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  • Electronic Resource  (2)
  • Chlamydomonas Chloroplast RNA stability 5'UTR  (1)
  • Cytoplasmic, chloroplast and bacterial ribosomal proteins  (1)
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  • Electronic Resource  (2)
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  • 1
    ISSN: 1617-4623
    Keywords: Chlamydomonas Chloroplast RNA stability 5'UTR
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. In this paper, we examine the effects of mutations in the 5'UTR of the chloroplast rps7 transcript of Chlamydomonas reinhardtii that reduce the stability of the mRNA. Five point mutants in the rps7 5'UTR were selected on the basis of their failure to accumulate reporter mRNA in Escherichia coli. Each of these mutations produces alterations in the predicted higher-order structures of the rps7 5'UTR that destabilize the mRNA. Cis-acting suppressors of these mutations have been selected in E. coli and in the C. reinhardtii chloroplast that restore message stability and function. No differences in RNA melting and reannealing profiles have been observed between wild type, original mutant, and suppressor 5'UTRs transcribed in vitro. Proteins of 32 kDa and 47 kDa that bind to the wild-type rps7 5'UTR are not detected by UV cross-linking assays performed with any of the mutant rps7 5'UTRs. However, binding of the 32-kDa protein is restored in the six suppressor mutants examined. This suggests that the 32-kDa protein may be involved in protecting the rps7 5'UTR and the attached coding region from digestion by ribonucleases. Alternatively, the binding site for the 32-kDa protein may be independently lost in the rearranged tertiary structure of the mutant 5'UTR that exposes the RNA to degradation and is restored in the suppressor mutants.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 206 (1987), S. 226-237 
    ISSN: 1617-4623
    Keywords: Cytoplasmic, chloroplast and bacterial ribosomal proteins ; Immunoblotting ; Chlamydomonas reinhardtii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Experiments were undertaken to characterize the cytoplasmic ribosomal proteins (r-proteins) in Chlamydomonas reinhardtii and to compare immunologically several cytoplasmic r-proteins with those of chloroplast ribosomes of this alga, Escherichia coli, and yeast. The large and small subunits of the C. reinhardtii cytoplasmic ribosomes were shown to contain, respectively, 48 and 45 r-proteins, with apparent molecular weights of 12,000–59,000. No cross-reactivity was seen between antisera made against cytoplasmic r-proteins of Chlamydomonas and chloroplast r-proteins, except in one case where an antiserum made against a large subunit r-protein cross-reacted with an r-protein of the small subunit of the chloroplast ribosome. Antisera made against one out of five small subunit r-proteins and three large subunit r-proteins recognized r-proteins from the yeast large subunit. Each of the yeast r-proteins has been previously identified as an rRNA binding protein. The antiserum to one large subunit r-protein cross-reacted with specific large subunit r-proteins from yeast and E. coli.
    Type of Medium: Electronic Resource
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