메뉴 건너뛰기




Volumn 180, Issue 1, 2012, Pages 101-109

Contribution of hydrophobic interactions to the folding and fibrillation of histone H1 and its carboxy-terminal domain

Author keywords

Amyloid fibers; Carboxy terminal domain; Folding; Histone H1; Hydrophobic interactions; Phosphorylation

Indexed keywords

HISTONE H1;

EID: 84866999588     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2012.07.004     Document Type: Article
Times cited : (13)

References (51)
  • 1
    • 0842281643 scopus 로고    scopus 로고
    • Mammalian prion biology: one century of evolving concepts
    • Aguzzi A., Polymenidou M. Mammalian prion biology: one century of evolving concepts. Cell 2004, 16:313-327.
    • (2004) Cell , vol.16 , pp. 313-327
    • Aguzzi, A.1    Polymenidou, M.2
  • 2
    • 0344672542 scopus 로고    scopus 로고
    • Structure and dynamics of membrane proteins as studied by infrared spectroscopy
    • Arrondo J.L.R., Goñi F.M. Structure and dynamics of membrane proteins as studied by infrared spectroscopy. Prog. Biophys. Mol. Biol. 1999, 72:367-405.
    • (1999) Prog. Biophys. Mol. Biol. , vol.72 , pp. 367-405
    • Arrondo, J.L.R.1    Goñi, F.M.2
  • 3
    • 0031422517 scopus 로고    scopus 로고
    • Histone H1; a neuronal protein that binds bacterial lipopolysaccharide
    • Bolton S.J., Perry V.H. Histone H1; a neuronal protein that binds bacterial lipopolysaccharide. J. Neurocytol. 1997, 26:823-831.
    • (1997) J. Neurocytol. , vol.26 , pp. 823-831
    • Bolton, S.J.1    Perry, V.H.2
  • 4
    • 0032527909 scopus 로고    scopus 로고
    • Extracellularly occurring histone H1 mediates the binding of thyroglobulin to the cell surface of mouse macrophages
    • Brix K., Summa W., Lottspeich F., Herzog V. Extracellularly occurring histone H1 mediates the binding of thyroglobulin to the cell surface of mouse macrophages. J. Clin. Invest. 1998, 102:283-293.
    • (1998) J. Clin. Invest. , vol.102 , pp. 283-293
    • Brix, K.1    Summa, W.2    Lottspeich, F.3    Herzog, V.4
  • 5
    • 4744349987 scopus 로고    scopus 로고
    • Combining prediction, computation and experiment for the characterization of protein disorder
    • Bracken C., Iakoucheva L.M., Romero P.R., Dunker A.K. Combining prediction, computation and experiment for the characterization of protein disorder. Curr. Opin. Struct. Biol. 2004, 14:570-576.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 570-576
    • Bracken, C.1    Iakoucheva, L.M.2    Romero, P.R.3    Dunker, A.K.4
  • 6
    • 79958068470 scopus 로고    scopus 로고
    • Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered H1 carboxyl-terminal domain
    • Caterino T.L., Fang H., Hayes J.J. Nucleosome linker DNA contacts and induces specific folding of the intrinsically disordered H1 carboxyl-terminal domain. Mol. Cell. Biol. 2011, 11:2341-2348.
    • (2011) Mol. Cell. Biol. , vol.11 , pp. 2341-2348
    • Caterino, T.L.1    Fang, H.2    Hayes, J.J.3
  • 7
    • 0029842987 scopus 로고    scopus 로고
    • Histone H1 suppresses tumor growth of leukemia cells in vitro, ex vivo and in an animal model suggesting extracellular functions of histones
    • Class R., Lindman S., Fassbender C., Leinenbach H.P., Rawer S., et al. Histone H1 suppresses tumor growth of leukemia cells in vitro, ex vivo and in an animal model suggesting extracellular functions of histones. Am. J. Clin. Oncol. 1996, 19:522-531.
    • (1996) Am. J. Clin. Oncol. , vol.19 , pp. 522-531
    • Class, R.1    Lindman, S.2    Fassbender, C.3    Leinenbach, H.P.4    Rawer, S.5
  • 9
    • 33746338256 scopus 로고    scopus 로고
    • Linker histone H1 binds to disease associated amyloid-like fibrils
    • Duce J.A., Smith D.P., Blake R.E., Crouch P.J., Li Q.-X., et al. Linker histone H1 binds to disease associated amyloid-like fibrils. J. Mol. Biol. 2006, 361:493-505.
    • (2006) J. Mol. Biol. , vol.361 , pp. 493-505
    • Duce, J.A.1    Smith, D.P.2    Blake, R.E.3    Crouch, P.J.4    Li, Q.-X.5
  • 10
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., Wright P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 2005, 6:197-208.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 12
  • 13
    • 0034894258 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27(Kip1)
    • Flaugh S.L., Lumb K.J. Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27(Kip1). Biomacromolecules 2001, 2:538-540.
    • (2001) Biomacromolecules , vol.2 , pp. 538-540
    • Flaugh, S.L.1    Lumb, K.J.2
  • 14
    • 36348996602 scopus 로고    scopus 로고
    • Phospholipid interaction induces molecular-level polymorphism in apolipoprotein C-II amyloid fibrils via alternative assembly pathways
    • Griffin M.D., Mok M.L., Wilson L.M., Pham C.L., Waddington L.J., et al. Phospholipid interaction induces molecular-level polymorphism in apolipoprotein C-II amyloid fibrils via alternative assembly pathways. J. Mol. Biol. 2008, 375:240-256.
    • (2008) J. Mol. Biol. , vol.375 , pp. 240-256
    • Griffin, M.D.1    Mok, M.L.2    Wilson, L.M.3    Pham, C.L.4    Waddington, L.J.5
  • 15
    • 33646557678 scopus 로고    scopus 로고
    • The role of lipid-protein interactions in amyloid-type protein fibril formation
    • Gorbenko G.P., Kinnunen P.K.S. The role of lipid-protein interactions in amyloid-type protein fibril formation. Chem. Phys. Lipids 2006, 141:72-82.
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 72-82
    • Gorbenko, G.P.1    Kinnunen, P.K.S.2
  • 17
    • 0017401125 scopus 로고
    • Studies on the role and mode of operation of the very-lysine-rich histone H1 in eukaryote chromatin. The three structural regions of the histone H1 molecule
    • Hartman P.G., Chapman G.E., Moss T., Bradbury E.M. Studies on the role and mode of operation of the very-lysine-rich histone H1 in eukaryote chromatin. The three structural regions of the histone H1 molecule. Eur. J. Biochem. 1977, 77:45-51.
    • (1977) Eur. J. Biochem. , vol.77 , pp. 45-51
    • Hartman, P.G.1    Chapman, G.E.2    Moss, T.3    Bradbury, E.M.4
  • 18
    • 0022411691 scopus 로고
    • Human peripheral blood monocytes display surface antigens recognized by monoclonal antinuclear antibodies
    • Holers V.M., Kotzin B.L. Human peripheral blood monocytes display surface antigens recognized by monoclonal antinuclear antibodies. J. Clin. Invest. 1985, 76:991-998.
    • (1985) J. Clin. Invest. , vol.76 , pp. 991-998
    • Holers, V.M.1    Kotzin, B.L.2
  • 19
    • 0031417782 scopus 로고    scopus 로고
    • Histone-induced damage of a mammalian epithelium: the role of protein and membrane structure
    • Kleine T.J., Lewis P.N., Lewis S.A. Histone-induced damage of a mammalian epithelium: the role of protein and membrane structure. Am. J. Physiol. 1997, 273:C1925-C1936.
    • (1997) Am. J. Physiol. , vol.273
    • Kleine, T.J.1    Lewis, P.N.2    Lewis, S.A.3
  • 20
    • 0018022569 scopus 로고
    • Dissociation, aggregation of sesame alpha-globulin in nonionic detergent solution
    • Lakshmi T.S., Nandi P.K. Dissociation, aggregation of sesame alpha-globulin in nonionic detergent solution. Int. J. Pept. Protein Res. 1978, 12:197-203.
    • (1978) Int. J. Pept. Protein Res. , vol.12 , pp. 197-203
    • Lakshmi, T.S.1    Nandi, P.K.2
  • 21
    • 0042388117 scopus 로고    scopus 로고
    • Revisiting the structure and functions of the linker histone C-terminal tail domain
    • Lu X., Hansen J.C. Revisiting the structure and functions of the linker histone C-terminal tail domain. Biochem. Cell Biol. 2003, 81:173-176.
    • (2003) Biochem. Cell Biol. , vol.81 , pp. 173-176
    • Lu, X.1    Hansen, J.C.2
  • 22
    • 1542305640 scopus 로고    scopus 로고
    • Identification of specific functional subdomains within the linker histone H10 C-terminal domain
    • 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.
    • (2004) J. Biol. Chem. , vol.279 , pp. 8701-8707
    • Lu, X.1    Hansen, J.C.2
  • 24
    • 38049056730 scopus 로고    scopus 로고
    • Lipids revert inert A beta amyloid fibrils to neurotoxic protofibrils that affect learning in mice
    • Martins I.C., Kuperstein I., Wilkinson H., Maes E., Vanbravant M., et al. Lipids revert inert A beta amyloid fibrils to neurotoxic protofibrils that affect learning in mice. EMBO J. 2008, 27:224-233.
    • (2008) EMBO J. , vol.27 , pp. 224-233
    • Martins, I.C.1    Kuperstein, I.2    Wilkinson, H.3    Maes, E.4    Vanbravant, M.5
  • 25
    • 0018557002 scopus 로고
    • Theory of H1-mediated control of higher orders of structure in chromatin
    • Manning G.S. Theory of H1-mediated control of higher orders of structure in chromatin. Biopolymers 1979, 18:2929-2942.
    • (1979) Biopolymers , vol.18 , pp. 2929-2942
    • Manning, G.S.1
  • 26
    • 0034713846 scopus 로고    scopus 로고
    • Involvement of electrostatic interactions in the mechanism of peptide folding induced by sodium dodecyl sulfate binding
    • Montserret R., McLeish M.J., Böckman A., Geourjon C., Penin F. Involvement of electrostatic interactions in the mechanism of peptide folding induced by sodium dodecyl sulfate binding. Biochemistry 2000, 39:8362-8373.
    • (2000) Biochemistry , vol.39 , pp. 8362-8373
    • Montserret, R.1    McLeish, M.J.2    Böckman, A.3    Geourjon, C.4    Penin, F.5
  • 27
    • 4444311182 scopus 로고    scopus 로고
    • Conformational prerequisites for formation of amyloid fibrils from histones
    • Munishkina L.A., Fink A.L., Uversky V.N. Conformational prerequisites for formation of amyloid fibrils from histones. J. Mol. Biol. 2004, 342:1305-1324.
    • (2004) J. Mol. Biol. , vol.342 , pp. 1305-1324
    • Munishkina, L.A.1    Fink, A.L.2    Uversky, V.N.3
  • 28
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • Nilsson M.R. Techniques to study amyloid fibril formation in vitro. Methods 2004, 34:151-160.
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 29
    • 79953210733 scopus 로고    scopus 로고
    • Protein-surfactant interactions: A tale of many states
    • Otzen O. Protein-surfactant interactions: A tale of many states. Biochim. Biophys. Acta 2011, 1814:562-591.
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 562-591
    • Otzen, O.1
  • 30
    • 33749866720 scopus 로고    scopus 로고
    • On the possibility that H1 histone interaction with DNA occurs through phosphates connecting lysine and arginine side chain groups
    • Piscopo M., De Petrocellis L., Conte M., Pulcrano G., Geraci G. On the possibility that H1 histone interaction with DNA occurs through phosphates connecting lysine and arginine side chain groups. Acta Biochim. Pol. 2006, 53:507-515.
    • (2006) Acta Biochim. Pol. , vol.53 , pp. 507-515
    • Piscopo, M.1    De Petrocellis, L.2    Conte, M.3    Pulcrano, G.4    Geraci, G.5
  • 31
    • 61549124413 scopus 로고    scopus 로고
    • Neutron-scattering probe of complexes of sodium dodecyl sulfate and serum albumin during polyacrylamide gel electrophoresis
    • Pozzo D.C. Neutron-scattering probe of complexes of sodium dodecyl sulfate and serum albumin during polyacrylamide gel electrophoresis. Langmuir 2009, 25:1558-1565.
    • (2009) Langmuir , vol.25 , pp. 1558-1565
    • Pozzo, D.C.1
  • 32
    • 17044454299 scopus 로고    scopus 로고
    • Efficacy of macromolecular crowding in forcing proteins to fold
    • Qu Y., Bolen D.W. Efficacy of macromolecular crowding in forcing proteins to fold. Biophys. Chem. 2002, 101-102:155-165.
    • (2002) Biophys. Chem. , pp. 155-165
    • Qu, Y.1    Bolen, D.W.2
  • 34
    • 0025966012 scopus 로고
    • Cooperative interaction of the C-terminal domain of histone H1 with DNA
    • Rodríguez A.T., Pérez L., Morán F., Montero F., Suau P. Cooperative interaction of the C-terminal domain of histone H1 with DNA. Biophys. Chem. 1991, 39:145-152.
    • (1991) Biophys. Chem. , vol.39 , pp. 145-152
    • Rodríguez, A.T.1    Pérez, L.2    Morán, F.3    Montero, F.4    Suau, P.5
  • 35
    • 25444523218 scopus 로고    scopus 로고
    • DNA-induced secondary structure of the carboxyl-terminal domain of histone H1
    • Roque A., Iloro I., Ponte I., Arrondo J.L., Suau P. DNA-induced secondary structure of the carboxyl-terminal domain of histone H1. J. Biol. Chem. 2005, 280:32141-32147.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32141-32147
    • Roque, A.1    Iloro, I.2    Ponte, I.3    Arrondo, J.L.4    Suau, P.5
  • 36
    • 11444267576 scopus 로고    scopus 로고
    • The preferential binding of histone H1 to DNA scaffold-associated regions is determined by its C-terminal domain
    • Roque A., Orrego M., Ponte I., Suau P. The preferential binding of histone H1 to DNA scaffold-associated regions is determined by its C-terminal domain. Nucleic Acids Res. 2004, 32:6111-6119.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 6111-6119
    • Roque, A.1    Orrego, M.2    Ponte, I.3    Suau, P.4
  • 37
    • 34548722169 scopus 로고    scopus 로고
    • Macromolecular crowding induces a molten globule state in the C-terminal domain of histone H1
    • Roque A., Ponte I., Suau P. Macromolecular crowding induces a molten globule state in the C-terminal domain of histone H1. Biophys J. 2007, 93:2170-2177.
    • (2007) Biophys J. , vol.93 , pp. 2170-2177
    • Roque, A.1    Ponte, I.2    Suau, P.3
  • 38
    • 49249102932 scopus 로고    scopus 로고
    • Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation
    • Roque A., Ponte I., Arrondo J.L.R., Suau P. Phosphorylation of the carboxy-terminal domain of histone H1: effects on secondary structure and DNA condensation. Nucleic Acids Res. 2008, 36:4719-4726.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4719-4726
    • Roque, A.1    Ponte, I.2    Arrondo, J.L.R.3    Suau, P.4
  • 39
    • 69549124299 scopus 로고    scopus 로고
    • Role of charge neutralization in the folding of the carboxy-terminal domain of histone H1
    • Roque A., Ponte I., Suau P. Role of charge neutralization in the folding of the carboxy-terminal domain of histone H1. J. Phys. Chem. 2009, 113:12061-12066.
    • (2009) J. Phys. Chem. , vol.113 , pp. 12061-12066
    • Roque, A.1    Ponte, I.2    Suau, P.3
  • 40
    • 0031814274 scopus 로고    scopus 로고
    • Potential role of epithelial cell-derived histone H1 proteins in innate antimicrobial defense in the human gastrointestinal tract
    • Rose F.R., Bailey K., Keyte J.W., Chan W.C., Greenwood D., et al. Potential role of epithelial cell-derived histone H1 proteins in innate antimicrobial defense in the human gastrointestinal tract. Infect. Immun. 1998, 66:3255-3263.
    • (1998) Infect. Immun. , vol.66 , pp. 3255-3263
    • Rose, F.R.1    Bailey, K.2    Keyte, J.W.3    Chan, W.C.4    Greenwood, D.5
  • 42
    • 0029086411 scopus 로고
    • Evidence for sodium dodecyl sulfate/protein complexes adpting a necklace structure
    • Samsó M., Daban J.R., Hansen S., Jones G.R. Evidence for sodium dodecyl sulfate/protein complexes adpting a necklace structure. Eur. J. Biochem. 1995, 232:818-824.
    • (1995) Eur. J. Biochem. , vol.232 , pp. 818-824
    • Samsó, M.1    Daban, J.R.2    Hansen, S.3    Jones, G.R.4
  • 43
    • 33646569673 scopus 로고    scopus 로고
    • Histone H1 phosphorylation occurs site-specifically during interphase and mitosis: identification of a novel phosphorylation site on histone H1
    • Sarg B., Helliger W., Talasz H., Förg B., Lindner H.H. Histone H1 phosphorylation occurs site-specifically during interphase and mitosis: identification of a novel phosphorylation site on histone H1. J. Biol. Chem. 2006, 281:6573-6580.
    • (2006) J. Biol. Chem. , vol.281 , pp. 6573-6580
    • Sarg, B.1    Helliger, W.2    Talasz, H.3    Förg, B.4    Lindner, H.H.5
  • 44
    • 77950548496 scopus 로고    scopus 로고
    • Dissecting the binding mechanism of the linker histone in live cells: an integrated FRAP analysis
    • 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.
    • (2010) EMBO J. , vol.29 , pp. 1225-1234
    • Stasevich, T.J.1    Mueller, F.2    Brown, D.T.3    McNally, J.G.4
  • 45
    • 0031592945 scopus 로고    scopus 로고
    • Common core structure of amyloid fibrils by synchrotron X-ray diffraction
    • Sunde M., Serpell L.C., Bartlam M., Fraser P.E., Pepys M.B., et al. Common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Biol. 1997, 273:729-739.
    • (1997) J. Mol. Biol. , vol.273 , pp. 729-739
    • Sunde, M.1    Serpell, L.C.2    Bartlam, M.3    Fraser, P.E.4    Pepys, M.B.5
  • 46
    • 0030068951 scopus 로고    scopus 로고
    • In vivo phosphorylation of histone H1 variants during the cell cycle
    • Talasz H., Helliger W., Puschendorf B., Lindner H. In vivo phosphorylation of histone H1 variants during the cell cycle. Biochemistry 1996, 35:1761-1767.
    • (1996) Biochemistry , vol.35 , pp. 1761-1767
    • Talasz, H.1    Helliger, W.2    Puschendorf, B.3    Lindner, H.4
  • 47
    • 19644400009 scopus 로고    scopus 로고
    • The histone H1 C-terminal domain binds to the apoptotic nuclease, DNA fragmentation factor (DFF40/CAD) and stimulates DNA cleavage
    • Widlak P., Kalinowska M., Parseghian M.H., Lu X., Hansen J.C., Garrard W.T. The histone H1 C-terminal domain binds to the apoptotic nuclease, DNA fragmentation factor (DFF40/CAD) and stimulates DNA cleavage. Biochemistry 2005, 44:7871.
    • (2005) Biochemistry , vol.44 , pp. 7871
    • Widlak, P.1    Kalinowska, M.2    Parseghian, M.H.3    Lu, X.4    Hansen, J.C.5    Garrard, W.T.6
  • 48
    • 3543060532 scopus 로고    scopus 로고
    • Interactions of histone H1 with phospholipids and comparison of its binding to giant liposomes and human leukemic T cells
    • Zhao H., Shambhunath B., Tuominen E.K.J., Kinnunen K.J. Interactions of histone H1 with phospholipids and comparison of its binding to giant liposomes and human leukemic T cells. Biochemistry 2004, 43:10192-10202.
    • (2004) Biochemistry , vol.43 , pp. 10192-10202
    • Zhao, H.1    Shambhunath, B.2    Tuominen, E.K.J.3    Kinnunen, K.J.4
  • 49
    • 4043100348 scopus 로고    scopus 로고
    • Formation of amyloid fibers triggered by phosphatidylserine-containing membranes
    • Zhao H., Tuominen E.K.J., Kinnunen K.J. Formation of amyloid fibers triggered by phosphatidylserine-containing membranes. Biochemistry 2004, 43:10302-10307.
    • (2004) Biochemistry , vol.43 , pp. 10302-10307
    • Zhao, H.1    Tuominen, E.K.J.2    Kinnunen, K.J.3
  • 50
    • 0026608073 scopus 로고
    • Environment affects amino acid preference for secondary structure
    • Zhong L., Johnson W.C. Environment affects amino acid preference for secondary structure. Proc. Natl. Acad. Sci. USA 1992, 89:4462-4465.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4462-4465
    • Zhong, L.1    Johnson, W.C.2
  • 51
    • 0033813699 scopus 로고    scopus 로고
    • Linker histone binding and displacement: versatile mechanism for transcripcional regulation
    • Zlatanova J., Caiafa P., van Holde K. Linker histone binding and displacement: versatile mechanism for transcripcional regulation. FASEB J. 2000, 14:1697-1704.
    • (2000) FASEB J. , vol.14 , pp. 1697-1704
    • Zlatanova, J.1    Caiafa, P.2    van Holde, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.