Chlamydomonas reinhardtii

The biflagellate unicellular green alga Chlamydomonas reinhardtii is prone to spontaneous mutations that produce deficiencies in flagellar proteins and MT assembly, substructure, and function. Viable mutants that are either nonmotile or slow moving can be isolated and analyzed biochemically and morphologically, thereby establishing structure-function correlations. Electron microscopic analysis... [Pg.11]

Huang, B. (1986). Chlamydomonas reinhardtii. A model system for genetic analysis of flagellar structure and motility. Inti. Rev. Cytol. 99, 181-215. [Pg.39]

Holub, O., Seufferheld, M. J., Gohlke, C., Govindjee, G. J., Heiss, G. J. and Clegg, R. M. (2007). Fluorescence lifetime imaging microscopy of Chlamydomonas reinhardtii Non-photochemical quenching mutants and the effect of photosynthetic inhibitors on the slow chlorophyll fluorescence transients. J. Microsc. 226, 90-120. [Pg.63]

Y. Sakihama, S. Nakamura, and H. Yamasaki, Nitric oxide production mediated by nitrate reductase in the green alga Chlamydomonas reinhardtii an alternative NO production pathway in photosynthetic organisms. Plant Cell Physiol. 43, 290-297 (2002). [Pg.51]

Simple plants Physcomitrella patens Chlamydomonas reinhardtii Lemna minor Containment, clonal propagation, batch consistency, secretion of proteins into medium, regulatory compliance, homologous recombination in Physcomitrella Scalability... [Pg.193]

Green alga (fresh water), Chlamydomonas reinhardtii 18 pg/L for 24 h... [Pg.179]

Winner, R.W. and H.A. Owen. 1991. Toxicity of copper to Chlamydomonas reinhardtii (Chlorophyceae) and Ceriodaphnia dubia (Crustacea) in relation to changes in water chemistry of a freshwater pond. Aquat. Toxicol. 21 157-170. [Pg.234]

Behra, R. 1993. In vitro effects of cadmium, zinc and lead on calmodulin-dependent actions in Oncorhynchus mykiss, Mytilus sp., and Chlamydomonas reinhardtii. Arch. Environ. Contam. Toxicol. 24 21-27. [Pg.325]

R. Debuchy, S. Purton, JD. Rochaix (1989) The arginino-succinate lyase gene of Chlamydomonas reinhardtii an important tool for nuclear transformation and for correlating the genetic and molecular maps of the ARG7 locus. EMBOJ., 8 2803-2809... [Pg.114]

EL. De Hostos, J. Schilling, AR. Grossman (1989) Structure and expression of the gene encoding the periplasmatic arylsulfatase of Chlamydomonas reinhardtii. Mol. Gen. Genet., 218 229-239... [Pg.114]

T. Happe, JD. Naber (1993) Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii. Eur. J. Biochem., 214 475-481... [Pg.114]

KL. Kindle (1990) High frequency nuclear transformation of Chlamydomonas reinhardtii. Proc. Natl. Acad Sci. USA, 87 1228-1232... [Pg.115]

IDENTIFICATION OF A CVS-ACTING ELEMENT CONTROLLING ANAEROBIC EXPRESSION OF THE HYDA GENE FROM CHLAMYDOMONAS REINHARDTII... [Pg.117]

J. P. Davies, D. P. Weeks, A. R Grossman (1992) Expression of the arylsulfatase gene from the C2-tubulin promoter in Chlamydomonas reinhardtii. Nttcl. Acids Res., 20 2959-2965... [Pg.126]

D. Hahn U. Kiick (1999) Identification of DNA sequences controlling light-and chloroplast-dependent expression of the Ihcbl gene from Chlamydomonas reinhardtii. Curr. Genet, 34 459-466... [Pg.126]

U. Johanningmeier, S. H. Howell (1984) Regulation of light-harvesting chlorophyll-binding protein mRNA accumulation in Chlamydomonas reinhardtii. Possible involvement of chlorophyll synthesis precursors. J. Biol. Chem., 259 13541-13549... [Pg.127]

T. Lien, O. Schreiner (1975) Purification of a derepressible arylsulfatase from Chlamydomonas reinhardtii. Biochim. Biophys. Acta, 384 168-179... [Pg.127]

S. Purton, J.-D. Rochaix (1994) Characterization of the arg7 gene of Chlamydomonas reinhardtii and its application to nuclear transformation. Eur. J. Phycol., 30 141-148... [Pg.127]

J. M. Quinn, M. Eriksson, J. L. Moseley, S. Merchant (2002) Oxygen deficiency responsive gene expression in Chlamydomonas reinhardtii through a copper-sensing signal transduction pathway. Plant Physiol., 128 463-471... [Pg.127]

PS1 The PS 1-prep, introduced in this communication is the first reported with a polyhistidine tag fused to the N-terminus of the PsaF subunit. This construct was possible due to the fact that cyanobacterial PsaF-deletion mutants show no impact on photoautotrophic growth - in contrast to Chlamydomonas reinhardtii, where inactivation of PsaF results in a severe reduction of electron transfer from plastocyanin to PS 1 [Hippier et al. 1997], Also, the N-terminus of the F-subunit which was decorated by the tag is located towards the lumen side which enables an attachment of the isolated PS1 with the lumen-exposed /donor-side to the electrode surface in our hydrogen-producing device. [Pg.177]

Hippier, M., F. Drepper, J. Farah and J. D. Rochaix (1997) Fast electron transfer from cytochrome c6 and plastocyanin to photosystem I of Chlamydomonas reinhardtii requires PsaF. Biochemistry, 36 6343-6349... [Pg.178]

Among the trace metals, Hudson and Morel [7] postulated that Fe and Zn were closest to a diffusion-limited situation based upon measured cellular metal quotas and concentrations in marine systems (e.g. Zn would be diffusion limited for cells > 20 pm). Similarly, Hassler and Wilkinson [90] showed that for cells grown under conditions of Zn starvation, transport was diffusion limited for [Zn2+] < 10 12 mol dm. Fortin and Campbell [91] showed that, in the presence of chloride, the Ag transport flux to Chlamydomonas reinhardtii was close to a diffusion limitation at the lower Ag concentrations that were examined. Diffusion limitation of trace metals is most likely in systems where the concentrations are low and concentrations of competing metals are high, especially for essential metals that are taken up by passive diffusion across the membrane [8], The final point of essentiality could be especially important when transport systems are upregulated in response to lowmetal concentrations (see also Section 2.2 [90,92]). [Pg.462]

See also in sourсe #XX -- [ Pg.203 ]

See also in sourсe #XX -- [ Pg.67 , Pg.145 , Pg.257 , Pg.1107 , Pg.1108 , Pg.1109 , Pg.1655 ]

See also in sourсe #XX -- [ Pg.123 ]

See also in sourсe #XX -- [ Pg.75 ]

See also in sourсe #XX -- [ Pg.67 , Pg.145 , Pg.257 , Pg.1107 , Pg.1108 , Pg.1109 , Pg.1655 ]

See also in sourсe #XX -- [ Pg.160 ]

See also in sourсe #XX -- [ Pg.9 ]

See also in sourсe #XX -- [ Pg.214 ]

See also in sourсe #XX -- [ Pg.26 , Pg.46 , Pg.86 , Pg.105 , Pg.108 , Pg.126 , Pg.136 , Pg.137 ]

See also in sourсe #XX -- [ Pg.40 , Pg.61 , Pg.94 , Pg.117 , Pg.164 ]

See also in sourсe #XX -- [ Pg.235 , Pg.246 , Pg.251 ]

See also in sourсe #XX -- [ Pg.57 ]

See also in sourсe #XX -- [ Pg.262 , Pg.287 ]

See also in sourсe #XX -- [ Pg.795 , Pg.1422 ]

See also in sourсe #XX -- [ Pg.235 , Pg.246 , Pg.251 ]

See also in sourсe #XX -- [ Pg.9 ]

See also in sourсe #XX -- [ Pg.26 , Pg.364 ]

See also in sourсe #XX -- [ Pg.14 , Pg.127 , Pg.299 ]

See also in sourсe #XX -- [ Pg.364 ]

See also in sourсe #XX -- [ Pg.592 ]

See also in sourсe #XX -- [ Pg.16 , Pg.32 , Pg.46 , Pg.47 , Pg.48 , Pg.50 , Pg.51 , Pg.53 , Pg.58 , Pg.73 , Pg.112 , Pg.113 , Pg.152 , Pg.194 , Pg.197 , Pg.198 , Pg.199 , Pg.206 ]

See also in sourсe #XX -- [ Pg.250 , Pg.252 ]

See also in sourсe #XX -- [ Pg.160 ]

See also in sourсe #XX -- [ Pg.59 , Pg.76 , Pg.498 ]

See also in sourсe #XX -- [ Pg.86 , Pg.87 ]

See also in sourсe #XX -- [ Pg.15 ]

See also in sourсe #XX -- [ Pg.82 ]

See also in sourсe #XX -- [ Pg.35 ]

See also in sourсe #XX -- [ Pg.82 , Pg.83 ]

See also in sourсe #XX -- [ Pg.68 , Pg.70 ]

See also in sourсe #XX -- [ Pg.179 , Pg.411 ]

Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...