The cloning and sequencing of a cDNA for human ribosomal protein L4 is reported. The corresponding mRNA has a very short 5' untranslated region initiating with a sequence of 12 pyrimidines, characteristic of all vertebrate ribosomal protein mRNAs. The deduced amino acid sequence shows that human ribosomal protein L4 has 425 amino acid residues and a calculated molecular mass of 47821 Da. Comparison with the homologous counterparts of Xenopus, Drosophila and yeast shows that this protein has a very conserved amino-terminus region and an extremely divergent carboxyl-terminus portion.
Bagni, C., Mariottini, P., Annesi, F., Amaldi, F. (1993). Human ribosomal protein L4: cloning and sequencing of the cDNA and primary structure of the protein. BIOCHIMICA ET BIOPHYSICA ACTA, N. GENE STRUCTURE AND EXPRESSION, 1216(3), 475-478 [10.1016/0167-4781(93)90017-8].
Human ribosomal protein L4: cloning and sequencing of the cDNA and primary structure of the protein
Bagni, C;Amaldi, F
1993-01-01
Abstract
The cloning and sequencing of a cDNA for human ribosomal protein L4 is reported. The corresponding mRNA has a very short 5' untranslated region initiating with a sequence of 12 pyrimidines, characteristic of all vertebrate ribosomal protein mRNAs. The deduced amino acid sequence shows that human ribosomal protein L4 has 425 amino acid residues and a calculated molecular mass of 47821 Da. Comparison with the homologous counterparts of Xenopus, Drosophila and yeast shows that this protein has a very conserved amino-terminus region and an extremely divergent carboxyl-terminus portion.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
