Chem 279:24274–24282CrossRef

Jenuwein T (2001) Translating the histone code. Science 293:1074–1080CrossRef

Strahl BD, Allis CD (2000) The language of covalent histone modifications. Nature 403:41–45CrossRef

Schwammle V et al (2014) Large scale analysis of co-existing post-translational modifications in histone tails reveals global fine structure of cross-talk. Mol Cell Proteomics 13:1855–1865CrossRef

10.

Lin S, Garcia BA (2012) Examining histone posttranslational modification patterns by high-resolution mass spectrometry. Methods Enzymol 512:3–28

11.

Tan M et al (2011) Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification. Cell 146:1016–1028CrossRef

12.

Singh MP, Wijeratne SSK, Zempleni J (2013) Biotinylation of lysine 16 in histone H4 contributes toward nucleosome condensation. Arch Biochem Biophys 529:105–111CrossRef

13.

Dhall A et al (2014) Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions. J Biol Chem 289:33827–33837CrossRef

14.

Sakabe K, Wang Z, Hart GW (2010) Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Proc Natl Acad Sci U S A 107:19915–19920CrossRef

15.

Fierz B, Muir TW (2012) Chromatin as an expansive canvas for chemical biology. Nat Chem Biol 8:417–427CrossRef

16.

Pick H, Kilic S, Fierz B (2014) Engineering chromatin states: chemical and synthetic biology approaches to investigate histone modification function. Biochim Biophys Acta 1839:644–656CrossRef

17.

Fierz B (2014) Synthetic chromatin approaches to probe the writing and erasing of histone modifications. ChemMedChem 9:495–504CrossRef

18.

Frederiks F et al (2011) A modified epigenetics toolbox to study histone modifications on the nucleosome core. ChemBioChem 12:308–313CrossRef

19.

Matsubara K et al (2007) Global analysis of functional surfaces of core histones with comprehensive point mutants. Genes Cells 12:13–33CrossRef

20.

Hyland EM et al (2005) Insights into the role of histone H3 and histone H4 core modifiable residues in Saccharomyces cerevisiae. Mol Cell Biol 25:10060–10070CrossRef

21.

Luger K, Rechsteiner TJ, Richmond TJ (1999) Preparation of nucleosome core particle from recombinant histones. Methods Enzymol 304:1–19

22.

Watanabe S et al (2010) Structural characterization of H3K56Q nucleosomes and nucleosomal arrays. Biochim Biophys Acta 1799:480–486CrossRef

23.

Muthurajan UM et al (2004) Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions. EMBO 23:260–270CrossRef

24.

Iwasaki W et al (2011) Comprehensive structural analysis of mutant nucleosomes containing lysine to glutamine (KQ) substitutions in the H3 and H4 histone-fold domains. Biochemistry 50:7822–7832CrossRef

25.

Yu Q et al (2011) Differential contributions of histone H3 and H4 residues to heterochromatin structure. Genetics 188:291–308CrossRef

26.

Wang X, Hayes JJ (2008) Acetylation mimics within individual core histone tail domains indicate distinct roles in regulating the stability of higher-order chromatin structure. Mol Cell Biol 28:227–236CrossRef

27.

Allahverdi A et al (2010) The effects of histone H4 tail acetylations on cation-induced chromatin folding and self-association. Nucleic Acids Res 39:1680–1691CrossRef

28.

Manohar M et al (2009) Acetylation of histone H3 at the nucleosome dyad alters DNA-histone binding. J Biol Chem 284:23312–23321CrossRef

29.

North JA et al (2011) Phosphorylation of histone H3(T118) alters nucleosome dynamics and remodeling. Nucleic Acids Res 39:6465–6474CrossRef

30.

North JA et al (2014) Histone H3 phosphorylation near the nucleosome dyad alters chromatin structure. Nucleic Acids Res 42:4922–4933CrossRef

31.

Shimko JC et al (2011) Preparation of fully synthetic histone H3 reveals that acetyl-lysine 56 facilitates protein binding within nucleosomes. J Mol Biol 408:187–204CrossRef

32.

Neumann H et al (2009) A method for genetically installing site-specific acetylation in recombinant histones defines the effects of H3 K56 acetylation. Mol Cell 36:153–163CrossRef

33.

Masumoto H et al (2005) A role for cell-cycle-regulated histone H3 lysine 56 acetylation in the DNA damage response. Nature 436:294–298CrossRef

34.

Liu CC, Schultz PG (2010) Adding new chemistries to the genetic code. Annu Rev Biochem 79:413–444CrossRef

35.

Chin JW (2014) Expanding and reprogramming the genetic code of cells and animals. Annu Rev Biochem 83:379–408CrossRef

36.

Hao B et al (2002) A new UAG-encoded residue in the structure of a methanogen methyltransferase. Science 296:1462–1466CrossRef

37.

Tarrant MK, Cole PA (2009) The chemical biology of protein phosphorylation. Annu Rev Biochem 78:797–825CrossRef

38.

Tropberger P, Schneider R (2013) Scratching the (lateral) surface of chromatin regulation by histone modifications. Nat Struct Mol Biol 20:657–661CrossRef

39.

Di Cerbo V et al. (2014) Acetylation of histone H3 at lysine 64 regulates nucleosome dynamics and facilitates transcription. Elife 3:e01632

40.

Nguyen DP et al (2010) Genetically directing ɛ-N,N-dimethyl-l-lysine in recombinant histones. Chem Biol 17:1072–1076CrossRef

41.

Wang Y-S et al (2010) A genetically encoded photocaged N^ε-methyl-l-lysine. Mol BioSyst 6:1557CrossRef

42.

Xie Z et al (2012) Lysine succinylation and lysine malonylation in histones. Mol Cell Proteomics 11:100–107CrossRef

43.

Gattner MJ, Vrabel M, Carell T (2013) Synthesis of ε-N-propionyl-, ε-N-butyryl-, and ε-N-crotonyl-lysine containing histone H3 using the pyrrolysine system. Chem Commun 49:379CrossRef

44.

Kim CH et al (2012) Site-specific incorporation of ε-N-crotonyllysine into histones. Angew Chem Int Ed 51:7246–7249CrossRef

45.

Yang R et al (2009) Dual native chemical ligation at lysine. JACS Commun 131:13592–13593CrossRef

46.

Li X et al (2009) A pyrrolysine analogue for site-specific protein ubiquitination. Angew Chem Int Ed 48:9184–9187CrossRef

47.

Yang R et al (2014) Native chemical ubiquitination using a genetically incorporated azidonorleucine. Chem Commun 50:7971CrossRef

48.

Guo J et al (2008) Site-specific incorporation of methyl- and acetyl-lysine analogues into recombinant proteins. Angew Chem Int Ed 47:6399–6401CrossRef

49.

Wang ZU et al (2012) A facile method to synthesize histones with posttranslational modification mimics. Biochemistry 51:5232–5234CrossRef

50.

Chalker JM et al (2011) Methods for converting cysteine to dehydroalanine on peptides and proteins. Chem Sci 2:1666CrossRef

51.

Chalker JM et al (2012) Conversion of cysteine into dehydroalanine enables access to synthetic histones bearing diverse post-translational modifications. Angew Chem Int Ed Engl 51:1835–1839CrossRef

52.

Sawicka A, Seiser C (2014) Sensing core histone phosphorylation — a matter of perfect timing. Biochim Biophys Acta 1839:711–718CrossRef

53.

Park HS et al (2011) Expanding the genetic code of Escherichia coli with phosphoserine. Science 333:1151–1154CrossRef

54.

Lee S et al (2013) A facile strategy for selective incorporation of phosphoserine into histones. Angew Chem Int Ed 52:5771–5775CrossRef

55.

Chin JW et al (2003) Progress toward an expanded eukaryotic genetic code. Chem Biol 10:511–519CrossRef

56.

Lajoie MJ et al (2013) Genomically recoded organisms expand biological functions. Science 342:357–360CrossRef

57.

Ambrogelly A, Palioura S, Söll D (2007) Natural expansion of the genetic code. Nat Chem Biol 3:29–35CrossRef

58.

Anderson JC et al. (2004) An expanded genetic code with a functional quadruplet codon. Proc Natl Acad Sci 101:7566–7571

59.

Wang K, Schmied WH, Chin JW (2012) Reprogramming the genetic code: from triplet to quadruplet codes. Angew Chem Int Ed 51:2288–2297CrossRef

60.

Riddle DL, Carbon J (1973) Frameshift suppression: a nucleotide addition in the anticodon of a glycine transfer RNA. Nat New Biol 242:230–234CrossRef

61.

Bowman A et al (2010) Probing the (H3-H4)2 histone tetramer structure using pulsed EPR spectroscopy combined with site-directed spin labelling. Nucleic Acids Res 38:695–707CrossRef

62.

Ward R et al (2009) Long distance PELDOR measurements on the histone core particle. J Am Chem Soc 131:1348–1349CrossRef

63.

Tims HS, Widom J (2007) Stopped-flow fluorescence resonance energy transfer for analysis of nucleosome dynamics. Methods (San Diego, Calif.) 41:296–303

64.

Dechassa ML et al (2008) Architecture of the SWI/SNF-nucleosome complex. Mol Cell Biol 28:6010–6021CrossRef

65.

Ferreira H et al (2007) Histone tails and the H3 αN helix regulate nucleosome mobility and stability. Mol Cell Biol 27:4037–4048CrossRef

66.

Kurumizaka H et al (2013) Current progress on structural studies of nucleosomes containing histone H3 variants. Curr Opin Struct Biol 23:109–115CrossRef

67.

Flaus A et al (1996) Mapping nucleosome position at single base-pair resolution by using site-directed hydroxyl radicals. Proc Natl Acad Sci U S A 93:1370–1375CrossRef

68.

Poirier MG et al (2009) Dynamics and function of compact nucleosome arrays. Nat Struct Mol Biol 16:938–944CrossRef

69.

Simon MD et al (2007) The site-specific installation of methyl-lysine analogs into recombinant histones. Cell 128:1003–1012CrossRef

70.

Kenyon G, Bruice TW (1977) Novel sulfhydryl reagents. Methods Enzymol 47:407–430CrossRef

71.

Lauberth SM et al (2013) H3K4me3 interactions with TAF3 regulate preinitiation complex assembly and selective gene activation. Cell 152:1021–1036CrossRef

72.

Lu X et al (2008) The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure. Nat Struct Mol Biol 15:1122–1124CrossRef

73.

Xu C et al (2008) Structural basis for the recognition of methylated histone H3K36 by the Eaf3 subunit of histone deacetylase complex Rpd3S. Structure 16:1740–1750CrossRef

74.

Eidahl JO et al (2013) Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes. Nucleic Acids Res 41:3924–3936CrossRef

75.

Hung T et al (2009) ING4 mediates crosstalk between histone H3 K4 trimethylation and H3 acetylation to attenuate cellular transformation. Mol Cell 33:248–256CrossRef

76.

Margueron R et al (2009) Role of the polycomb protein EED in the propagation of repressive histone marks. Nature 461:762–767CrossRef

77.

Huang R et al (2010) Site-specific introduction of an acetyl-lysine mimic into peptides and proteins by cysteine alkylation. J Am Chem Soc 132:9986–9987CrossRef

78.

Hoyle CE, Bowman CN (2010) Thiol-ene click chemistry. Angew Chem Int Ed 49:1540–1573CrossRef

79.

Li F et al (2011) A direct method for site-specific protein acetylation. Angew Chem Int Ed 50:9611–9614CrossRef

80.

Le D et al. (2013) Site-Specific and Regiospecific Installation of Methylarginine Analogues into Recombinant Histones and Insights into Effector Protein Binding. J Am Chem Soc 135:2879–2882.CrossRef

81.

Chatterjee A et al (2010) Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation. Nat Chem Biol 6:267–269CrossRef

82.

Whitcomb SJ et al (2012) Histone monoubiquitylation position determines specificity and direction of enzymatic cross-talk with histone methyltransferases Dot1L and PRC2. J Biol Chem 287:23718–23725CrossRef

83.

Dawson PE et al (1994) Synthesis of proteins by native chemical ligation. Science 266:776–779CrossRef

84.

He S et al. (2003) Facile synthesis of site-specifically acetylated and methylated histone proteins: reagents for evaluation of the histone code hypothesis. Proc Natl Acad Sci 100:12033–12038

85.

Shogren-Knaak MA, Fry CJ, Peterson CL (2003) A native peptide ligation strategy for deciphering nucleosomal histone modifications. J Biol Chem 278:15744–15748CrossRef

86.

Fierz B et al (2011) Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction. Nat Chem Biol 7:113–119CrossRef

87.

Nguyen DP et al (2014) Genetic encoding of photocaged cysteine allows photoactivation of TEV protease in live mammalian cells. J Am Chem Soc 136:2240–2243CrossRef

88.

Fry CJ, Shogren-Knaak MA, Peterson CL (2004) Histone H3 amino-terminal tail phosphorylation and acetylation: synergistic or independent transcriptional regulatory marks? Cold Spring Harb Symp Quant Biol 69:219–226CrossRef

89.

Shogren-Knaak M (2006) Histone H4-K16 acetylation controls chromatin structure and protein interactions. Science 311:844–847CrossRef

90.

Ferreira H, Flaus A, Owen-Hughes T (2007) Histone modifications influence the action of Snf2 family remodelling enzymes by different mechanisms. J Mol Biol 374:563–579CrossRef

91.

Liu Y et al (2011) Influence of histone tails and H4 tail acetylations on nucleosome-nucleosome interactions. J Mol Biol 414:749–764CrossRef

92.

Chiang KP et al (2009) A semisynthetic strategy to generate phosphorylated and acetylated histone H2B. Chembiochem 10:2182–2187CrossRef

93.

Casadio F et al (2013) H3R42me2a is a histone modification with positive transcriptional effects. PNAS 110:14894–14899CrossRef

94.

Kim J et al (2013) The n-SET domain of Set1 regulates H2B ubiquitylation-dependent H3K4 methylation. Mol Cell 49:1121–1133CrossRef

95.

Chen Z, Gryzbowski AT, Ruthenburg AJ (2014) Traceless semisynthesis of a set of histone 3 species bearing specific lysine methylation marks. ChemBioChem 15:2071–2075CrossRef

96.

Hackeng TM, Dawson PE (1999) Protein synthesis by native chemical ligation: expanded scope by using straightforward methodology. Proc Natl Acad Sci U S A 96:10069–10073CrossRef

97.

Li S, Shogren-Knaak MA (2008) Cross-talk between histone H3 tails produces cooperative nucleosome acetylation. Proc Natl Acad Sci 105:18243–18248

98.

Fry CJ et al (2006) The LRS and SIN domains: two structurally equivalent but functionally distinct nucleosomal surfaces required for transcriptional silencing. Mol Cell Biol 26:9045–9059CrossRef

99.

Zhu Y, van der Donk W (2001) Convergent synthesis of peptide conjugates using dehydroalanines for chemoselective ligations. Org Lett 3:1189–1192CrossRef

100.

Wan Q, Danishefsky SJ (2007) Free-radical-based, specific desulfurization of cysteine: a powerful advance in the synthesis of polypeptides and glycopolypeptides. Angew Chem Int Ed 46:9248–9252CrossRef

101.

Fierz B et al (2012) Stability of nucleosomes containing homogenously ubiquitylated H2A and H2B prepared using semisynthesis. J Am Chem Soc 134:19548–19551CrossRef

102.

Wong CTT et al (2014) Realizing serine/threonine ligation: scope and limitations and mechanistic implication thereof. Front Chem 2:28

103.

Haase C, Rohde H, Seitz O (2008) Native chemical ligation at valine. Angew Chem Int Ed 47:6807–6810CrossRef

104.

Crich D, Banerjee A (2007) Native chemical ligation at phenylalanine. JACS Commun 129:10064–10065CrossRef

105.

Mersfelder EL, Parthun MR (2006) The tale beyond the tail: histone core domain modifications and the regulation of chromatin structure. Nucleic Acids Res 34:2653–2662CrossRef

106.

Jack AM, Hake S (2014) Getting down to the core of histone modifications. Chromosoma 123:355–371CrossRef

107.

Wood DW, Camarero JA (2014) Intein applications: from protein purification and labeling to metabolic control methods. J Biol Chem 289:14512–14519CrossRef

108.

Ayers B et al (1999) Introduction of unnatural amino acids into proteins using expressed protein ligation. Pept Sci 51:343–354CrossRef

109.

McGinty RK et al (2008) Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation. Nature 453:812–816CrossRef

110.

Shimko JC et al. (2013) Preparing semisynthetic and fully synthetic histones H3 and H4 to modify the nucleosome core. Methods Mol Biol 981:177–192

111.

Simon M et al (2011) Histone fold modifications control nucleosome unwrapping and disassembly. Proc Natl Acad Sci U S A 108:12711–12716CrossRef

112.

Javaid S et al (2009) Nucleosome remodeling by hMSH2-hMSH6. Mol Cell 36:1086–1094CrossRef

113.

Kruger W et al (1995) Amino acid substitutions in the structured domains of histones H3 and H4 partially relieve the requirement of the yeast SWI/SNF complex for transcription. Genes Dev 9:2770–2779CrossRef

114.

Hurd PJ et al (2009) Phosphorylation of histone H3 Thr-45 is linked to apoptosis. J Biol Chem 284:16675–16683CrossRef

115.

Ulyanova NP, Schnitzler GR (2005) Human SWI/SNF generates abundant, structurally altered dinucleosomes on polynucleosomal templates. Mol Cell Biol 25:11156–11170CrossRef

116.

Schnitzler GR, Sif S, Kingston RE (1998) Human SWI/SNF interconverts a nucleosome between its base state and a stable remodeled state. Cell 94:17–27CrossRef

117.

McGinty RK et al (2009) Structure–activity analysis of semisynthetic nucleosomes: mechanistic insights into the stimulation of dot1l by ubiquitylated histone H2B. ACS Chem Biol 4:958–968CrossRef

118.

Nguyen UTT et al (2014) Accelerated chromatin biochemistry using DNA-barcoded nucleosome libraries. Nat Methods 11:834–840CrossRef

119.

Mahto SK et al (2011) A reversible protection strategy to improve Fmoc-SPPS of peptide thioesters by the N-acylurea approach. ChemBioChem 12:2488–2494CrossRef

120.

Fang GM, Wang JX, Liu L (2012) Convergent chemical synthesis of proteins by ligation of peptide hydrazides. Angew Chem Int Ed Engl 51:10347–10350CrossRef

121.

Li J et al (2014) One-pot native chemical ligation of peptide hydrazides enables total synthesis of modified histones. Org Biomol Chem 12:5435CrossRef

122.

Siman P et al (2013) Convergent chemical synthesis of histone H2B protein for the site-specific ubiquitination at Lys34. Angew Chem Int Ed 52:8059–8063CrossRef

123.

Jbara M, Seenaiah M, Brik A (2014) Solid phase chemical ligation employing a Rink amide linker for the synthesis of histone H2B protein. Chem Commun 50:12534–12537CrossRef

124.

Linghu C et al (2013) Discovering common combinatorial histone modification patterns in the human genome. Gene 518:171–178CrossRef

125.

Zheng C, Hayes JJ (2003) Intra- and inter-nucleosomal protein-DNA interactions of the core histone tail domains in a model system. J Biol Chem 278:24217–24224CrossRef

126.

Mohberg J, Rusch HP (1969) Isolation of the nuclear histones from the myxomycete, Physarum polycephalum. Arch Biochem Biophys 134:577–589CrossRef

127.

Thiriet C, Hayes JJ (1999) Histone proteins in vivo: cell-cycle-dependent physiological effects of exogenous linker histones incorporated into Physarum polycephalum. Methods 17:140–150CrossRef

128.

Prior CP et al (1980) Incorporation of exogenous pyrene-labeled histone into Physarum chromatin: a system for studying changes in nucleosomes assembled in vivo. Cell 20:597–608CrossRef

129.

Adamatzky A (2013) Slimeware: engineering devices with slime mold. Artificial Life 19:317–330CrossRef

130.

Taylor B et al (2014) Physarum polycephalum: towards a biological controller. Biosystems 127C:42–46

131.

Ejlassi-Lassallette A et al (2010) H4 replication-dependent diacetylation and Hat1 promote S-phase chromatin assembly in vivo. Mol Biol Cell 22:245–255CrossRef

132.

Thiriet C, Hayes JJ (2001) A novel labeling technique reveals a function for histone H2A/H2B dimer tail domains in chromatin assembly in vivo. Genes Dev 15:2048–2053CrossRef

133.

Studitsky VM, Clark DJ, Felsenfeld G (1994) A histone octamer can step around a transcribing polymerase without leaving the template. Cell 76:371–382CrossRef

134.

Kireeva ML et al (2002) Nucleosome remodeling induced by RNA polymerase II: loss of the H2A-H2B dimer during transcription. Mol Cell 9:541–552CrossRef

135.

Nishiyama A et al (2008) Intracellular delivery of acetyl-histone peptides inhibits native bromodomain-chromatin interactions and impairs mitotic progression. FEBS Lett 582:1501–1507CrossRef

136.

Heo K et al (2013) Cell-penetrating H4 tail peptides potentiate p53-mediated transactivation via inhibition of G9a and HDAC1. Oncogene 32:2510–2520CrossRef

137.

Keller AA et al (2014) Transduction of proteins into Leishmania tarentolae by formation of non-covalent complexes with cell-penetrating peptides. J Cell Biochem 115:243–252CrossRef

138.

Rosenbluh J et al (2004) Non-endocytic penetration of core histones into petunia protoplasts and cultured cells: a novel mechanism for the introduction of macromolecules into plant cells. Biochim Biophys Acta 1664:230–240CrossRef

139.

Hariton-Gazal E et al (2003) Direct translocation of histone molecules across cell membranes. J Cell Sci 116:4577–4586CrossRef

140.

Balicki D et al. (2002) Structure and function correlation in histone H2A peptide-mediated gene transfer. Proc Natl Acad Sci 99:7467–7471

141.

Kaouass M, Beaulieu R, Balicki D (2006) Histonefection: Novel and potent non-viral gene delivery. J Control Release 113:245–254CrossRef

Titel: Chemical and Biological Tools for the Preparation of Modified Histone Proteins
verfasst von: Cecil J. Howard
Ruixuan R. Yu
Miranda L. Gardner
John C. Shimko
Jennifer J. Ottesen
Verlag: Springer International Publishing
Buch: Protein Ligation and Total Synthesis II
Print ISBN: 978-3-319-19188-1

Electronic ISBN: 978-3-319-19189-8

Copyright-Jahr: 2015
DOI: https://doi.org/10.1007/128_2015_629