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  • 1
    Electronic Resource
    Electronic Resource
    Capping it all with algae (1992)
    [s.l.] : Nature Publishing Group
    Nature 360 (1992), S. 427-427 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] DASYCLADALES are a remarkable order of unicellular green algae widely found in the shallow waters of tropical or sub-tropical shores. Cells of the genus Acetabularia (top, x2.2) and the re-lated genus Polphysa (bottom, x20) can grow to lengths of up to 20 cm and develop perfect radial caps ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/360427a0
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  • 2
    Electronic Resource
    Electronic Resource
    Topography of Chlamydomonas: fine structure and polypeptide components of the gametic flagellar membrane surface and the cell wall (1983)
    Springer
    Planta 158 (1983), S. 517-533 
    Details
    ISSN: 1432-2048
    Keywords: Chlamydomonas ; Flagellum ; Gamete ; Membrane, flagellar ; Mutant (Chlamydomonas)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Surface polypeptide components of the flagellar membrane of Chlamydomonas reinhardi Dang. gametes are identified by their accessibility to in-vivo vectoral labeling by glucose oxidase-coupled lactoperoxidase-dependent 125I iodination. Vectoral labeling is accomplished without observable adverse effects on cell viability or gametic function. Flagella isolated from labeled wild-type cells carry about 3% of the total incorporated label, which is found by one-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis to be distributed among 16 identifiable polypeptide bands. The most prominent surface-labeled species migrates in the Mr (relative molecular weight) 350 k region of the gel; each of the remaining iodinated polypeptides, which range in Mr from 25 k to 500 k, carries only a small proportion of incorporated label. To determine which polypeptides are unique to the flagellum and which are contaminants from the cell wall, wild-type profiles were compared with those of mutant strains and of mechanically isolated cell walls. Identification of contaminants was also facilitated by two-dimensional peptide mapping. We conclude that only 11 of the labeled bands are contributed by flagellar polypeptides; the remaining five bands are shown to be contaminants from the cell wall, and additional cell-wall polypeptides are found to co-migrate with flagellar species. A polypeptide designated as a possible membrane tubulin in preliminary studies is shown here to be different from tubulin in its peptide map. The 11 polypeptides assigned as specific flagellar surface components are candidate participants in such biological events as sexual adhesion, flagellar surface motility, and sensory signalling.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00397243
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  • 3
    Electronic Resource
    Electronic Resource
    Domain conservation in several volvocalean cell wall proteins (1994)
    Springer
    Plant molecular biology 26 (1994), S. 947-960 
    Details
    ISSN: 1573-5028
    Keywords: cell wall ; HRGPs ; domain conservation ; exon shuffling ; protein evolution ; Chlamydomonas
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Based on our previous work demonstrating that (SerPro)x epitopes are common to extensin-like cell wall proteins in Chlamydomonas reinhardtii, we looked for similar proteins in the distantly related species C. eugametos. Using a polyclonal antiserum against a (SerPro)10 oligopeptide, we found distinct sets of stage-specific polypeptides immunoprecipitated from in vitro translations of C. eugametos RNA. Screening of a C. eugametos cDNA expression library with the antiserum led to the isolation of a cDNA (WP6) encoding a (SerPro)x-rich multidomain wall protein. Analysis of a similarly selected cDNA (VSP-3) from a C. reinhardtii cDNA expression library revealed that it also coded for a (SerPro)x-rich multidomain wall protein. The C-terminal rod domains of VSP-3 and WP6 are highly homologous, while the N-terminal domains are dissimilar; however, the N-terminal domain of VSP-3 is homologous to the globular domain of a cell wall protein from Volvox carteri. Exon shuffling might be responsible for this example of domain conservation over 350 million years of volvocalean cell wall protein evolution.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00028861
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  • 4
    Electronic Resource
    Electronic Resource
    Volvocine cell walls and their constituent glycoproteins: An evolutionary perspective (1994)
    Springer
    Protoplasma 181 (1994), S. 245-258 
    Details
    ISSN: 1615-6102
    Keywords: Evolution ; Hydroxyproline-rich glycoprotein ; Cell wall ; Phylogenetics ; Chlamydomonas ; Volvocales
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Similarities in the composition of the extracellular matrix suggest that only some species of the unicellularChlamydomonas are closely related to the colonial and multicellular flagellated members of the family Volvocaceae. The cell walls from all of the algae in this volvocine group contain a crystalline layer. This lattice structure can be used as a phylogenetic marker to divideChlamydomonas species into distinct classes, only one of which includes the volvocacean algae. Similarly, not all species ofChlamydomonas are sensitive to each other's cell wall lytic enzymes, implying divergence of the enzyme's inner wall substrate. Interspecific reconstitution of the crystalline layer is possible betweenC. reinhardtii and the multicellularVolvox carteri, but not betweenC. reinhardtii andC. eugametos. The hydroxyproline-rich glycoproteins (HRGPs) which make up the crystalline layer in genera which have a similar crystal structure exhibit many homologies. Interestingly, the evolutionarily distant cell walls ofC. reinhardtii andC. eugametos also contain some HRGPs displaying a few morphological and amino acid sequence homologies. The morphological similarities between the flagellar agglutinins (HRGPs responsible for sexual recognition and adhesion during the mating reaction) and the cell wall HRGPs leads to the proposal of a superfamily from which novel HRGPs (designed for self-assembly/recognition) can constantly evolve. Just as variations in the wall HRGPs can lead to unique wall structures, new agglutinins facilitate sexual isolation of new species. Thus, the HRGPs could emerge as valuable phylogenetic markers.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01666399
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  • 5
    Electronic Resource
    Electronic Resource
    A gene/pseudogene tandem duplication encodes a cysteine-rich protein expressed during zygote development in Chlamydomonas reinhardtii (1992)
    Springer
    Molecular genetics and genomics 232 (1992), S. 81-88 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Class V zygote-specific gene from Chlamydomonas reinhardtii has been cloned and sequenced. This gene encodes a polypeptide of 86 amino acids, which contains a signal peptide and 6 cysteine residues arranged in an inverted symmetrical repeat. The Class V gene product is postulated to be a component of the zygote cell wall. Southern analysis revealed two tandemly oriented and closely linked copies of the Class V gene, designated A and B. The A gene appears to be a pseudogene, based on analysis of Class V cDNAs, primer extension with gene-specific primers, and Northern analysis which failed to detect an A gene transcript. Genetic analysis using a related Chlamydomonas species that lacks the A gene, but which produces normal zygotic progeny, further indicates that the A gene is not required for zygote development.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00299140
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  • 6
    Electronic Resource
    Electronic Resource
    Tipping of flagellar agglutinins by gametes of Chlamydomonas reinhardtii (1993)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 25 (1993), S. 179-189 
    Details
    ISSN: 0886-1544
    Keywords: mating reaction ; migration ; cross-linked agglutinins ; gametic flagellar tips ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The migration of cross-linked agglutinins to the gametic flagellar tips (tipping) is a hallnmark of the Chlamydomonas mating reaction. In this study, an assay was developed to analyze the kinetics and biological requirements for the tipping response: isolated flagella from mt- gametes of C. reinhardtii were allowed to agglutinate to the immotile flagella of pf-18 mt+ gametes, and their migration to the tips was monitored by phase microscopy. The tipping process is shown to require both adhesion and elevated levels of cAMP. The cAMP may activate tipping motors directly. In addition, cAMP stimulates the recruitment of agglutinins to flagellar surface to replace those inactivated by adhesion. These results are compared with previous studies on the tipping of flagellar surface proteins cross-linked by soluble ligands, and an integrated model is presented. © 1993 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970250207
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  • 7
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    A Rubisco-binding protein is required for normal pyrenoid number and starch sheath morphology inChlamydomonas reinhardtii (2019)
    National Academy of Sciences
    Details
    Publication Date: 2019-08-27
    Description: A phase-separated, liquid-like organelle called the pyrenoid mediates CO2fixation in the chloroplasts of nearly all eukaryotic algae. While most algae have 1 pyrenoid per chloroplast, here we describe a mutant in the model algaChlamydomonasthat has on average 10 pyrenoids per chloroplast. Characterization of the mutant leads us to propose a model where multiple pyrenoids are favored by an increase in the surface area of the starch sheath that surrounds and binds to the liquid-like pyrenoid matrix. We find that the mutant’s phenotypes are due to disruption of a gene, which we call StArch Granules Abnormal 1 (SAGA1) because starch sheath granules, or plates, in mutants lacking SAGA1 are more elongated and thinner than those of wild type. SAGA1 contains a starch binding motif, suggesting that it may directly regulate starch sheath morphology. SAGA1 localizes to multiple puncta and streaks in the pyrenoid and physically interacts with the small and large subunits of the carbon-fixing enzyme Rubisco (ribulose-1,5-bisphosphate carboxylase/oxygenase), a major component of the liquid-like pyrenoid matrix. Our findings suggest a biophysical mechanism by which starch sheath morphology affects pyrenoid number and CO2-concentrating mechanism function, advancing our understanding of the structure and function of this biogeochemically important organelle. More broadly, we propose that the number of phase-separated organelles can be regulated by imposing constraints on their surface area.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 8
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    LHCSR1 induces a fast and reversible pH-dependent fluorescence quenching in LHCII in Chlamydomonas reinhardtii cells (2016)
    National Academy of Sciences
    Details
    Publication Date: 2016-06-22
    Description: To avoid photodamage, photosynthetic organisms are able to thermally dissipate the energy absorbed in excess in a process known as nonphotochemical quenching (NPQ). Although NPQ has been studied extensively, the major players and the mechanism of quenching remain debated. This is a result of the difficulty in extracting molecular information from in vivo experiments and the absence of a validation system for in vitro experiments. Here, we have created a minimal cell of the green alga Chlamydomonas reinhardtii that is able to undergo NPQ. We show that LHCII, the main light harvesting complex of algae, cannot switch to a quenched conformation in response to pH changes by itself. Instead, a small amount of the protein LHCSR1 (light-harvesting complex stress related 1) is able to induce a large, fast, and reversible pH-dependent quenching in an LHCII-containing membrane. These results strongly suggest that LHCSR1 acts as pH sensor and that it modulates the excited state lifetimes of a large array of LHCII, also explaining the NPQ observed in the LHCSR3-less mutant. The possible quenching mechanisms are discussed.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 9
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    A repeat protein links Rubisco to form the eukaryotic carbon-concentrating organelle (2016)
    National Academy of Sciences
    Details
    Publication Date: 2016-05-10
    Description: Biological carbon fixation is a key step in the global carbon cycle that regulates the atmosphere's composition while producing the food we eat and the fuels we burn. Approximately one-third of global carbon fixation occurs in an overlooked algal organelle called the pyrenoid. The pyrenoid contains the CO2-fixing enzyme Rubisco and enhances carbon fixation by supplying Rubisco with a high concentration of CO2. Since the discovery of the pyrenoid more that 130 y ago, the molecular structure and biogenesis of this ecologically fundamental organelle have remained enigmatic. Here we use the model green alga Chlamydomonas reinhardtii to discover that a low-complexity repeat protein, Essential Pyrenoid Component 1 (EPYC1), links Rubisco to form the pyrenoid. We find that EPYC1 is of comparable abundance to Rubisco and colocalizes with Rubisco throughout the pyrenoid. We show that EPYC1 is essential for normal pyrenoid size, number, morphology, Rubisco content, and efficient carbon fixation at low CO2. We explain the central role of EPYC1 in pyrenoid biogenesis by the finding that EPYC1 binds Rubisco to form the pyrenoid matrix. We propose two models in which EPYC1’s four repeats could produce the observed lattice arrangement of Rubisco in the Chlamydomonas pyrenoid. Our results suggest a surprisingly simple molecular mechanism for how Rubisco can be packaged to form the pyrenoid matrix, potentially explaining how Rubisco packaging into a pyrenoid could have evolved across a broad range of photosynthetic eukaryotes through convergent evolution. In addition, our findings represent a key step toward engineering a pyrenoid into crops to enhance their carbon fixation efficiency.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 10
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    Sex determination in Chlamydomonas (2007)
    Elsevier
    Details
    Publication Date: 2007-06-01
    Print ISSN: 1084-9521
    Electronic ISSN: 1096-3634
    Topics: Biology , Medicine
    Published by Elsevier
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