Human ribosomal protein L4: Cloning and sequencing of the cDNA and primary structure of the protein

Details

Serval ID
serval:BIB_F9C4F9C4AD05
Type
Article: article from journal or magazin.
Collection
Publications
Title
Human ribosomal protein L4: Cloning and sequencing of the cDNA and primary structure of the protein
Journal
Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression
Author(s)
Bagni Claudia, Mariottini Paolo, Annesi Flavia, Amaldi Francesco
ISSN
0167-4781
ISSN-L
1879-2634
Publication state
Published
Issued date
12/1993
Peer-reviewed
Oui
Volume
1216
Number
3
Pages
475-478
Language
english
Notes
Publication types: Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
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 47,821 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.

Keywords
Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, DNA, Complementary/chemistry, DNA, Complementary/metabolism, Drosophila melanogaster/genetics, Humans, Molecular Sequence Data, Ribosomal Proteins/biosynthesis, Ribosomal Proteins/genetics, Saccharomyces cerevisiae/genetics, Sequence Homology, Amino Acid, Xenopus laevis, Biophysics, Genetics, Biochemistry, Structural Biology
Pubmed
Web of science
Create date
06/03/2017 18:23
Last modification date
20/08/2019 17:25
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