Abstract
Nucleolin is a key nucleolar protein in higher eukaryotic cells and is involved directly in ribosome biogenesis. Using an antiserum raised against hamster nucleolin, the homologous protein was detected in nucleoli of Xenopus laevis hepatocytes as well as in the amplified nucleoli of oocytes. A cDNA encoding Xenopus nucleolin has been isolated and sequenced. The deduced protein sequence reveals similar domains in Xenopus and in mammals, but they have undergone separate evolutions. In particular, each of the four RNA-binding domains has evolved differently--the carboxy-proximal domain is twice as conserved (87%) as the amino-proximal domain (42%). These data shed some light on the possible roles of each domain. The expression of nucleolin has been followed throughout oogenesis and embryogenesis. The appearance of nucleolin during early development precedes the transcription of rDNA and the synthesis of ribosomal proteins. The maximal accumulation of nucleolin at gastrulation coincides with nucleolar reformation. Furthermore, when ribosomal synthesis is activated during oogenesis and embryogenesis, peptides immunorelated to nucleolin appear and accumulate. The results suggest that nucleolin plays a role not only in ribosome assembly but also in nucleologenesis.
References
52
Referenced
74
10.1083/jcb.105.4.1483
10.1093/nar/12.7.3025
10.1073/pnas.84.19.6770
10.1007/BF00777472
10.1016/0022-2836(88)90476-7
{'key': '2021111319543999000_3.3.324.6', 'first-page': '37', 'article-title': 'Nucleolin, a RNA binding protein involved in biosynthesis of preribosomes in eukaryotes.', 'volume': '404', 'year': '1988', 'journal-title': 'J. Cell. Biochem. UCLA Symp.'}
/ J. Cell. Biochem. UCLA Symp. / Nucleolin, a RNA binding protein involved in biosynthesis of preribosomes in eukaryotes. (1988)10.1111/j.1432-1033.1982.tb06989.x
/ Eur. J. Biochem. / Detection and localization of a class of proteins immunologically related to a 100 kD nucleolar protein. (1982)10.1016/S0021-9258(18)60904-4
/ J. Biol. Chem. / RNA binding fragments from nucleolin contain the ribonucleoprotein consensus sequence. (1987)10.1101/gad.1.1.97
10.1016/0012-1606(82)90052-5
10.1016/0006-291X(84)91323-8
10.1021/bi00398a051
10.1002/prot.340010302
{'key': '2021111319543999000_3.3.324.14', 'first-page': '3636', 'article-title': 'Structure of rodent helix-stabilizing protein revealed by cDNA cloning.', 'volume': '261', 'year': '1986', 'journal-title': 'J. Biol. Chem.'}
/ J. Biol. Chem. / Structure of rodent helix-stabilizing protein revealed by cDNA cloning. (1986)- Davidson, E.H. 1986. Gene activity in early development 3rd edition, pp. 160â163. Academic Press, New York.
10.1016/0092-8674(87)90587-3
10.1002/j.1460-2075.1987.tb04720.x
/ EMBO J. / Nucleoplasmin cDNA sequence reveals polyglutamic acid tracts and a cluster of sequences homologous to putative nuclear localization signals. (1987)10.1002/jmor.1051360203
10.1083/jcb.105.4.1479
10.1111/j.1432-1033.1988.tb14224.x
/ Eur. J. Biochem. / A major nucleolar protein, nucleolin, induces chromatin decondensation by binding of hisotne H1. (1988)10.1016/0014-4827(85)90092-8
10.1073/pnas.83.17.6450
10.1111/j.1768-322X.1985.tb00369.x
/ Biol. Cell / Immunolocalization of 100 kDa nucleolar protein during the mitotic cycle in CHO cells. (1985)-
Hadjiolov, A.A. 1985. The nucleolus and ribosome biogenesis. In Cell biology monographs, vol. 12, pp. 133â165. Springer, New York.
(
10.1007/978-3-7091-8742-5_7
) 10.1242/jcs.2.2.151
/ J. Cell Sci. / Fine structure of the nucleolus in normal and mutant Xenopus embryos. (1967)10.1021/bi00368a063
10.1002/j.1460-2075.1988.tb02988.x
/ EMBO J. / Hyperphosphorylation of N-60, a protein structurally and immunologically related to nucleolin after tumour promoter treatment. (1988)10.1016/0092-8674(84)90457-4
10.1016/0014-5793(84)81373-3
10.1002/j.1460-2075.1986.tb04681.x
/ EMBO J. / Molecular characterization of a karyophilic histone binding protein: cDNA cloning, aminoacid sequence and expression of nuclear protein N1/N2 of Xenopus laevis. (1986){'key': '2021111319543999000_3.3.324.31', 'first-page': '680', 'article-title': 'Cleavage of structural protein during the assembly of the head of bacteriophage T4.', 'volume': '256', 'year': '1970', 'journal-title': 'Nature'}
/ Nature / Cleavage of structural protein during the assembly of the head of bacteriophage T4. (1970)10.1093/nar/13.16.5805
10.1016/S0021-9258(18)67634-3
/ J. Biol. Chem. / Protein and cDNA sequence of a glycine-rich dimethylarginine containing region located near the carboxyl-terminal end of nucleolin. (1986)10.1073/pnas.84.6.1472
10.1016/S0021-9258(17)38718-5
/ J. Biol. Chem. / Purification and partial characterization of a nucleolar scleroderma antigen (Mr 34,000; pl, 8.5) rich in dimethylarginine. (1985){'key': '2021111319543999000_3.3.324.36', 'first-page': '1051', 'article-title': 'Effets biologiques de solution de protéines chromatiniennes non histones sur un système embryonnaire en différentiation in vitro.', 'volume': '33', 'year': '1975', 'journal-title': 'J. Embryol. Exp. Morphol.'}
/ J. Embryol. Exp. Morphol. / Effets biologiques de solution de protéines chromatiniennes non histones sur un système embryonnaire en différentiation in vitro. (1975)10.1016/S0076-6879(80)65059-9
/ Methods Enzymol. / Sequencing end labeled DNA with base specific chemical cleavages. (1980)- Nieuwkoop, P.D. and J. Faber. 1956. Normal table of Xenopus laevis (Daudin). North Holland, Amsterdam.
10.1007/BF00327463
10.1021/bi00282a023
10.1073/pnas.70.5.1316
10.1016/0006-291X(83)90387-X
10.1016/0092-8674(82)90022-8
10.1016/S0092-8674(85)80127-6
10.1016/0022-2836(79)90173-6
10.1093/nar/8.20.4613
10.1073/pnas.74.12.5463
10.1093/nar/14.17.6803
10.1002/j.1460-2075.1987.tb02447.x
/ EMBO J. / A constitutive nucleolar protein identified as a member of the nucleoplasmin family. (1987)10.1016/S0021-9258(17)39562-5
/ J. Biol. Chem. / Effects of androgen and polyamines on the phosphorylation of nucleolar proteins from rat ventral prostates with particular reference to a 110-kDa phosphoprotein. (1985)10.1073/pnas.77.9.5201
-
Walker, J.M. 1982. Primary structures In The HMG chromosomal proteins. (ed. E.W. Johns), pp. 69â87. Academic Press, London.
(
10.1016/B978-0-12-386050-7.50009-5
)
Dates
Type | When |
---|---|
Created | 18 years, 2 months ago (June 5, 2007, 5:15 p.m.) |
Deposited | 1 year, 6 months ago (Feb. 14, 2024, 4:26 p.m.) |
Indexed | 2 weeks, 5 days ago (Aug. 5, 2025, 9:01 a.m.) |
Issued | 36 years, 5 months ago (March 1, 1989) |
Published | 36 years, 5 months ago (March 1, 1989) |
Published Online | 36 years, 5 months ago (March 1, 1989) |
Published Print | 36 years, 5 months ago (March 1, 1989) |
@article{Caizergues_Ferrer_1989, title={Nucleolin from Xenopus laevis: cDNA cloning and expression during development.}, volume={3}, ISSN={1549-5477}, url={http://dx.doi.org/10.1101/gad.3.3.324}, DOI={10.1101/gad.3.3.324}, number={3}, journal={Genes & Development}, publisher={Cold Spring Harbor Laboratory}, author={Caizergues-Ferrer, M and Mariottini, P and Curie, C and Lapeyre, B and Gas, N and Amalric, F and Amaldi, F}, year={1989}, month=mar, pages={324–333} }