Activation mechanism of the nuclear chaperone nucleoplasmin: Role of the core domain

Journal of Molecular Biology

Volumn 334, Issue 3, 2003, Pages 585-593

  Bañuelos, Sonia ^a,b   Hierro, Aitor ^a,b,d   Arizmendi, Jesús M ^b   Montoya, Guillermo ^c   Prado, Adelina ^a,b   Muga, Arturo ^a,b  

^a CSIC UPV Unidad de Biofisica UBF   (Spain)

^b UNIVERSITY OF THE BASQUE COUNTRY UPV EHU   (Spain)

^c Centro Nacional de Investigaciones Oncológicas   (Spain)

^d NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

Author keywords

Electrostatic potential; Nuclear chaperone; Nucleoplasmin; Protein activation; Protein phosphorylation

Indexed keywords

ASPARTIC ACID; BASIC PROTEIN; CHAPERONE; GLUTAMIC ACID; MUTANT PROTEIN; NUCLEAR PROTEIN; NUCLEOPLASMIN; RECOMBINANT PROTEIN;

ACIDITY; ANIMAL CELL; ARTICLE; BINDING SITE; CHROMATIN CONDENSATION; CONTROLLED STUDY; EGG; ELECTRIC POTENTIAL; FEMALE; GENE MUTATION; MALE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN ISOLATION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; REPRODUCIBILITY; SPERM; XENOPUS LAEVIS;

XENOPUS LAEVIS;

EID: 0242578112     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.09.067     Document Type: Article

References (26)

1. Philpott A., Krude T., Laskey R.A. Nuclear chaperones. Semin. Cell Dev. Biol. 11:2000;7-14.
2. Laskey R.A., Honda B.M., Mills A.D., Finch J.T. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA. Nature. 275:1978;416-420.
3. Dingwall C., Dilworth S.M., Black S.J., Kearsey S.E., Cox L.S., Laskey R.A. Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals. EMBO J. 6:1987;69-74.
4. Hierro A., Arizmendi J.M., De Las Rivas J., Urbaneja M.A., Prado A., Muga A. Structural and functional properties of Escherichia coli-derived nucleoplasmin. A comparative study of recombinant and natural proteins. Eur. J. Biochem. 268:2001;1739-1748.
5. Saperas N., Chiva M., Aligué R., Itoh T., Katagiri C., Subirana J.A., Ausió J. Physicochemical and functional characterization of Xenopus laevis nucleoplasmin obtained from oocytes and from overexpression in bacteria. Arch. Biochem. Biophys. 361:1999;135-141.
6. Hierro A., Arizmendi J.M., Bañuelos S., Prado A., Muga A. Electrostatic interactions at the C-terminal domain of nucleoplasmin modulate its chromatin decondensation activity. Biochemistry. 41:2002;6408-6413.
7. Dutta S., Akey I.V., Dingwall C., Hartman K.L., Laue T., Nolte R.T., et al. The crystal structure of nucleoplasmin-core: implications for histone binding and nucleosome assembly. Mol. Cell. 8:2001;841-853.
8. Namboodiri V.M., Dutta S., Akey I.V., Head J.F., Akey C.W. The crystal structure of Drosophila NLP-core provides insight into pentamer formation and histone binding. Structure. 11:2003;175-186.
9. Leno G.H., Mills A.D., Philpott A., Laskey R.A. Hyperphosphorylation of nucleoplasmin facilitates Xenopus sperm decondensation at fertilization. J. Biol. Chem. 271:1996;7253-7256.
10. Cotten M., Sealy L., Chalkley R. Massive phosphorylation distinguishes Xenopus laevis nucleoplasmin isolated from oocytes or unfertilized eggs. Biochemistry. 25:1986;5063-5069.
11. Philpott A., Leno G.H. Nucleoplasmin remodels sperm chromatin in Xenopus egg extracts. Cell. 69:1992;759-767.
12. Mann M., Risley M.S., Eckhardt R.A., Kasinsky H.E. Characterization of spermatid/sperm basic chromosomal proteins in the genus Xenopus (Anura, Pipidae). J. Expt. Zool. 173:1982;86.
13. Delmolino L.M., Saha P., Dutta A. Multiple mechanisms regulate subcellular localization of human CDC6. J. Biol. Chem. 276:2001;26947-26954.
14. Xiao C.Y., Jans P., Jans D.A. Negative charge at the protein kinase CKII site enhances recognition of the SV40 large T-antigen NLS by importin: effect of conformation. FEBS Letters. 440:1998;297-301.
15. Blom N., Gammeltoft S., Brunak S. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J. Mol. Biol. 294:1999;1351-1362.
16. Gurdon J.B., Wickens M.P. The use of Xenopus oocytes for the expression of cloned genes. Methods Enzymol. 101:1983;370-386.
17. Leno G.H. Cell-free systems to study chromatin remodeling. Methods Cell Biol. 53:1998;497-515.
18. Vancurova S., Paine T.M., Lou W., Paine P.L. Nucleoplasmin associates with and is phosphorylated by casin kinase II. J. Cell Sci. 108:1995;779-787.
19. Fujii-Nakata T., Ishimi Y., Okuda A., Kikuchi A. Functional analysis of nucleosome assembly protein, NAP-1. The negatively charged COOH-terminal region is not necessary for the intrinsic assembly activity. J. Biol. Chem. 267:1992;20980-20986.
20. Akey C.W., Luger K. Histone chaperones and nucleosome assembly. Curr. Opin. Struct. Biol. 13:2003;6-14.
21. Haavik J., Martínez A., Flatmark T. pH-dependent release of catecholamines from tyrosine hydroxylase and the effect of phosphorylation of Ser-40. FEBS Letters. 262:1990;363-365.
22. Zweidler A. Resolution of histones by polyacrylamide gel electrophoresis in presence of nonionic detergents. Methods Cell Biol. 17:1978;223-233.
23. Robertson E.F., Dannelly H.K., Malloy P.J., Reeves H.C. Rapid isoelectric focusing in a vertical polyacrylamide minigel system. Anal. Biochem. 167:1987;290-294.
24. Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
25. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstieve R.W., et al. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallog. sect. D, Biol. Crystallog. 54:1998;905-921.
26. Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.