Effects of site-directed mutations in the central domain of 16 S ribosomal RNA upon ribosomal protein binding, RNA processing and 30 S subunit assembly

1984 ◽  
Vol 178 (2) ◽  
pp. 303-322 ◽  
Author(s):  
Michael J.R. Stark ◽  
Richard J. Gregory ◽  
Richard L. Gourse ◽  
David L. Thurlow ◽  
Christian Zwieb ◽  
...  
Keyword(s):  
Protein Binding ◽  
Ribosomal Protein ◽  
Ribosomal Rna ◽  
Rna Processing ◽  
Central Domain ◽  
Subunit Assembly

scholarly journals Location of Ribosomal Protein Binding Sites on 16S Ribosomal RNA

1972 ◽  
Vol 69 (5) ◽  
pp. 1282-1286 ◽  
Author(s):  
R. A. Zimmermann ◽  
A. Muto ◽  
P. Fellner ◽  
C. Ehresmann ◽  
C. Branlant
Keyword(s):  
Protein Binding ◽  
Ribosomal Protein ◽  
Ribosomal Rna ◽  
Binding Sites ◽  
16S Ribosomal Rna ◽  
Protein Binding Sites

Adenovirus infection retards ribosomal RNA processing

1989 ◽  
Vol 138 (1) ◽  
pp. 205-207 ◽  
Author(s):  
Susan H. Lawler ◽  
Robert W. Jones ◽  
Brian P. Eliceiri ◽  
George L. Eliceiri
Keyword(s):  
Ribosomal Rna ◽  
Rna Processing ◽  
Adenovirus Infection ◽  
Ribosomal Rna Processing

Developmental expression of fibrillarin and U3 snRNA in Xenopus laevis

Development ◽  
1991 ◽  
Vol 112 (1) ◽  
pp. 317-326
Author(s):  
M. Caizergues-Ferrer ◽  
C. Mathieu ◽  
P. Mariottini ◽  
F. Amalric ◽  
F. Amaldi
Keyword(s):  
Ribosomal Rna ◽  
Rna Processing ◽  
Protein Detection ◽  
Developmental Expression ◽  
Oocyte Growth ◽  
Small Nuclear Ribonucleoprotein ◽  
Hybridization Probes ◽  
Ribosomal Rna Processing ◽  
Protein Components ◽  
Nuclear Ribonucleoprotein

Fibrillarin is one of the protein components that together with U3 snRNA constitute the U3 snRNP, a small nuclear ribonucleoprotein particle involved in ribosomal RNA processing in eucaryotic cells. Using an antifibrillarin antiserum for protein detection and a fibrillarin cDNA and a synthetic oligonucleotide complementary to U3 snRNA as hybridization probes, the expression of these two components has been studied during Xenopus development. Fibrillarin mRNA is accumulated early in oogenesis, like many other messengers, and translated during oocyte growth. Fibrillarin protein is thus progressively accumulated throughout oogenesis to be assembled with U3 snRNA and used for ribosome production in the amplified nucleoli. After fertilization, the amount of U3 snRNA decreases while the maternally accumulated fibrillarin mRNA is maintained and utilized to produce more protein. After the mid-blastula transition, stored fibrillarin is assembled with newly synthesized U3 snRNA and becomes localized in the prenucleolar bodies and reforming nucleoli.

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