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Nucleic Acids Research, 1990, Vol. 18, No. 15 4423-4426
© 1990

MOLECULAR BIOLOGY

Structure of Xenopus laevis ribosomal protein L32 and its expression during development

Claudia Bagni, Paolo Mariottini, Flavia Annesi and Francesco Amaldi*

Dipartimento di Biologia, II Universita di Roma Tor Vergata via E.Carnevale, 00173 Rome, Italy

*To whom correspondence should be addressed

Received May 16, 1990. Revised June 26, 1990. Accepted June 26, 1990.

cDNA clones for Xenopus laevis ribosomal protein L32 have been isolated and sequenced. The deduced amino acid sequence indicates that L32 is a basic protein of 110 amino acids, has a molecular weight of 12,603 and is homologous to the rat ribosomal protein L35. Using the cDNA clone as a probe to follow the expression of this gene during Xenopus development, it has been shown that the pattern of accumulation of this mRNA follows the one previously described for other ribosomal protein mRNAs during oogenesis and embryogenesis. The analysis of the utilization of L32 mRNA during embryogenesis shows that this is controlled by the translational regulation typical of other ribosomal protein mRNAs.


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