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Nucleotide sequence of the L1 ribosomal protein gene of Xenopus laevis: remarkable sequence homology among introns.
Author(s) -
Loreni F.,
Ruberti I.,
Bozzoni I.,
PierandreiAmaldi P.,
Amaldi F.
Publication year - 1985
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1985.tb04107.x
Subject(s) - biology , intron , genetics , homology (biology) , gene , nucleic acid sequence , ribosomal protein , ribosomal rna , xenopus , sequence (biology) , microbiology and biotechnology , ribosome , rna
Ribosomal protein L1 is encoded by two genes in Xenopus laevis. The comparison of two cDNA sequences shows that the two L1 gene copies (L1a and L1b) have diverged in many silent sites and very few substitution sites; moreover a small duplication occurred at the very end of the coding region of the L1b gene which thus codes for a product five amino acids longer than that coded by L1a. Quantitatively the divergence between the two L1 genes confirms that a whole genome duplication took place in Xenopus laevis approximately 30 million years ago. A genomic fragment containing one of the two L1 gene copies (L1a), with its nine introns and flanking regions, has been completely sequenced. The 5′ end of this gene has been mapped within a 20‐pyridimine stretch as already found for other vertebrate ribosomal protein genes. Four of the nine introns have a 60‐nucleotide sequence with 80% homology; within this region some boxes, one of which is 16 nucleotides long, are 100% homologous among the four introns. This feature of L1a gene introns is interesting since we have previously shown that the activity of this gene is regulated at a post‐transcriptional level and it involves the block of the normal splicing of some intron sequences.