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  • 1
    Electronic Resource
    Electronic Resource
    Genetic Analysis of the Chloroplast and Mitochondrial Genomes (1974)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Genetics 8 (1974), S. 347-391 
    Details
    ISSN: 0066-4197
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ge.08.120174.002023
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  • 2
    Electronic Resource
    Electronic Resource
    Translational Regulation of Gene Expression in Chloroplasts and Mitochondria (1994)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Genetics 28 (1994), S. 71-93 
    Details
    ISSN: 0066-4197
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.ge.28.120194.000443
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    dr and spr/sr mutations of Chlamydomonas reinhardtii affecting D1 protein function and synthesis define two independent steps leading to chronic photoinhibition and confer differential fitness (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Plant, cell & environment 20 (1997), S. 0 
    Details
    ISSN: 1365-3040
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology
    Notes: The effects of introduced chloroplast gene mutations affecting D1 synthesis, turnover and function on photosynthesis, growth and competitive ability were examined in autotrophic cultures of Chlamydomonas reinhardtii (Chlorophyta) adapted to low or high irradiance. Few discernible effects were evident when the mutants were grown in low light (LL, 70 μmol m−2 s−1). The herbicide-resistant psbA mutation Ser264→ Ala (dr) slowed electron transfer and accelerated D1 degradation in cells grown under high light (HL, 600 μmol m−2 s−1). The maximum rate of light-and CO2-saturated photosynthesis, cell growth rate and competitive ability in the dr mutant were reduced compared to wild type under HL. However, the wild-type rate of D1 synthesis in dr was adequate to compensate for accelerated D1 degradation. 16S rRNA mutations conferring resistance to streptomycin and spectinomycin (spr/sr) that altered chloroplast ribosome structure and assembly were used to inhibit chloroplast protein synthesis. In spr/sr cells grown under HL, D1 synthesis was reduced by 40–60% compared to wild type and D1 degradation was accelerated, leading to a 4-fold reduction in D1 pool size. The reduced D1 levels were accompanied by an elevation of Fo and a decline in Fv/Fm, quantum yield and maximum rate of CO2-saturated photosynthesis. Chemostat experiments showed that the growth rate and competitive ability of spr/sr were reduced against both wild type and dr.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-3040.1997.d01-143.x
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  • 4
    Electronic Resource
    Electronic Resource
    Shine-Dalgarno-like sequences are not required for translation of chloroplast mRNAs in Chlamydomonas reinhardtii chloroplasts or in Escherichia coli (1998)
    Springer
    Molecular genetics and genomics 257 (1998), S. 271-282 
    Details
    ISSN: 1617-4623
    Keywords: Key wordsChlamydomonas ; Translational control ; Chloroplast genetics ; Shine-Dalgarno sequence ; Chloroplast reporter genes
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Initiation of translation in Escherichia coli and related eubacteria involves well-defined interactions between a conserved Shine-Dalgarno (SD) sequence immediately upstream of the initiation codon in the mRNA leader and an equally conserved anti-SD sequence at the 3′ end of the 16S rRNA. SD-like sequences found in the leaders of many, but not all, mRNAs from cyanobacteria and chloroplasts are hypervariable in location, size, and base composition compared to those in E. coli, while anti-SD sequences in the respective 16S rRNAs remain highly conserved. We have examined the function of the SD-like sequences found in the leaders of four chloroplast genes of the green alga Chlamydomonas reinhardtii using replacement mutagenesis to eliminate complementarity with the anti-SD sequences and insertion of canonical SD sequences (GGAGG) at positions −9 to −5 relative to the initiation codon. Promoter-leader regions of the atpB, atpE, rps4, and rps7 genes representing the diversity of chloroplast SD-like sequences were fused to aadA and uidA reporter genes encoding spectinomycin resistance and GUS activity respectively. Analysis of chloroplast transformants of C. reinhardtii and transformants of E. coli carrying the wild-type and mutant reporter constructs revealed that mutagenic replacement of the putative SD sequences had no effect on the expression of either the aadA or uidA reporter genes. Chloroplast transformants with the canonical SD sequence also showed no differences in reporter gene expression, whereas expression of the reporter genes was increased by 10 to 30% in the E. coli transformants. Collectively our results suggest that even though SD-dependent initiation predominates in E. coli, this bacterium also has the capacity to initiate translation by an SD-independent mechanism. In contrast, plant chloroplasts, and very probably their cyanobacterial ancestors, appear to have adopted the SD-independent mechanism for translational initiation of most mRNAs.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004380050648
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  • 5
    Electronic Resource
    Electronic Resource
    Mutations that alter the higher-order structure of its 5' untranslated region affect the stability of chloroplast rps7 mRNA (2000)
    Springer
    Molecular genetics and genomics 264 (2000), S. 291-299 
    Details
    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
    URL: http://dx.doi.org/10.1007/s004380000321
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  • 6
    Electronic Resource
    Electronic Resource
    The cytoplasmic ribosomes of Chlamydomonas reinhardtii: Characterization of antibiotic sensitivity and cycloheximide-resistant mutants (1987)
    Springer
    Molecular genetics and genomics 210 (1987), S. 419-428 
    Details
    ISSN: 1617-4623
    Keywords: Cytoplasmic ribosomes ; Cycloheximide ; Chlamydomonas reinhardtii
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary In vitro protein synthesis was used to characterize the antibiotic sensitivity of cytoplasmic ribosomes from wild-type and antibiotic-resistant strains of Chlamydomonas reinhardtii. Cytoplasmic ribosomes from two cycloheximide-resistant mutants, act-1 and act-2, were resistant to the antibiotic in vitro. The alteration effected by the act-1 mutation, which was dominant in diploids, was localized to the large subunit of the cytoplasmic ribosomes, but no ribosomal protein alterations were detected using two-dimensional gel electrophoresis. The act-2 mutation, which was semidominant in diploids, was frequently associated with a charge alteration in the large subunit ribosomal protein (r-protein) cyL38 that segregated independently from the antibiotic-resistant phenotype in crosses.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00327192
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  • 7
    Electronic Resource
    Electronic Resource
    Cytoplasmic ribosomal proteins from Chlamydomonas reinhardtii: Characterization and immunological comparisons (1987)
    Springer
    Molecular genetics and genomics 206 (1987), S. 226-237 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00333578
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