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Journal articles on the topic 'Chlamydomonas reinhardi'

Author: Grafiati

Published: 4 June 2021

Last updated: 17 February 2022

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1

Hasnain, S. E., E. K. Manavathu, and W. C. Leung. "DNA-mediated transformation of Chlamydomonas reinhardi cells: use of aminoglycoside 3'-phosphotransferase as a selectable marker." Molecular and Cellular Biology 5, no. 12 (1985): 3647–50. http://dx.doi.org/10.1128/mcb.5.12.3647.

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Using a modified vector, we developed a method for DNA-mediated transformation of Chlamydomonas reinhardi with increased efficiency. The vector contained the yeast 2 microns origin of replication as a heterologous replicon. The aminoglycoside 3'-phosphotransferase (APH) gene linked to the simian virus 40 early promoter was used as an antibiotic selectable marker. The C. reinhardi transformants were resistant to 12 micrograms of G418 or 150 micrograms of kanamycin per ml. A quick-blot mRNA analysis demonstrated the presence of RNase-sensitive transcripts from the APH gene in the transformants,

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2

Hasnain, S. E., E. K. Manavathu, and W. C. Leung. "DNA-mediated transformation of Chlamydomonas reinhardi cells: use of aminoglycoside 3'-phosphotransferase as a selectable marker." Molecular and Cellular Biology 5, no. 12 (1985): 3647–50. http://dx.doi.org/10.1128/mcb.5.12.3647-3650.1985.

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Using a modified vector, we developed a method for DNA-mediated transformation of Chlamydomonas reinhardi with increased efficiency. The vector contained the yeast 2 microns origin of replication as a heterologous replicon. The aminoglycoside 3'-phosphotransferase (APH) gene linked to the simian virus 40 early promoter was used as an antibiotic selectable marker. The C. reinhardi transformants were resistant to 12 micrograms of G418 or 150 micrograms of kanamycin per ml. A quick-blot mRNA analysis demonstrated the presence of RNase-sensitive transcripts from the APH gene in the transformants,

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3

Silflow, C. D., R. L. Chisholm, T. W. Conner, and L. P. Ranum. "The two alpha-tubulin genes of Chlamydomonas reinhardi code for slightly different proteins." Molecular and Cellular Biology 5, no. 9 (1985): 2389–98. http://dx.doi.org/10.1128/mcb.5.9.2389.

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Full-length cDNA clones corresponding to the transcripts of the two alpha-tubulin genes in Chlamydomonas reinhardi were isolated. DNA sequence analysis of the cDNA clones and cloned gene fragments showed that each gene contains 1,356 base pairs of coding sequence, predicting alpha-tubulin products of 451 amino acids. Of the 27 nucleotide differences between the two genes, only two result in predicted amino acid differences between the two gene products. In the more divergent alpha 2 gene, a leucine replaces an arginine at amino acid 308, and a valine replaces a glycine at amino acid 366. The r

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4

Silflow, C. D., R. L. Chisholm, T. W. Conner, and L. P. Ranum. "The two alpha-tubulin genes of Chlamydomonas reinhardi code for slightly different proteins." Molecular and Cellular Biology 5, no. 9 (1985): 2389–98. http://dx.doi.org/10.1128/mcb.5.9.2389-2398.1985.

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Full-length cDNA clones corresponding to the transcripts of the two alpha-tubulin genes in Chlamydomonas reinhardi were isolated. DNA sequence analysis of the cDNA clones and cloned gene fragments showed that each gene contains 1,356 base pairs of coding sequence, predicting alpha-tubulin products of 451 amino acids. Of the 27 nucleotide differences between the two genes, only two result in predicted amino acid differences between the two gene products. In the more divergent alpha 2 gene, a leucine replaces an arginine at amino acid 308, and a valine replaces a glycine at amino acid 366. The r

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5

Goodenough, U. W., W. S. Adair, P. Collin-Osdoby, and J. E. Heuser. "Structure of the Chlamydomonas agglutinin and related flagellar surface proteins in vitro and in situ." Journal of Cell Biology 101, no. 3 (1985): 924–41. http://dx.doi.org/10.1083/jcb.101.3.924.

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Using the quick-freeze, deep-etch technique, we compare the structure of the cane-shaped plus and minus sexual agglutinin molecules purified from gametes of Chlamydomonas reinhardi. We also describe the structure of three additional gamete-specific fibrillar molecules, called short canes, loops, and crescents, which are structurally related to the agglutinins. Four non-agglutinating mutant strains are found to produce the three latter fibrils but not canes, supporting our identification of the cane-shaped molecule as the agglutinin. The heads of the plus and minus canes are shown to differ in

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6

Merchant, S., and L. Bogorad. "Regulation by copper of the expression of plastocyanin and cytochrome c552 in Chlamydomonas reinhardi." Molecular and Cellular Biology 6, no. 2 (1986): 462–69. http://dx.doi.org/10.1128/mcb.6.2.462.

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Plastocyanin and cytochrome c552 are interchangeable electron carriers in the photosynthetic electron transfer chains of some cyanobacteria and green algae (P. M. Wood, Eur. J. Biochem. 87:9-19, 1978; G. Sandmann et al., Arch. Microbiol. 134:23-27, 1983). Chlamydomonas reinhardi cells respond to the availability of copper in the medium and accordingly accumulate either plastocyanin (if copper is available) or cytochrome c552 (if copper is not available). The response occurs in both heterotrophically and phototrophically grown cells. We have studied the molecular level at which this response oc

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7

Merchant, S., and L. Bogorad. "Regulation by copper of the expression of plastocyanin and cytochrome c552 in Chlamydomonas reinhardi." Molecular and Cellular Biology 6, no. 2 (1986): 462–69. http://dx.doi.org/10.1128/mcb.6.2.462-469.1986.

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Plastocyanin and cytochrome c552 are interchangeable electron carriers in the photosynthetic electron transfer chains of some cyanobacteria and green algae (P. M. Wood, Eur. J. Biochem. 87:9-19, 1978; G. Sandmann et al., Arch. Microbiol. 134:23-27, 1983). Chlamydomonas reinhardi cells respond to the availability of copper in the medium and accordingly accumulate either plastocyanin (if copper is available) or cytochrome c552 (if copper is not available). The response occurs in both heterotrophically and phototrophically grown cells. We have studied the molecular level at which this response oc

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8

Wettern, M., and G. Galling. "Degradation of the 32-kilodalton thylakoid-membrane polypeptide of Chlamydomonas reinhardi Y-1." Planta 166, no. 4 (1985): 474–82. http://dx.doi.org/10.1007/bf00391271.

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9

Nakano, Yuka, Nozumu Koizumi, Tomonobu Kusano, and Hiroshi Sano. "Isolation and properties of an S-adenosyl-L-methionine binding protein from the green alga, Chlamydomonas reinhardi." Journal of Plant Physiology 157, no. 6 (2000): 707–11. http://dx.doi.org/10.1016/s0176-1617(00)80015-2.

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10

Baker, E. J., L. R. Keller, J. A. Schloss, and J. L. Rosenbaum. "Protein synthesis is required for rapid degradation of tubulin mRNA and other deflagellation-induced RNAs in Chlamydomonas reinhardi." Molecular and Cellular Biology 6, no. 1 (1986): 54–61. http://dx.doi.org/10.1128/mcb.6.1.54.

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After flagellar detachment in Chlamydomonas reinhardi, there is a rapid synthesis and accumulation of mRNAs for tubulin and other flagellar proteins. Maximum levels of these mRNAs (flagellar RNAs) are reached within 1 h after deflagellation, after which they are rapidly degraded to their predeflagellation levels. The degradation of alpha- and beta-tubulin RNAs was shown to be due to the shortening of their half-lives after accumulation (Baker et al., J. Cell Biol. 99:2074-2081, 1984). Deflagellation in the presence of protein synthesis inhibitors results in the accumulation of tubulin and othe

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11

Baker, E. J., L. R. Keller, J. A. Schloss, and J. L. Rosenbaum. "Protein synthesis is required for rapid degradation of tubulin mRNA and other deflagellation-induced RNAs in Chlamydomonas reinhardi." Molecular and Cellular Biology 6, no. 1 (1986): 54–61. http://dx.doi.org/10.1128/mcb.6.1.54-61.1986.

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After flagellar detachment in Chlamydomonas reinhardi, there is a rapid synthesis and accumulation of mRNAs for tubulin and other flagellar proteins. Maximum levels of these mRNAs (flagellar RNAs) are reached within 1 h after deflagellation, after which they are rapidly degraded to their predeflagellation levels. The degradation of alpha- and beta-tubulin RNAs was shown to be due to the shortening of their half-lives after accumulation (Baker et al., J. Cell Biol. 99:2074-2081, 1984). Deflagellation in the presence of protein synthesis inhibitors results in the accumulation of tubulin and othe

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12

Goodenough, U. W., and J. E. Heuser. "The Chlamydomonas cell wall and its constituent glycoproteins analyzed by the quick-freeze, deep-etch technique." Journal of Cell Biology 101, no. 4 (1985): 1550–68. http://dx.doi.org/10.1083/jcb.101.4.1550.

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Using the quick-freeze, deep-etch technique, we have analyzed the structure of the intact cell wall of Chlamydomonas reinhardi, and have visualized its component glycoproteins after mechanical shearing and after depolymerization induced by perchlorate or by the wall-disrupting agent, autolysin. The intact wall has previously been shown in a thin-section study (Roberts, K., M. Gurney-Smith, and G. J. Hills, 1972, J. Ultrastruct. Res. 40:599-613) to consist of a discrete central triplet bisecting a meshwork of fibrils. The deep-etch technique provides additional information about the architectur

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13

Kloppstech, Klaus, Gabriele Meyer, Gadi Schuster, and Itzhak Ohad. "Synthesis, transport and localization of a nuclear coded 22-kd heat-shock protein in the chloroplast membranes of peas and Chlamydomonas reinhardi." EMBO Journal 4, no. 8 (1985): 1901–9. http://dx.doi.org/10.1002/j.1460-2075.1985.tb03869.x.

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14

Podstavková, Svetlana, Daniel Vlček, Eva Miadoková, and Andrea Slivková. "The localization of Chlamydomonas reinhardtii repair genes." Algological Studies/Archiv für Hydrobiologie, Supplement Volumes 82 (November 21, 1996): 97–102. http://dx.doi.org/10.1127/algol_stud/82/1996/97.

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15

Stepanov, S. S. "Stimulation of accumulation of lipid bodies in Chlamydomonas reinhardtii cells." Studia Biologica 10, no. 3–4 (2016): 165–68. http://dx.doi.org/10.30970/sbi.1003.482.

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16

Lechtreck, Karl F. "Chlamydomonas reinhardtii as a model for flagellar assembly." Perspectives in Phycology 1, no. 1 (2014): 41–51. http://dx.doi.org/10.1127/2198-011x/2014/0006.

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17

Vlčková, Viera, Svetlana Podstavková, Miroslava Slaninová, Eva Miadoková, and Daniel Vlček. "The green alga Chlamydomonas reinhardtii: bioactivator of nitrosoamines." Algological Studies/Archiv für Hydrobiologie, Supplement Volumes 100 (December 20, 2000): 181–93. http://dx.doi.org/10.1127/algol_stud/100/2000/181.

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18

Craig, Rory J., Ahmed R. Hasan, Rob W. Ness, and Peter D. Keightley. "Comparative genomics of Chlamydomonas." Plant Cell 33, no. 4 (2021): 1016–41. http://dx.doi.org/10.1093/plcell/koab026.

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Abstract Despite its role as a reference organism in the plant sciences, the green alga Chlamydomonas reinhardtii entirely lacks genomic resources from closely related species. We present highly contiguous and well-annotated genome assemblies for three unicellular C. reinhardtii relatives: Chlamydomonas incerta, Chlamydomonas schloesseri, and the more distantly related Edaphochlamys debaryana. The three Chlamydomonas genomes are highly syntenous with similar gene contents, although the 129.2 Mb C. incerta and 130.2 Mb C. schloesseri assemblies are more repeat-rich than the 111.1 Mb C. reinhard

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19

KLOPPSTECH, Klaus, and Itzhak OHAD. "Heat-shock protein synthesis in Chlamydomonas reinhardi. Translational control at the level of initiation of a poly(A)-rich-RNA coded 22-KDa protein in a cell-free system." European Journal of Biochemistry 154, no. 1 (1986): 63–68. http://dx.doi.org/10.1111/j.1432-1033.1986.tb09359.x.

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20

Husic, H. David. "Extracellular carbonic anhydrase of Chlamydomonas reinhardtii: localization, structural properties, and catalytic properties." Canadian Journal of Botany 69, no. 5 (1991): 1079–87. http://dx.doi.org/10.1139/b91-138.

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In the unicellular green alga Chlamydomonas reinhardtii, a form of the enzyme carbonic anhydrase that is localized outside of the plasma membrane is an inducible component of a system that is involved in inorganic carbon acquisition and concentration from the growth medium. This article contains a review and analysis of the current literature regarding the extracellular carbonic anhydrase from Chlamydomonas reinhardtii and presents some new studies on its extracellular localization, physiological role in inorganic carbon acquisition, and some of the structural and catalytic properties of the e

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21

Stauber, Einar J., and Michael Hippler. "Chlamydomonas reinhardtii proteomics." Plant Physiology and Biochemistry 42, no. 12 (2004): 989–1001. http://dx.doi.org/10.1016/j.plaphy.2004.09.008.

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22

Roesler, Keith R., and William L. Ogren. "Chlamydomonas reinhardtii Phosphoribulokinase." Plant Physiology 93, no. 1 (1990): 188–93. http://dx.doi.org/10.1104/pp.93.1.188.

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23

Koblenz, Bettina, and Karl-Ferdinand Lechtreck. "The NIT1 Promoter Allows Inducible and Reversible Silencing of Centrin in Chlamydomonas reinhardtii." Eukaryotic Cell 4, no. 11 (2005): 1959–62. http://dx.doi.org/10.1128/ec.4.11.1959-1962.2005.

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ABSTRACT An inverted repeat corresponding to parts of the centrin gene of Chlamydomonas reinhardtii was placed downstream of the NIT1 promoter, which is induced by ammonium starvation. After induction, transformants developed centrin deficiency as assayed by immunofluorescence, Western blotting, and Northern blotting. The effect was reversible, demonstrating that the NIT1 promoter allowed controlled RNA interference in Chlamydomonas reinhardtii.

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24

Stepanov, S. S. "Accumulation of neutral lipids in the cells of Chlamydomonas reinhardtii under stress conditions." Fiziologia rastenij i genetika 48, no. 5 (2016): 401–15. http://dx.doi.org/10.15407/frg2016.05.401.

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25

Gibbs, Martin, Rene P. Gfeller, and Changguo Chen. "Fermentative Metabolism of Chlamydomonas reinhardii." Plant Physiology 82, no. 1 (1986): 160–66. http://dx.doi.org/10.1104/pp.82.1.160.

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26

Dimitrova, Maria, Evgeniya Dimova, Zhana Mitrovska, Veneta Kapchina-Toteva, and Stephka Chankova. "Testing of polluted soil samples for genotoxic potential using Chlamydomonas reinhardtii." Algological Studies 123 (May 1, 2007): 111–21. http://dx.doi.org/10.1127/1864-1318/2007/0123-0111.

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27

Brown, L. E., S. L. Sprecher, and L. R. Keller. "Introduction of exogenous DNA into Chlamydomonas reinhardtii by electroporation." Molecular and Cellular Biology 11, no. 4 (1991): 2328–32. http://dx.doi.org/10.1128/mcb.11.4.2328.

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The fate of exogenous DNA introduced into Chlamydomonas reinhardtii by electroporation was analyzed. With single and double electrical pulses, plasmids as large as 14 kb were introduced into cells with and without intact cell walls. Within hours after introduction, exogenous plasmid DNA was associated with nuclei isolated from cells; several weeks after introduction, exogenous DNA was stably integrated into the Chlamydomonas genome. These studies establish electroporation as a method for introducing DNA, and potentially other molecules, into C. reinhardtii.

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Brown, L. E., S. L. Sprecher, and L. R. Keller. "Introduction of exogenous DNA into Chlamydomonas reinhardtii by electroporation." Molecular and Cellular Biology 11, no. 4 (1991): 2328–32. http://dx.doi.org/10.1128/mcb.11.4.2328-2332.1991.

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The fate of exogenous DNA introduced into Chlamydomonas reinhardtii by electroporation was analyzed. With single and double electrical pulses, plasmids as large as 14 kb were introduced into cells with and without intact cell walls. Within hours after introduction, exogenous plasmid DNA was associated with nuclei isolated from cells; several weeks after introduction, exogenous DNA was stably integrated into the Chlamydomonas genome. These studies establish electroporation as a method for introducing DNA, and potentially other molecules, into C. reinhardtii.

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29

Hou, Qintang, Shi Qiu, Qiong Liu, Jing Tian, Zhangli Hu, and Jiazuan Ni. "Selenoprotein-Transgenic Chlamydomonas reinhardtii." Nutrients 5, no. 3 (2013): 624–36. http://dx.doi.org/10.3390/nu5030624.

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30

Matagne, R. F., C. Remacle, and M. Dinant. "Cytoduction in Chlamydomonas reinhardtii." Proceedings of the National Academy of Sciences 88, no. 16 (1991): 7447–50. http://dx.doi.org/10.1073/pnas.88.16.7447.

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31

Hamilton, Bradford S., Kazuo Nakamura, and Daniel A. K. Roncari. "Accumulation of starch in Chlamydomonas reinhardtii flagellar mutants." Biochemistry and Cell Biology 70, no. 3-4 (1992): 255–58. http://dx.doi.org/10.1139/o92-039.

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Paralyzed flagellar mutants pf-1, pf-2, pf-7, and pf-18 of the green alga Chlamydomonas reinhardtii (Dangeard) were shown to store a significantly greater amount of starch than the motile wild type 137c+. The increase in starch storage was significant relative to protein, chlorophyll, and cell number. Analysis of average cell size revealed that the paralyzed mutants were larger than the wild type. This increase in storage molecule accumulation supports an inverse relationship between chemical energy storage and energy utilization for biomechanical/motile cellular functions. Chlamydomonas reinh

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32

Goto, K., and C. H. Johnson. "Is the cell division cycle gated by a circadian clock? The case of Chlamydomonas reinhardtii." Journal of Cell Biology 129, no. 4 (1995): 1061–69. http://dx.doi.org/10.1083/jcb.129.4.1061.

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Circadian oscillators are known to regulate the timing of cell division in many organisms. In the case of Chlamydomonas reinhardtii, however, this conclusion has been challenged by several investigators. We have reexamined this issue and find that the division behavior of Chlamydomonas meets all the criteria for circadian rhythmicity: persistence of a cell division rhythm (a) with a period of approximately 24 h under free-running conditions, (b) that is temperature compensated, and (c) which can entrain to light/dark signals. In addition, a mutation that lengthens the circadian period of the p

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33

Volgusheva, Alena, Galina Kukarskikh, Tatyana Krendeleva, Andrey Rubin, and Fikret Mamedov. "Hydrogen photoproduction in green algae Chlamydomonas reinhardtii under magnesium deprivation." RSC Advances 5, no. 8 (2015): 5633–37. http://dx.doi.org/10.1039/c4ra12710b.

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34

Miadoková, Eva, Svetlana Podstavková, and Daniel Vlček. "Caffeine effects on UV-mutability of repair-deficient strains of Chlamydomonas reinhardtii." Algological Studies/Archiv für Hydrobiologie, Supplement Volumes 79 (December 14, 1995): 109–17. http://dx.doi.org/10.1127/algol_stud/79/1995/109.

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35

Kselíková, Veronika, Vilém Zachleder, and Kateřina Bišová. "To Divide or Not to Divide? How Deuterium Affects Growth and Division of Chlamydomonas reinhardtii." Biomolecules 11, no. 6 (2021): 861. http://dx.doi.org/10.3390/biom11060861.

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Extensive in vivo replacement of hydrogen by deuterium, a stable isotope of hydrogen, induces a distinct stress response, reduces cell growth and impairs cell division in various organisms. Microalgae, including Chlamydomonas reinhardtii, a well-established model organism in cell cycle studies, are no exception. Chlamydomonas reinhardtii, a green unicellular alga of the Chlorophyceae class, divides by multiple fission, grows autotrophically and can be synchronized by alternating light/dark regimes; this makes it a model of first choice to discriminate the effect of deuterium on growth and/or d

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36

Nakamura, Kazuo, Charles F. Landry, Christine A. Goertzen, and N. Wayne Ikebuchi. "Limited uptake as a mechanism for the nonrecoverability of arginine auxotrophs in Chlamydomonas eugametos." Canadian Journal of Botany 63, no. 5 (1985): 909–15. http://dx.doi.org/10.1139/b85-120.

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To address the problem of amino acid auxotroph scarcities in algae, an explanation was sought specifically for the nonrecoverability of arginine auxotrophs in the unicellular green alga Chlamydomonas eugametos. Chlamydomonas reinhardtii, in which the auxotroph has been recovered, was taken as a reference. In C. eugametos, unlike previously reported in C. reinhardtii, the use of selective media free of [Formula: see text] appeared not to affect the mutation spectrum. Arginine supported growth as the sole nitrogen source and canavanine sulfate inhibited growth, but both effects were less pronoun

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37

Hotter, Vivien, David Zopf, Hak Joong Kim, et al. "A polyyne toxin produced by an antagonistic bacterium blinds and lyses a Chlamydomonad alga." Proceedings of the National Academy of Sciences 118, no. 33 (2021): e2107695118. http://dx.doi.org/10.1073/pnas.2107695118.

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Algae are key contributors to global carbon fixation and form the basis of many food webs. In nature, their growth is often supported or suppressed by microorganisms. The bacterium Pseudomonas protegens Pf-5 arrests the growth of the green unicellular alga Chlamydomonas reinhardtii, deflagellates the alga by the cyclic lipopeptide orfamide A, and alters its morphology [P. Aiyar et al., Nat. Commun. 8, 1756 (2017)]. Using a combination of Raman microspectroscopy, genome mining, and mutational analysis, we discovered a polyyne toxin, protegencin, which is secreted by P. protegens, penetrates the

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38

Bertiaux-Lequoy, Eloïse, Philippe Hammel, Virginie Hamel, and Paul Guichard. "The RB530 antibody recognizes microtubules by immunofluorescence." Antibody Reports 2, no. 4 (2019): e65. http://dx.doi.org/10.24450/journals/abrep.2019.e65.

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39

Yogesha, M., Venkatramanan G. Rao, Elvis A. F. Martis, et al. "Structural features of FAP174, a MYCBP-1 orthologue from Chlamydomonas reinhardtii, revealed by computational and experimental analyses." RSC Advances 7, no. 81 (2017): 51391–402. http://dx.doi.org/10.1039/c7ra07836f.

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40

PRÖSCHOLD, THOMAS, TATYANA DARIENKO, LOTHAR KRIENITZ, and ANNETTE W. COLEMAN. "Chlamydomonas schloesseri sp. nov. (Chlamydophyceae, Chlorophyta) revealed by morphology, autolysin cross experiments, and multiple gene analyses." Phytotaxa 362, no. 1 (2018): 21. http://dx.doi.org/10.11646/phytotaxa.362.1.2.

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Chlamydomonas in the traditional sense is one of the largest green algal genera, comprising more than 500 described species. However, since the designation of the model organism C. reinhardtii as conserved type of this genus in 2007, only two species remained in Chlamydomonas. Investigations of three new strains isolated from soil samples, which were collected near Lake Nakuru (Kenya), demonstrated that the isolates represent a new species of Chlamydomonas. Phylogenetic analyses of nuclear SSU and ITS rDNA and plastid-coding rbcL sequences have clearly revealed that this species is closely rel

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41

Tural, Baran, and James V. Moroney. "Regulation of the expression of photorespiratory genes inChlamydomonas reinhardtii." Canadian Journal of Botany 83, no. 7 (2005): 810–19. http://dx.doi.org/10.1139/b05-066.

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The regulation of the photorespiratory pathway in Chlamydomonas reinhardtii Dangeard during a shift from high- to low-CO2conditions was investigated. To this end, a set of C. reinhardtii cDNA sequences for known photorespiratory enzymes was assembled using the Chlamydomonas expressed sequence tag database and primary sequencing data. Expression data indicates that there is a rapid and coordinated induction of photorespiratory and CCM gene expression during a time course switch from high-CO2conditions (5% (v/v)) to low-CO2conditions (0.038% (v/v)). While the expression of photorespiratory and C

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42

Thomas, James E., Christine A. Goertzen, and Kazuo Nakamura. "Heterogeneity in endogenous amino acid pools of Chlamydomonas reinhardtii and C. eugametos." Canadian Journal of Botany 69, no. 6 (1991): 1194–98. http://dx.doi.org/10.1139/b91-153.

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Levels of endogenous amino acid pools were measured for two species of the unicellular green alga Chlamydomonas. In C. reinhardtii, opposite mating types, designated + and −, of strain 137c were examined. The soluble pool of glutamic acid was most abundant in strain 137c−. In strain 137c+ similar levels of this amino acid were present, and high levels of cystine were observed. A soluble pool for the amino acid methionine was not detected in either strain. In opposite mating types of C. eugametos (strain Nos. 9 and 10), a soluble pool of alanine was most abundant, whereas neither cystine nor me

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43

Hu, Shengxi, Ken W. K. Lau, and Madeline Wu. "Cadmium sequestration in Chlamydomonas reinhardtii." Plant Science 161, no. 5 (2001): 987–96. http://dx.doi.org/10.1016/s0168-9452(01)00501-5.

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44

Gfeller, Rene P., and Martin Gibbs. "Fermentative Metabolism of Chlamydomonas reinhardtii." Plant Physiology 77, no. 2 (1985): 509–11. http://dx.doi.org/10.1104/pp.77.2.509.

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Maul, Jude E., Jason W. Lilly, Liying Cui, et al. "The Chlamydomonas reinhardtii Plastid Chromosome." Plant Cell 14, no. 11 (2002): 2659–79. http://dx.doi.org/10.1105/tpc.006155.

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Beck, Christoph F., and Axel Acker. "Gametic Differentiation of Chlamydomonas reinhardtii." Plant Physiology 98, no. 3 (1992): 822–26. http://dx.doi.org/10.1104/pp.98.3.822.

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SILFLOW, CAROLYN D., and JAMES YOUNGBLOM. "Chlamydomonas reinhardtii Tubulin Gene Structure." Annals of the New York Academy of Sciences 466, no. 1 Dynamic Aspec (1986): 18–30. http://dx.doi.org/10.1111/j.1749-6632.1986.tb38381.x.

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Zhu, Chi, Chuanhong Chen, Liangyuan Zhao, et al. "Bioflocculant produced by Chlamydomonas reinhardtii." Journal of Applied Phycology 24, no. 5 (2011): 1245–51. http://dx.doi.org/10.1007/s10811-011-9769-x.

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Holmes, J. A., and S. K. Dutcher. "Cellular asymmetry in Chlamydomonas reinhardtii." Journal of Cell Science 94, no. 2 (1989): 273–85. http://dx.doi.org/10.1242/jcs.94.2.273.

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Abstract:

Although largely bilaterally symmetric, the two sides of the unicellular alga Chlamydomonas reinhardtii can be distinguished by the location of the single eyespot. When viewed from the anterior end, the eyespot is always closer to one flagellum than the other, and located at an angle of approximately 45 degrees clockwise of the flagellar plane. This location correlates with the position of one of four acetylated microtubule bundles connected to the flagellar apparatus. Each basal body is attached to two of these microtubule rootlets. The rootlet that positions the eyespot is always attached to

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Chen, Zhenzhong, and Won Gu Lee. "A switching role of hard-uptake nanoparticles in microalgae cell electroporation." Analyst 144, no. 11 (2019): 3581–89. http://dx.doi.org/10.1039/c9an00314b.

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