Nucleolar protein B23 has molecular chaperone activities

Protein Science

Volumn 8, Issue 4, 1999, Pages 905-912

  Szebeni, Attila ^a   Olson, Mark O J ^a  

^a UNIVERSITY OF MISSISSIPPI MEDICAL CENTER   (United States)

Author keywords

HIV 1 Rev protein; Molecular chaperone; Nucleolar protein B23; Protein denaturation; Protein folding

Indexed keywords

ALCOHOL DEHYDROGENASE; CARBOXYPEPTIDASE A; CELL PROTEIN; CHAPERONE; CITRATE SYNTHASE; PHOSPHOPROTEIN; REV PROTEIN; THIOSULFATE SULFURTRANSFERASE;

ARTICLE; ENZYME ACTIVITY; ENZYME SUBSTRATE COMPLEX; HUMAN IMMUNODEFICIENCY VIRUS 1; LIGHT SCATTERING; NUCLEOLUS; POLYMERIZATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN DENATURATION; PROTEIN DETERMINATION; PROTEIN FOLDING; PROTEIN LOCALIZATION; STOICHIOMETRY; STRUCTURE ACTIVITY RELATION; TEMPERATURE DEPENDENCE;

EID: 0032917157     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.8.4.905     Document Type: Article

References (44)

1. Borer RA, Lehner CF, Eppenberger HM, Nigg EA. 1989. Major nucleolar proteins shuttle between nucleus and cytoplasm. Cell 56:379-390.
2. Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
3. Buchner J. 1996. Supervising the fold: Functional principles of molecular chaperones. FASEB J 10:10-19.
4. Buchner JB, Grallert H, Jacob U. 1998. Analysis of chaperone function using citrate synthase as nonnative substrate protein. Methods Enzymol 290:323-338.
5. Busch H, Smetana K. 1970. The nucleolus. New York: Academic Press.
6. Campbell KS, Mullane KP, Aksoy IA, Stubdal H, Zalvide J, Pipas JM, Silver PA, Roberts TM, Schaffhausen BS, DeCaprio JA. 1997. DnaJ/hsp40 chaperone domain of SV40 large T antigen promotes efficient viral DNA replication. Genes Develop 17:1098-1110.
7. Chan WY, Liu QR, Borjigin J, Busch H, Rennert OM, Tease LA, Chan PK. 1989. Characterization of the cDNA encoding human nucleophosmin and studies of its role in normal and abnormal growth. Biochemistry 28:1033-1039.
8. Chang JH, Lin JY, Wu MH, Yung BYM. 1998. Evidence for the ability of nucleophosmin/B23 to bind ATP. Biochem J 329:539-544.
9. Chang J-H, Olson MOJ. 1990. Structure of the gene for rat nucleolar protein B23. J Biol Chem 265:18227-18233.
10. Eichler DC, Craig N. 1994. Processing of eukaryotic ribosomal RNA. Prog Nucleic Acid Res Mol Biol 49:197-239.
11. Ellis RJ. 1997. Molecular chaperones: Avoiding the crowd. Curr Biol 7:R531-R533.
12. Fankhauser C, Izaurralde E, Adachi Y, Wingfield P, Laemmli UK. 1991. Specific complex of human immunodeficiency virus type I rev and nucleolar protein B23 proteins: Dissociation by the rev response element. Mol Cell Biol 11:2567-2575.
13. Fedorov AN, Baldwin TO. 1997. Cotranslational protein folding. J Biol Chem 272:32715-32718.
14. Feuerstein N, Mond JJ. 1987. Identification of a prominent nuclear protein associated with proliferation of normal and malignant B cells. J Immunol 139:1818-1822.
15. Goldfarb DS. 1988. Karyophilic peptides: Applications to the study of nuclear transport. Cell Biol Intern Rep 128:809-832.
16. Guagliardi A, Cerchia L, Rossi M. 1995. Prevention of in vitro protein thermal aggregation by the Sulfolobus solfataricus chaperonin. Evidence for non-equivalent binding surfaces on the chaperonin molecule. J Biol Chem 270:28126-28132.
17. Hadjiolov AA. 1984. The nucleolus and ribosome biogenesis. New York: Springer-Verlag.
18. Hendrick JP, Hartl F-U. 1995. The role of molecular chaperones in protein folding. FASEB J 9:1559-1569.
19. Jaenicke R, Rudolph R. 1990. Folding proteins. In: Creighton TE, ed. Protein structure a practical approach. Oxford, UK: IRL Press. pp 191-223.
20. Jakob U, Buchner J. 1994. Assisting spontaneity - The role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem Sci 19:205-211.
21. Jakob U, Gaestel M, Engel K, Buchner J. 1993. Small heat shock proteins are molecular chaperones. J Biol Chem 268:1517-1520.
22. Karn J, Churcher MJ, Rittner K, Kelley A, Butler PJG, Mann DA, Gait MJ. 1995. RNA binding assays for the regulatory proteins Tat and Rev. In: Karn J, eds. HIV a practical approach, biochemistry, molecular biology and drug discovery. Vol. 2. Oxford, UK: IRL Press, pp 147-165.
23. Li Y-P, Busch RK, Valdez BC, Busch H. 1996. C23 interacts with B23, a putative nudeolar-localization-signal-binding protein. Eur J Biochem 237: 153-158.
24. Martin J, Langer T, Toteva R, Schramel A, Horwich AL, Hartl FU. 1991. Chaperonin-mediated protein folding at the surface of groEL through a molten globule-like intermediate. Nature 352:36-42.
25. Mock DM, Lankford G, Horowitz P. 1988. A study of the interaction of avidin with 2-anilinonaphthalene-6-sulfonic acid as a probe of the biotin binding site. Biochim Biophys Acta 950:23-29.
26. Moss T, Stefanovsky VY. 1995. Promotion and regulation of ribosomal transcription in eukaryotes by RNA polymerase I. Prog Nucleic Acid Res Mol Biol 50:25-66.
27. Muchowski PJ, Bassuk JA, Lubsen NH, Clark JH. 1997. Human B-crystallin. Small heat shock protein and molecular chaperone. J Biol Chem 272:2578-2582.
28. Norcum M. 1996. Novel isolation method and structural stability of a eucaryotic chaperonin: The TCP-1 ring complex from rabbit reticulocytes. Protein Sci 5:1366-1375.
29. Olson MOJ. 1990. The role of proteins in nucleolar structure and function. In: Strauss PR. Wilson SH, eds. The eukaryotic nucleus: Molecular biochemistry and macromolecular assemblies, Vol 2. West Caldwell, NJ: Telford Press. pp 541-546.
30. Olson MOJ, Wallace MO, Herrera AH, Marshall-Carlson L, Hunt RC. 1986. Preribosomal ribonucleoprotein particles are a major component of a nucleolar matrix fraction. Biochemistry 25:484-491.
31. Ruddon RW, Bedows E. 1997. Assisted protein folding. J Biol Chem 272:3125-3128.
32. Schmidt-Zachmann MS, Hugle-Dorr B, Franke W. 1987. A constitutive nucleolar protein identified as a member of the nucleoplasmin family. EMBO J 6:1881-1890.
33. Shan X, Xue Z, Melese T. 1994. Yeast NP146 encodes a novel prolyl cis-trans isomerase that is located in the nucleolus. J Cell Biol 120:853-862.
34. Szebeni A, Herrera JE, Olson MOJ. 1995. Interaction of nucleolar protein B23 with peptides related to nuclear localization signals. Biochemistry 34:8037-8042.
35. Szebeni A, Mehrotra B, Baumann A, Adam SA, Wingfield PT, Olson MO. 1997. Nucleolar protein B23 stimulates the nuclear import of the HIV-1 Rev protein and NLS-conjugated albumin. Biochemistry 36:3941-3949.
36. Taguchi T, Yoshida M. 1998. Chaperonin from thermophile Thermos thermophilus. Methods Enzymol 290:169-180.
37. Theopold U, Dal Zotto L, Hultmark D. 1995. FKBP39, a Drosophila member of a family of proteins that bind the immunosuppressive drug FK506. Gene 156:247-251.
38. Umekawa H, Chang JH, Correia J, Wang D, Wingfield PT, Olson MOJ. 1993. Nucleolar protein B23: Bacterial expression, purification, oligomerization and secondary structures of two isoforms. Cell Mol Biol Res 39:635-645.
39. Valdez BC, Perlaky L, Henning D, Saijo Y, Chan PK. 1994. Identification of the nuclear and nucleolar localization signals of the protein p120. J Biol Chem 269:23776-23783.
40. Warner JR. 1990. The nucleolus and ribosome formation. Curr Opin Cell Biol 2:521-527.
41. Welch WJ, Feramisco JR. 1984. Nuclear and nucleolar localization of the 72,000 dalton heat shock protein in heat shocked mammalian cells. J Biol Chem 259:4501-4513.
42. Wiech H, Buchner J, Zimmermann R, Jakob U. 1992. Hsp90 chaperones protein folding in vitro. Nature 355:169-170.
43. Wingfield PT, Stahl SJ, Payton MA, Venkatesan S, Misra M, Steven AC. 1991. HIV-1 Rev expressed in recombinant E. coli: Purification, polymerization, and conformational properties. Biochemistry 30:7527-7534.
44. Zimmerman SB, Minton AP. 1993. Macromolecular crowding: Biochemical, biophysical, and physiological consequences. Ann Rev Biophys Biomol Struct 22:27-65.