Translational Regulation of the Expression of Ribosomal Protein Genes in Xenopus laevis

Enzyme ◽  
1990 ◽  
Vol 44 (1-4) ◽  
pp. 93-105 ◽  
Author(s):  
Francesco Amaldi ◽  
Paola Pierandrei-Amaldi
Keyword(s):  
Xenopus Laevis ◽  
Ribosomal Protein ◽  
Translational Regulation ◽  
Ribosomal Protein Genes

Structure and expression of ribosomal protein genes in Xenopus laevis

1995 ◽  
Vol 73 (11-12) ◽  
pp. 969-977 ◽  
Author(s):  
Francesco Amaldi ◽  
Olga Camacho-Vanegas ◽  
Francesco Cecconi ◽  
Fabrizio Loreni ◽  
Beatrice Cardinali ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Ribosomal Protein ◽  
Ribosomal Proteins ◽  
Translational Regulation ◽  
Cultured Cells ◽  
Structural Features ◽  
Ribosomal Protein Genes ◽  
Translation Apparatus ◽  
And Function

In Xenopus laevis, as well as in other vertebrates, ribosomal proteins (r-proteins) are coded by a class of genes that share some organizational and structural features. One of these, also common to genes coding for other proteins involved in the translation apparatus synthesis and function, is the presence within their introns of sequences coding for small nucleolar RNAs. Another feature is the presence of common structures, mainly in the regions surrounding the 5′ ends, involved in their coregulated expression. This is attained at various regulatory levels: transcriptional, posttranscriptional, and translational. Particular attention is given here to regulation at the translational level, which has been studied during Xenopus oogenesis and embryogenesis and also during nutritional changes of Xenopus cultured cells. This regulation, which responds to the cellular need for new ribosomes, operates by changing the fraction of rp-mRNA (ribosomal protein mRNA) engaged on polysomes. A typical 5′ untranslated region characterizing all vertebrate rp-mRNAs analyzed to date is responsible for this translational behaviour: it is always short and starts with an 8–12 nucleotide polypyrimidine tract. This region binds in vitro some proteins that can represent putative trans-acting factors for this translational regulation.Key words: ribosomal proteins, snoRNA, translational regulation, Xenopus laevis.

Isolation and structural analysis of ribosomal protein genes in Xenopus laevis

1982 ◽  
Vol 161 (3) ◽  
pp. 353-371 ◽  
Author(s):  
Irene Bozzoni ◽  
Angelo Tognoni ◽  
Paola Pierandrei-Amaldi ◽  
Elena Beccari ◽  
Mario Buongiorno-Nardelli ◽  
...  
Keyword(s):  
Structural Analysis ◽  
Xenopus Laevis ◽  
Ribosomal Protein ◽  
Ribosomal Protein Genes

scholarly journals Xenopus laevis ribosomal protein genes: isolation of recombinant cDNA clones and study of the genomic organization

1981 ◽  
Vol 9 (5) ◽  
pp. 1069-1086 ◽  
Author(s):  
Irene Bozzoni ◽  
Elena Beccari ◽  
Zhong Xun Luo ◽  
Francesco Amaldi ◽  
Paola Pierandrei-Amaldi ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Ribosomal Protein ◽  
Genomic Organization ◽  
Cdna Clones ◽  
Ribosomal Protein Genes

scholarly journals XrpFI, an amphibian transcription factor composed of multiple polypeptides immunologically related to the GA-binding protein alpha and beta subunits, is differentially expressed during Xenopus laevis development.

1993 ◽  
Vol 13 (10) ◽  
pp. 6479-6489 ◽  
Author(s):  
M Marchioni ◽  
S Morabito ◽  
A L Salvati ◽  
E Beccari ◽  
F Carnevali
Keyword(s):  
Xenopus Laevis ◽  
Ribosomal Protein ◽  
Transcriptional Activation ◽  
Binding Protein ◽  
Ribosomal Protein Gene ◽  
Target Sequence ◽  
Xenopus Laevis Oocyte ◽  
Ribosomal Protein Genes ◽  
Related Proteins ◽  
Ga Binding Protein

XrpFI, first identified in the extract of Xenopus laevis oocyte nuclei, binds to a proximal sequence of the L14 ribosomal protein gene promoter. Its target sequence, 5'-TAACCGGAAGTTTGT-3', is required to fully activate the promoter, and the two G's of the central motif are essential for factor binding and transcriptional activation; our data also suggest that XrpFI may play a role in cap site positioning. The binding site of XrpFI is homologous to the sequence recognized by the family of ets genes. Antibodies specific for Ets-1 and Ets-2 proteins did not react with XrpFI, but those raised against the rat alpha and beta GA-binding proteins both supershifted the retarded bands formed by XrpFI. The Xenopus polypeptides related to GA-binding protein alpha interact with DNA both as monomers and as heterodimers associated with beta-related proteins. Oocyte nuclei contain multiple forms of alpha- and beta-related proteins: the alpha-like proteins remain throughout development, while the pattern of the beta species changes in the embryonic stages examined. beta-like proteins are undetectable in the cleavage period up to the neurula stage, but at later stages, when ribosomal protein genes are actively transcribed, two beta-related polypeptides reappear.

Expression of two Xenopus laevis ribosomal protein genes in injected frog oocytes

1984 ◽  
Vol 180 (4) ◽  
pp. 987-1005 ◽  
Author(s):  
Irene Bozzoni ◽  
Paola Fragapane ◽  
Flavia Annesi ◽  
Paola Pierandrei-Amaldi ◽  
Francesco Amaldi ◽  
...  
Keyword(s):  
Xenopus Laevis ◽  
Ribosomal Protein ◽  
Ribosomal Protein Genes
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