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Nucleic Acids Research, 1982, Vol. 10, No. 19 5869-5878
© 1982

MOLECULAR BIOLOGY

The structure of the gene coding for the phosphorylated ribosomal protein S10 in yeast

Robert J. Leer, Mary M.C.van Raamsdonk-Duin, Constance M.Th. Molenaar, Louis H. Cohen*, Willem H. Mager and Rudi J. Planta

Biochemisch Laboratorium, Vrije Universiteit de Boelelaan 1083, 1081 HV Amsterdam, The Netherlands

Received June 23, 1982. Revised September 2, 1982. Accepted September 2, 1982.

From previous studies on cloned yeast ribosomal protein genes we obtained evidence that a large number of them contain an intron [Bollen et al. (1982) Gene 18, 29–38]. In the temperature-sensitive rna2-mutant Transcription of these genes leads to the accumulation of precursor RNAs at the restrictive temperature. These precursor mRNAs are several hundreds of nucleotides longer than the respective mature mRNAs. The split character of one of these ribosomal protein genes, viz. the gene coding for the major phosphorylated small-subunit protein S10, was further established by sequence analysis. The intervening sequence interrupts the coding sequence after the second codon and has a length of 352 nucleotides. Genomic Southern hybridizations with a DNA fragment carrying part of the S10-gene revealed that this gene is duplicated on the yeast genome. The molecular weight of S10 as deduced from the sequence analysis was estimated to be 31462 dal. Comparison of the N-terminal aminoacid sequence of the yeast ribosomal protein S10 with that of ribosomal protein S6 from rat liver revealed a striking homology between both proteins. Moreover, at the C-terminal end of the yeast ribosomal protein the sequence Arg-Ala-Ser-Ser-Leu-Lys is present which is very similar to the phosphorylation site of the rat liver protein S6.

*Present address: Gaubius Institute, Division of Health Research TNO, Leiden, The Netherlands


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