An abundant nucleolar phosphoprotein is associated with ribosomal DNA in Tetrahymena macronuclei

Molecular Biology of the Cell

Volumn 8, Issue 1, 1997, Pages 97-108

  McGrath, Kathleen E ^a   Smothers, James F ^a   Dadd, Christopher A ^a   Madireddi, Malavi T ^a   Gorovsky, Martin A ^a   Allis, C David ^a  

^a UNIVERSITY OF ROCHESTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOLIN; RIBOSOME DNA;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CROSS LINKING; DNA METABOLISM; ENZYME REGULATION; IMMUNOCYTOCHEMISTRY; MACRONUCLEUS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; RIBOSOME SUBUNIT; RNA PROCESSING; TETRAHYMENA; TRANSCRIPTION REGULATION;

MYXOZOA; PROTOZOA; TETRAHYMENA; TETRAHYMENA THERMOPHILA; VERTEBRATA;

EID: 0030747783     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.8.1.97     Document Type: Article

References (46)

1. Allis, CD., and Dennison, D.K.. 1982. Identification and purification of young macronuclear anlagen from conjugating cells of Tetrahymena thermophila. Dev. Biol. 93, 519-533.
2. cdc2 protein kinase. Mol. Cell. Biol. 10, 3607-3618.
3. Bouche, G., Caizergues-Ferrer, M., Bugler, B., and Amalric, F. (1984). Interrelations between the maturation of a 100 kDa nucleolar protein and pre-rRNA synthesis in CHO cells. Nucleic Acids Res. 12, 3025-3035.
4. Burd, C.G., and Dreyfuss, G. (1994). Conserved structures and diversity of functions of RNA-binding proteins. Science 265, 615-621.
5. Colavito-Shepanski, M., and Gorovsky, M.A. (1983). The histone ntentof of Tetrahymena ribosomal gene-containing chromatin. J. Biol. Chem. 258, 5944-5954.
6. Creancier, L., Prats, H., Zanibellato, C., Amalric, F., and Bugler, B. (1993). Determination of the functional domains involved in nucleolar targeting of nucleolin. Mol. Biol. Cell 4, 1239-1250.
7. Dadd, C.A., Cook, R.G., and Allis, C.D. (1993). Fractionation of small trypic phosphopeptides by alkaline PAGE followed by amino acid sequencing. Biotechniques 14, 266-273.
8. Dedon, P.C., Soults, J.A., Allis, C.D., and Gorovsky, M.A. (1991a). Formaldehyde cross-linking and immunoprecipitation demonstrate developmental changes in H1 association with transcriptionally active genes. Mol. Cell. Biol. 11, 1729-1733.
9. Dedon, P.C., Soults, J.A., Allis, C.D., and Gorovsky, M.A. (1991b). A simplified formaldehyde fixation and immunoprecipitation technique for studying protein-DNA interactions. Anal. Biochem. 197, 83-90.
10. Dingwall, C., Dilworth, S.M., Black, S.J., Kearsy, S.E., Cox, L.S., and Laskey, R.A. (1987). Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals. EMBO J. 6, 69-74.
11. Egyhazi, E., Pigon, A., Chang, J.-H., Ghaffari, S.H., Dreesen, T.D., Wellman, S.E., Case, S.T., and Olson, M.O.J. (1988). Effects of anti-C23 (nucleolin) antibody on transcription ot ribosomal DNA in Chironomus salivary gland cells. Exp. Cell Res. 178, 264-272.
12. Engberg, J., and Nielsen, H. (1990). Complete sequence of the extrachromosomal rDNA molecule from the ciliate Tetrahymena thermophila strain B1868VII. Nucleic Acids Res. 18, 6915-6919.
13. Erard, M., Lakhdar-Ghazal, F., and Amalric, F. (1990). Repeat peptide motifs which contain b-turns and modulate DNA condensation in chromatin. Eur. J. Biochem. 191, 19-26.
14. Erard, M.S., Belenguer, P., Caizergues-Ferrer, M., Pantaloni, A., and Amalric, F. (1988). A major nucleolar protein, nucleolin, induces chromatin decondensation by binding to histone H1. Eur. J. Biochem. 175, 525-530.
15. Frohman, M.A., Dush, M.K., and Martin, G.R. (1988). Rapid production of full-length cDNAs from rare transcripts: Amplification using a single gene-specific oligonucleotide primer. Proc. Natl. Acad. Sci. USA 85, 8998-9002.
16. Gaertig, J., and Gorovsky, M.A. (1992). Efficient mass transformation of Tetrahymena thermophila by electroporation ot conjugants. Proc. Natl. Acad. Sci. USA 89, 9196-9200.
17. Ghisolfi-Nieto, L., Joseph, G., Puvion-Dutilleul, F., Amalric, F., and Bouvet, P. (1996). Nucleolin is a sequence-specific RNA-binding protein: characterization of targets on pre-ribosomal RNA. J. Mol. Biol. 260, 34-53.
18. Ghisolfi, L., Joseph, G., Amalric, F., and Erard, M. (1992). The glycine-rich domain of nucleolin has an unusual supersecondary structure responsible for its RNA-helix-destabilizing properties. J. Biol. Chem. 267, 2955-2959.
19. Gorovsky, M.A. (1973). Macro- and micronuclei of Tetrahymena pyriformis: A model system for studying the structure and function of eukaryotic nuclei. J. Protozool. 20, 19-25.
20. Gorovsky, M.A., Yao, M.-C., Keevert, J.B., and Pleger, G.L. (1975). Isolation of micro- and macronuclei of Tetrahymena pyriformis. In: Methods in Cell Biology, ed. P.M. Prescott, New York: Academic Press, 311-327.
21. Herrera, A.H., and Olson, M.O.J. (1986). Associalation of protein C23 with rapidly labeled nucleolar RNA. Biochemistry 25, 6258-6264.
22. Jordan, G. (1987). At the heart of the nucleolus. Nature 329, 489-490.
23. Kondo, K., and Inouye, M. (1992). Yeast NSR1 protein that has structural similarity to mammalian nucleolin is involved in prerRNA processing. J. Biol. Chem. 267, 16252-16258.
24. Lapevre, B., Bourbon, H., and Amalric, F. (1987) Nucleolin, the major nucleolar protein of growing eukaryotic cells: An unusual protein structure revealed by the nucleotide sequence. Proc. Natl. Acad. Sci. USA 84, 1472-1476.
25. Lee, W.-C., Zabetakis, D., and Mélèse, T. (1992). NSR1 is required for pre-RNA processing and for the proper maintenance of steady-state levels of ribosomal subunits. Mol. Cell. Biol. 12, 3865-3871.
26. Lee, W.C., Xue, Z., and Mélèse, T. (1991). The NSR1 gene encodes a protein that specifically binds nuclear localization sequences and has two RNA recognition motifs. J. Cell Biol. 113, 1-12.
27. n single strand telomeric DNA in vitro. Nucleic Acids Res. 22, 4906-4913.
28. Madireddi, M.T., Davis, M.C., and Allis, C.D. (1994). Identification of a novel polypeptide involved in the formation of DNA-containing vesicles during macronuclear development in Tetrahymena. Dev. Biol. 165, 418-431.
29. Maridor, G., Krek, W., and Nigg, E.A. (1990). Structure and developmental expression of chicken nucleohn and NO38: coordinate expression of two abundant non-ribosomal nucleolar proteins. Biochim. Biophys. Acta 1049, 126-133.
30. Marin, O., Meggio, F., Marchiori, F., Borin, G., and Pinna, L.A. (1986). Sit specificity of casein kinase-2 (TS) from rat liver cytosol: A study with model peptide substrates. Eur. J. Biochem. 160, 239-244.
31. Meggio, F., and Pinna, L.A. (1988). Phosphorylation of phosvitin by casein kinase-2 provides the evidence that phosphoserines can replace carboxylic amino acids as specificity determinants. Biochim. Biophys. Acta 971, 227-231.
32. Meier, U.T., and Blobel, G. (1992). Nopp140 shuttles on tracks between nucleolus and cytoplasm. Cell 70, 1-20.
33. Olmsted, J.B. (1981). Affinity purification of antibodies from diazotized paper blots of heterogeneous protein samples. J. Biol. Chem. 256, 11955-11957.
34. Prescott, D.M. (1994). The DNA of ciliated protozoa. Microbiol. Rev. 58, 233-267.
35. Roth, S.Y., Schulman, I.G., Richman, R., Cook, R.G., and Allis, C.D. (1988). Characterization of phosphorylation sites in histone H1 in the amitotic macronucleus of Tetrahymena during different physiological states. J. Cell Biol. 107, 2473-2482.
36. Sapp, M., Richter, A., Weisshart, K., Caizergues-Ferrer, M., Amalric, F., Wallace, M.O., Kirstein, M.N., and Olson, M.O.J. (1989). Characterization of a 48-kDa nucleic-acid-binding fragment of nucleolin. Eur. J. Biochem. 179, 541-548.
37. Scheer, U., and Weisenberger, D. (1994). The nucleolus. Curr. Biol. 6, 354-359.
38. Schulman, I.G., Cook, R.G., Richman, R., and Allis, C.D. (1987). Tetrahymena contain two distinct and unusual high mobility group (HMG)-like proteins. J. Cell Biol. 104, 1485-1494.
39. Shan, X., Xue, Z., and Melese, T. (1994). Yeast NPI46 encodes a novel prolyl cis-trans isomerase that is located in the nucleolus. J. Cell Biol. 126, 853-862.
40. Stargell, L.A., Karrer, K.M., and Gorovsky, M.A. (1990). Transcriptional regulation of gene expression in Tetrahymena thermophila. Nucleic Acids Res. 18, 6637-6639.
41. Stargell, L.A., Bowen, J., Dadd, C.A., Dedon, P.C., Davis, M., Cook, R.G., Allis, C.D. and Gorovsky, M.A. (1993). Temporal and spatial association of histone H2A variant hvl with transcriptionally competent chromatin during macronuclear development in Tetrahymena thermophila. Genes Dev. 7, 2641-2651.
42. Wenkert, D., and Allis, C.D. (1984). Timing of the appearance of macronuclear-specific histone variant hv1 and gene expression in developing new macronuclei of Tetrahymena thermophila. J. Cell. Biol. 98, 2107-2117.
43. White, E.M., Allis, C.D., Goldfarb, D.S., Srivastva, A., Weir, J.W., and Gorovsky, M.A. (1989). Nucleus-specific and temporally restricted localization of proteins in Tetrahymena macronuclei and micronuclei. J. Cell Biol. 109, 1983-1992.
44. Yan, C., and Melese, T. (1993). Multiple regions of NSR1 are sufficient for accumulation of a fusion protein within the nucleolus. J. Cell Biol. 123, 1081-1091.
45. Yao, M.C., and Yao, C.H. (1991). Transformation of Tetrahymena to cycloheximide resistance with a ribosomal protein gene through sequence replacement. Proc. Natl. Acad. Sci. USA 88, 9493-9497.
46. Yu, G.L., Hasson, M., and Blackburn, E.H. (1988). Circular ribosomal DNA plasmids transform Tetrahymena thermophila by homologous recombination with endogenous macronuclear ribosomal DNA. Proc. Natl. Acad. Sci. USA 85, 5151-5155.