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  • Degradation  (1)
  • nucleotide sequence  (1)
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  • 1
    ISSN: 1617-4623
    Keywords: Lon protease ; Ribosomal protein L24 ; Degradation ; Suppression
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A suppressor mutation of a temperature-sensitive mutant of ribosomal protein L24 (rplX19) was mapped close to the lon gene by genetic analysis and was shown to affect protease LA. The degradation and the synthesis rates of individual ribosomal proteins were determined. Proteins L24, L14, L15 and L27 were found to be degraded faster in the original rplX19 mutant than in the rplX19 mutant containing the suppressor mutation. Other ribosomal proteins were either weakly or not at all degraded in both mutants. Temperature-sensitive growth was also suppressed by the overproduction of mutant protein L24 from a plasmid. Our results suggest that (1) either free ribosomal proteins or proteins bound to abortive assembly precursors are highly susceptible to the lon gene product and (2) the mutationally altered protein L24 can still function at the nonpermissive growth temperature of the mutant, if it is present in sufficient amounts.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1617-4623
    Keywords: r-protein genes ; nucleotide sequence ; γδ insertion ; open reading frame
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The DNA sequence of a cluster of genes for ribosomal proteins S6 (rpsF), S18 (rpsR) and L9 (rplI), and of their surrounding regions was determined. The order of the genes was established as promoter-rpsF-rpsR-rplI. There is a 315 bp open reading frame that begins seven nucleotides after the end of rpsF and ends immediately before rpsR. Based on the data of insertional mutagenesis experiments with transposon γδ, we concluded that these genes probably form an operon. The amino acid sequence deduced from the nucleotide sequence of the genes agrees completely with the published amino acid sequence data for protein S6, but there are discrepancies in the case of proteins S18 and L9. The C-terminus of protein S6 was deduced to end with two Glu residues, suggesting that the other Glu residues previously found in this protein are added post-translationally as has been predicted (Reeh and Pedersen 1979). A possible secondary structure in the leader sequence as well as a possible transcriptional terminator after rplI were noticed in the sequence.
    Type of Medium: Electronic Resource
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