Self-association of Chaetopterus variopedatus sperm histone H1-like. Relevance of arginine content and possible physiological role

• Autorzy: Salvati D. , Conforti S. , Conte M. , Matassa D.S. , Fucci L. , Piscopo M.
• Języki publikacji: EN

Abstrakty

EN

Self-association of histones H1 from calf thymus and from sperm of the marine worm Chaetopterus variopedatus was studied on native and glutaraldehyde cross-linked molecules by PAGE and by salt-induced turbidity measurements. Multiple polymers were generated by native sperm histone H1-like after glutaraldehyde cross-linking while the same treatment on its lysine- or arginine-modified derivatives and on somatic histone H1 failed to induce polymerization. This result suggests the relevance of arginine content in the formation of histone H1-like polymers particularly because Chaetopterus variopedatus and calf thymus histones H1 have similar content of lysine but different K/R ratio (2 and 15, respectively). Salt-induced turbidity experiments confirmed the high tendency of sperm histone H1-like to form oligomers, particularly in the presence of phosphate ions. Native PAGE analysis in the presence of phosphate supported this hypothesis. The reported results suggest that phosphate ions connecting lysine and arginine side chain groups contribute to the interaction of sperm histone H1-like with DNA in chromatin and mplay a key role in organization and stabilization of the chromatin higher order structures.

Słowa kluczowe

PL

histone H1; arginine; physiological role; marine worm; Chaetopterus variopedatus; sperm

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2008
• Tom: 55
• Numer: 4
• Opis fizyczny: p.701-706,fig.,ref.

Twórcy

autor

Salvati D.

• University of Naples Federico II, Via Cinthia, 80126 Napoli, Italy

autor

Conforti S.

autor

Conte M.

autor

Matassa D.S.

autor

Fucci L.

autor

Piscopo M.

Bibliografia

• Ali Z, Singh N (1987) Binding of linker histones to the core nucleosome. J Biol Chem 262:12989-12993.
• Ausio J (1992) Presence of a highly specific histone H1-like protein in the chromatin of the sperm of the bivalve mollusks. Mol Cell Biochem 115:163-172.
• Carter GJ, van Holde K (1998) Self-association of linker histone h5 and of its globular domain: evidence for specific self-contacts. Biochemistry 37:12477-12488.
• De Petrocellis B, Parente A, Tomei L, Geraci G (1983) An histone H1 and a protamine molecule organize the sperm chromatin of the marine worm C. variopedatus. Cell Differ 12:129-135.
• Draves PH, Lowary PT, Widom J (1992) Co-operative binding of the globular domain of histone H5 to DNA. J Mol Biol 225:1105-1121.
• Dubochet J, Noll M (1978) Nucleosome arcs and helices. Science 202:280-286.
• Giancotti V, Cosimi S, Cary PD, Crane-Robinson C, Geraci G (1981) Preparation and characterization of histone H1 from the sperm of the sea-urchin Sphaerechinus granularis. Biochem J 195: 171-176.
• Grau LP, Azorin F, Subirana JA (1982) Aggregation of mono- and dinucleosomes into chromatin-like fibers. Chromosoma 87:437-445.
• Itoh T, Ausio J, Katagiri C (1997) Histone H1 variants as sperm-specific nuclear proteins of Rana catesbeiana, and their role in maintaining a unique condensed state of sperm chromatin. Mol Reprod Dev 47:181-190.
• Johns EW (1971) in Histones and nucleohistones. Phillips DMP, ed, pp 61-67. Plenum Press, New York.
• Kasinsky HE, Huang SY, Mann M, Roca J, Subirana JA (1985) On the diversity of sperm histones in the vertebrates: IV. Cytochemical and amino acid analysis in Anura. J Exp Zool 234:33-46.
• Lewis JD, Ausio J (2002) Protamine-like proteins: evidence for a novel chromatin structure. Biochem Cell Biol 80:353-361.
• Lewis JD, Saperas N, Song Y, Zamora MJ, Chiva M, Ausio J (2004) Histone H1 and the origin of protamines. Proc Natl Acad Sci USA 101:4148-4152.
• Maman JD, Yager TD, Allan J (1994) Self-association of the globular domain of histone H5. Biochemistry 33:1300-1310.
• McIntosh DB (1992) Glutaraldehyde cross-links Lys-492 and Arg-678 at the active site of sarcoplasmic reticulum Ca2+-ATPase. J Biol Chem 267:22328-22335.
• Panyim S, Chalkley R (1969) High resolution acrylamide gel electrophoresis of histones. Arch Biochem Biophys 130:337-346.
• Piscopo M, Tomei L, De Petrocellis L, Geraci G (1993) Anion-mediated lysine-arginine interaction. Evidence in Chaetopterus variopedatussperm protamine. FEBS Lett 334:125-127.
• Piscopo M, De Petrocellis L, Conte M, Pulcrano G, Geraci G (2006) On the possibility that H1 histone interaction with DNA occurs through phosphates connecting lysine and arginine side chain groups. Acta Biochim Polon 53:507-513.
• Russo E, Giancotti V, Crane-Robinson C, Geraci G (1983) Histone H1 and chromatin higher order structure. Does histone H1 exhibit specific self-association? Int J Biochem 15:487-493.
• Saperas N, Chiva M, Pfeiffer DC, Kasinsky HE, Ausio J (1994) Sperm nuclear basic proteins (SNBPs) of agnathans and chondrichthyans: variability and evolution of sperm proteins in fish. J Mol Evol 44:422-431.
• Segers A, Muyldermans S, Wyns L (1991) The interaction of histone H5 and its globular domain with core particles, depleted chromatosomes, polynucleosomes, and a DNA decamer. J Biol Chem 266:1502-1508.
• Strickland WN, Strickland M, Brandt WF, Von Holt C, Lehmann A, Wittmann-Liebold B (1980) The primary structure of histone H1 from sperm of the sea urchin Parechinus angulosus. 2. Sequence of the C-terminal CNBr peptide and the entire primary structure. Eur J Biochem 104:567-578.
• Thomas JO, Rees C, Finch JT (1992) Cooperative binding of the globular domains of histones H1 and H5 to DNA. Nucleic Acids Res 20:187-194.
• Wang D (1976) Preparation of cross-linked dimers of pancreatic ribonuclease. Biochemistry 15:660-665.
• Watson CE, Davies PL (1998) The high molecular weight chromatin proteins of winter flounder sperm are related to an extreme histone H1 variant. J Biol Chem 273:6157-6162