Chlamydomonas Raudensis Research Articles

Cyclic electron flow (CEF) and ascorbate pathway activity provide constitutive photoprotection for the photopsychrophile, Chlamydomonas sp. UWO 241(renamed Chlamydomonas priscuii).

Under environmental stress, plants and algae employ a variety of strategies to protect the photosynthetic apparatus and maintain photostasis. To date, most studies on stress acclimation have focused on model organisms which possess limited to no tolerance to stressful extremes. We studied the ability of the Antarctic alga Chlamydomonas sp. UWO 241 (UWO 241) to acclimate to low temperature, high salinity or high light. UWO 241 maintained robust growth and photosynthetic activity at levels of temperature (2°C) and salinity (700mM NaCl) which were nonpermissive for a mesophilic sister species, Chlamydomonas raudensis SAG 49.72 (SAG 49.72). Acclimation in the mesophile involved classic mechanisms, including downregulation of light harvesting and shifts in excitation energy between photosystem I and II. In contrast, UWO 241 exhibited high rates of PSI-driven cyclic electron flow (CEF) and a larger capacity for nonphotochemical quenching (NPQ). Furthermore, UWO 241 exhibited constitutively high activity of two key ascorbate cycle enzymes, ascorbate peroxidase and glutathione reductase and maintained a large ascorbate pool. These results matched the ability of the psychrophile to maintain low ROS under short-term photoinhibition conditions. We conclude that tight control over photostasis and ROS levels are essential for photosynthetic life to flourish in a native habitat of permanent photooxidative stress.We propose to rename this organism Chlamydomonas priscuii.

Resolving the phylogenetic relationship between Chlamydomonas sp. UWO 241 and Chlamydomonas raudensis sag 49.72 (Chlorophyceae) with nuclear and plastid DNA sequences.

The Antarctic psychrophilic green alga Chlamy‐domonas sp. UWO 241 is an emerging model for studying microbial adaptation to polar environments. However, little is known about its evolutionary history and its phylogenetic relationship with other chlamydomonadalean algae is equivocal. Here, we attempt to clarify the phylogenetic position of UWO 241, specifically with respect to Chlamydomonas rau‐densis SAG 49.72. Contrary to a previous report, we show that UWO 241 is a distinct species from SAG 49.72. Our phylogenetic analyses of nuclear and plastid DNA sequences reveal that UWO 241 represents a unique lineage within the Moewusinia clade (sensu Nakada) of the Chlamydomonadales (Chlorophyceae, Chlorophyta), closely affiliated to the marine species Chlamydomonas parkeae SAG 24.89.

The Antarctic Psychrophile Chlamydomonas sp. UWO 241 Preferentially Phosphorylates a Photosystem I-Cytochrome b6/f Supercomplex.

Chlamydomonas sp. UWO 241 (UWO 241) is a psychrophilic green alga isolated from Antarctica. A unique characteristic of this algal strain is its inability to undergo state transitions coupled with the absence of photosystem II (PSII) light-harvesting complex protein phosphorylation. We show that UWO 241 preferentially phosphorylates specific polypeptides associated with an approximately 1,000-kD pigment-protein supercomplex that contains components of both photosystem I (PSI) and the cytochrome b₆/f (Cyt b₆/f) complex. Liquid chromatography nano-tandem mass spectrometry was used to identify three major phosphorylated proteins associated with this PSI-Cyt b₆/f supercomplex, two 17-kD PSII subunit P-like proteins and a 70-kD ATP-dependent zinc metalloprotease, FtsH. The PSII subunit P-like protein sequence exhibited 70.6% similarity to the authentic PSII subunit P protein associated with the oxygen-evolving complex of PSII in Chlamydomonas reinhardtii. Tyrosine-146 was identified as a unique phosphorylation site on the UWO 241 PSII subunit P-like polypeptide. Assessment of PSI cyclic electron transport by in vivo P700 photooxidation and the dark relaxation kinetics of P700(+) indicated that UWO 241 exhibited PSI cyclic electron transport rates that were 3 times faster and more sensitive to antimycin A than the mesophile control, Chlamydomonas raudensis SAG 49.72. The stability of the PSI-Cyt b₆/f supercomplex was dependent upon the phosphorylation status of the PsbP-like protein and the zinc metalloprotease FtsH as well as the presence of high salt. We suggest that adaptation of UWO 241 to its unique low-temperature and high-salt environment favors the phosphorylation of a PSI-Cyt b₆/f supercomplex to regulate PSI cyclic electron transport rather than the regulation of state transitions through the phosphorylation of PSII light-harvesting complex proteins.

Photoadaptation to the polar night by phytoplankton in a permanently ice-covered Antarctic lake

Photosynthetic microorganisms are a primary source of new organic carbon production in polar ecosystems. Despite their importance, relatively little is known about how they adapt to the bimodal solar cycles that exist at high latitudes. To understand how phytoplankton adapt to the extreme seasonal change in photoperiod, we transplanted cultures of a well-studied laboratory model for photosynthetic cold adaptation, Chlamydomonas raudensis UWO241, back to the water column of Lake Bonney (McMurdo Dry Valleys, Antarctica) at the depth from which it was originally cultured. The organism was suspended at this depth in dialysis tubing to allow the microalga to respond to the in situ light, temperature and dissolved ions. We then integrated in situ biological and chemical measurements with environmental molecular analyses and compared the responses of transplanted C. raudensis cultures with the natural phytoplankton community over the 6-week transition from Antarctic summer (24-h daylight) to polar night (24-h darkness). As solar radiation declined, natural communities exhibited a cessation of inorganic carbon fixation which was accompanied by a downregulation of expression of genes encoding for essential carbon fixation and photochemistry proteins. Transplanted C. raudensis cultures matched natural community trends in the regulation of photochemistry and carbon fixation gene expression, and shifted photochemical function to a shade adapted state in response to the polar night transition. We present a conceptual model for seasonal shifts in microbial community energy and carbon acquisition which integrates past cultivation-based studies in this model photopsychrophile with a body of recent work on adaptation of natural populations to polar night.

Review: the Antarctic Chlamydomonas raudensis: an emerging model for cold adaptation of photosynthesis

Permanently cold habitats dominate our planet and psychrophilic microorganisms thrive in cold environments. Environmental adaptations unique to psychrophilic microorganisms have been thoroughly described; however, the vast majority of studies to date have focused on cold-adapted bacteria. The combination of low temperatures in the presence of light is one of the most damaging environmental stresses for a photosynthetic organism: in order to survive, photopsychrophiles (i.e. photosynthetic organisms adapted to low temperatures) balance temperature-independent reactions of light energy capture/transduction with downstream temperature-dependent metabolic processes such as carbon fixation. Here, we review research on photopsychrophiles with a focus on an emerging model organism, Chlamydomonas raudensis UWO241 (UWO241). UWO241 is a psychrophilic green algal species and is a member of the photosynthetic microbial eukaryote community that provides the majority of fixed carbon for ice-covered lake ecosystems located in the McMurdo Dry Valleys, Antarctica. The water column exerts a range of environmental stressors on the phytoplankton community that inhabits this aquatic ecosystem, including low temperatures, extreme shade of an unusual spectral range (blue-green), high salinity, nutrient deprivation and extremes in seasonal photoperiod. More than two decades of work on UWO241 have produced one of our most comprehensive views of environmental adaptation in a cold-adapted, photosynthetic microbial eukaryote.

Separate Origins of Ice-Binding Proteins in Antarctic Chlamydomonas Species

The green alga Chlamydomonas raudensis is an important primary producer in a number of ice-covered lakes and ponds in Antarctica. A C. raudensis isolate (UWO241) from Lake Bonney in the McMurdo Dry Valleys, like many other Antarctic algae, was found to secrete ice-binding proteins (IBPs), which appear to be essential for survival in icy environments. The IBPs of several Antarctic algae (diatoms, a prymesiophyte, and a prasinophyte) are similar to each other (here designated as type I IBPs) and have been proposed to have bacterial origins. Other IBPs (type II IBPs) that bear no resemblance to type I IBPs, have been found in the Antarctic Chlamydomonas sp. CCMP681, a putative snow alga, raising the possibility that chlamydomonad IBPs developed separately from the IBPs of other algae. To test this idea, we obtained the IBP sequences of C. raudensis UWO241 by sequencing the transcriptome. A large number of transcripts revealed no sequences resembling type II IBPs. Instead, many isoforms resembling type I IBPs were found, and these most closely matched a hypothetical protein from the bacterium Stigmatella aurantiaca. The sequences were confirmed to encode IBPs by the activity of a recombinant protein and by the matching of predicted and observed isoelectric points and molecular weights. Furthermore, a mesophilic sister species, C. raudensis SAG49.72, showed no ice-binding activity or PCR products from UWO241 IBP primers. These results confirm that algal IBPs are required for survival in icy habitats and demonstrate that they have diverse origins that are unrelated to the taxonomic positions of the algae. Last, we show that the C. raudensis UWO241 IBPs can change the structure of ice in a way that could increase the survivability of cells trapped in the ice.

Shedding some light on cold acclimation, cold adaptation, and phenotypic plasticity

In the past, the role of light as an energy source was largely ignored in research focused on cold acclimation and freezing tolerance in plants. However, cold acclimation is an energy-requiring process. We summarize research illustrating that photoautrophs as diverse as cyanobacteria (Plectonema boryanum), green algae (Chlorella vulgaris, Dunaliella salina, Chlamydomonas raudensis), crop plants (Triticum aestivum L., Secale cereale L., Brassica napus L.), and conifers (Pinus banksiana) L.) tailor the structure and function of the photosynthetic apparatus to changes in temperature and irradiance to maintain cellular energy balance called photostasis. Modulation of either temperature or irradiance results in a similar imbalance in cellular energy that is sensed through changes in chloroplastic excitation pressure. Thus, concepts of photostasis and excitation pressure provide the context through which one can explain the congruence of phenotypic plasticity and photosynthetic performance associated with cold acclimation and photoacclimation. Photosynthetic organisms can sense changes in temperature and irradiance through modulation of the redox state of the photosynthetic electron transport chain, which, in turn, governs phenotype through the regulation of nuclear gene expression and chloroplast biogenesis. We suggest that elucidation of the molecular mechanism(s) by which excitation pressure regulates phenotypic plasticity and photosynthetic performance will be essential in addressing the challenge of maintaining or perhaps enhancing crop productivity under the suboptimal growth conditions predicted to occur as a consequence of climate change.

PLASTICITY OF THE PSYCHROPHILIC GREEN ALGA CHLAMYDOMONAS RAUDENSIS (UWO 241) (CHLOROPHYTA) TO SUPRAOPTIMAL TEMPERATURE STRESS(1).

Chlamydomonas raudensis H. Ettl (UWO 241) is a psychrophilic green alga endemic to Lake Bonney, Antarctica. The objective of this study was to investigate the response of UWO 241 to incubation at 24°C, a temperature close to optimum for related mesophilic species. Using chl a fluorescence analysis, shifting cells from a growth temperature of 10°C-24°C resulted in a decline in PSII photochemical efficiency with light energy being directed away from photochemistry and toward dissipative pathways. Using the SYTOX Green assay, it was determined that UWO 241 cells die when incubated at 24°C under growth irradiance with a half-time of 34.9 h. The role of light in cell death was minor as cell death occurred in darkness at 24°C with a half-time of 43.7 h. To examine the plasticity of UWO 241 to temperature stress, 10°C-grown cells were shifted to 24°C for 12 h and then returned to 10°C to recover. The 12 h incubation at 24°C, which resulted in <10% cell death, led to declines in both light-saturated rates of photosynthesis and respiration, PSII photochemistry and energy partitioning, and changes to transcript abundances-those associated with the light-harvesting protein of PSII and ferredoxin declining rapidly, whereas transcripts of specific heat-shock proteins (HSPs) increased. Within 24-48 h of being transferred back to 10°C, all parameters returned to levels occurring in 10°C-grown cells. This research shows, for the first time, that 24°C is a temperature that is lethal to UWO 241, and yet this organism displays considerable physiological and molecular plasticity.

Evidence for phenotypic plasticity in the Antarctic extremophile Chlamydomonas raudensis Ettl. UWO 241

Life in extreme environments poses unique challenges to photosynthetic organisms. The ability for an extremophilic green alga and its genetic and mesophilic equivalent to acclimate to changes in their environment was examined to determine the extent of their phenotypic plasticities. The Antarctic extremophile Chlamydomonas raudensis Ettl. UWO 241 (UWO) was isolated from an ice-covered lake in Antarctica, whereas its mesophilic counterpart C. raudensis Ettl. SAG 49.72 (SAG) was isolated from a meadow pool in the Czech Republic. The effects of changes in temperature and salinity on growth, morphology, and photochemistry were examined in the two strains. Differential acclimative responses were observed in UWO which include a wider salinity range for growth, and broader temperature- and salt-induced fluctuations in Fv/Fm, relative to SAG. Furthermore, the redox state of the photosynthetic electron transport chain, measured as 1–qP, was modulated in the extremophile whereas this was not observed in the mesophile. Interestingly, it is shown for the first time that SAG is similar to UWO in that it is unable to undergo state transitions. The different natural histories of these two strains exert different evolutionary pressures and, consequently, different abilities for acclimation, an important component of phenotypic plasticity. In contrast to SAG, UWO relied on a redox sensing and signalling system under the growth conditions used in this study. It is proposed that growth and adaptation of UWO under a stressful and extreme environment poises this extremophile for better success under changing environmental conditions.

Salinity affects the photoacclimation of Chlamydomonas raudensis Ettl UWO241

Chlamydomonas raudensis Ettl UWO241, a natural variant of C. raudensis, is deficient in state transitions. Its habitat, the deepest layer of Lake Bonney in Antarctica, features low irradiance, low temperature, and high salinity. Although psychrophily and low-light acclimation of this green alga has been described, very little information is available on the effect of salinity. Here, we demonstrate that this psychrophile is halotolerant, not halophilic, and it shows energy redistribution between photosystem I and II based on energy spillover under low-salt conditions. Furthermore, we revealed that C. raudensis exhibits higher non-photochemical quenching in comparison with the mesophile Chlamydomonas reinhardtii, when grown with low-salt, which is due to the lower proton conductivity across the thylakoid membrane. Significance of the C. raudensis UWO241 traits found in the low salinity culture are implicated with their natural habitats, including the high salinity and extremely stable light environments.

Identity and physiology of a new psychrophilic eukaryotic green alga, Chlorella sp., strain BI, isolated from a transitory pond near Bratina Island, Antarctica

Permanently low temperature environments are one of the most abundant microbial habitats on earth. As in most ecosystems, photosynthetic organisms drive primary production in low temperature food webs. Many of these phototrophic microorganisms are psychrophilic; however, functioning of the photosynthetic processes of these enigmatic psychrophiles (the "photopsychrophiles") in cold environments is not well understood. Here we describe a new chlorophyte isolated from a low temperature pond, on the Ross Ice Shelf near Bratina Island, Antarctica. Phylogenetic and morphological analyses place this strain in the Chlorella clade, and we have named this new chlorophyte Chlorella BI. Chlorella BI is a psychrophilic species, exhibiting optimum temperature for growth at around 10 degrees C. However, psychrophily in the Antarctic Chlorella was not linked to high levels of membrane-associated poly-unsaturated fatty acids. Unlike the model Antarctic lake alga, Chlamydomonas raudensis UWO241, Chlorella BI has retained the ability for dynamic short term adjustment of light energy distribution between photosystem II (PS II) and photosystem I (PS I). In addition, Chlorella BI can grow under a variety of trophic modes, including heterotrophic growth in the dark. Thus, this newly isolated photopsychrophile has retained a higher versatility in response to environmental change than other well studied cold-adapted chlorophytes.

The small domain of cytochromeffrom the psychrophileChlamydomonas raudensisUWO 241 modulates the apparent molecular mass and decreases the accumulation of cytochromefin the mesophileChlamydomonas reinhardtii

Cytochrome f from the psychrophile Chlamydomonas raudensis UWO 241 has a lower thermostability of its c-type heme and an apparent molecular mass that is 7 kDa lower than that of the model mesophilic green alga Chlamydomonas reinhardtii. We combined chloroplast transformation, site-directed mutagensis, and the creation of chimeric fusion constructs to assess the contribution of specific domains and (or) amino acids residues to the structure, stability, and accumulation of cytochrome f, as well as its function in photosynthetic intersystem electron transport. We demonstrate that differences in the amino acid sequence of the small domain and specific charged amino acids in the large domain of cytochrome f alter the physical properties of this protein but do not affect either the thermostability of the c-type heme, the apparent half-life of cytochrome f in the presence of the chloroplastic protein synthesis inhibitor chloramphenicol, or the capacity for photosynthetic intersystem electron transport, measured as e-/P700. However, pulse-labeling with [14C]acetate, combined with immunoblotting, indicated that the negative autoregulation of cytochrome f accumulation observed in mesophilic C. reinhardtii transformed with chimeric constructs from the psychrophile was likely the result of the defective association of the chimeric forms of cytochrome f with the other subunits of the cytochrome b6/f complex native to the C. reinhardtii wild type. These results are discussed in terms of the unique fatty acid composition of the thylakoid membranes of C. raudensis UWO 241 adapted to cold environments.

Chlamydomonas raudensis (UWO 241), Chlorophyceae, exhibits the capacity for rapid D1 repair in response to chronic photoinhibition at low temperature1

Maximum photosynthetic capacity indicates that the Antarctic psychrophile Chlamydomonas raudensis H. Ettl UWO 241 is photosynthetically adapted to low temperature. Despite this finding, C. raudensis UWO 241 exhibited greater sensitivity to low‐temperature photoinhibition of PSII than the mesophile Chlamydomonas reinhardtii P. A. Dang. However, in contrast with results for C. reinhardtii, the quantum requirement to induce 50% photoinhibition of PSII in C. raudensis UWO 241 (50 μmol photons) was comparable at either 8°C or 29°C. To our knowledge, this is the first report of a photoautotroph whose susceptibility to photoinhibition is temperature independent. In contrast, the capacity of the psychrophile to recover from photoinhibition of PSII was sensitive to temperature and inhibited at 29°C. The maximum rate of recovery from photoinhibition of the psychrophile at 8°C was comparable to the maximum rate of recovery of the mesophile at 29°C. We provide evidence that photoinhibition in C. raudensis UWO 241 is chronic rather than dynamic. The photoinhibition‐induced decrease in the D1 content in C. raudensis recovered within 30 min at 8°C. Both the recovery of the D1 content as well as the initial fast phase of the recovery of Fv/Fm at 8°C were inhibited by lincomycin, a chloroplast protein synthesis inhibitor. We conclude that the susceptibility of C. raudensis UWO 241 to low‐temperature photoinhibition reflects its adaptation to low growth irradiance, whereas the unusually rapid rate of recovery at low temperature exhibited by this psychrophile is due to a novel D1 repair cycle that is adapted to and is maximally operative at low temperature.

Psychrophily is associated with differential energy partitioning, photosystem stoichiometry and polypeptide phosphorylation in Chlamydomonas raudensis

Chlamydomonas raudensis UWO 241 and SAG 49.72 represent the psychrophilic and mesophilic strains of this green algal species. This novel discovery was exploited to assess the role of psychrophily in photoacclimation to growth temperature and growth irradiance. At their optimal growth temperatures of 8 °C and 28 °C respectively, UWO 241 and SAG 49.72 maintained comparable photostasis, that is energy balance, as measured by PSII excitation pressure. Although UWO 241 exhibited higher excitation pressure, measured as 1-qL, at all growth light intensities, the relative changes in 1-qL were similar to that of SAG 49.72 in response to growth light. In response to suboptimal temperatures and increased growth irradiance, SAG 49.72 favoured energy partitioning of excess excitation energy through inducible, down regulatory processes ( Φ NPQ) associated with the xanthophyll cycle and antenna quenching, while UWO 241 favoured xanthophyll cycle-independent energy partitioning through constitutive processes involved in energy dissipation ( Φ NO). In contrast to SAG 49.72, an elevation in growth temperature induced an increase in PSI/PSII stoichiometry in UWO 241. Furthermore, SAG 49.72 showed typical threonine-phosphorylation of LHCII, whereas UWO 241 exhibited phosphorylation of polypeptides of comparable molecular mass to PSI reaction centres but the absence of LHCII phosphorylation. Thus, although both strains maintain an energy balance irrespective of their differences in optimal growth temperatures, the mechanisms used to maintain photostasis were distinct. We conclude that psychrophily in C. raudensis is complex and appears to involve differential energy partitioning, photosystem stoichiometry and polypeptide phosphorylation.

Cytochrome f from the Antarctic psychrophile, Chlamydomonas raudensis UWO 241: structure, sequence, and complementation in the mesophile, Chlamydomonas reinhardtii

Although cytochrome f from the Antarctic psychrophile, Chlamydomonas raudensis UWO 241, exhibits a lower apparent molecular mass (34 kD) than that of the mesophile C. reinhardtii (41 kD) based on SDS-PAGE, both proteins are comparable in calculated molecular mass and show 79% identity in amino acid sequence. The difference in apparent molecular mass was maintained after expression of petA from both Chlamydomonas species in either E. coli or a C. reinhardtii DeltapetA mutant and after substitution of a unique third cysteine-292 to phenylalanine in the psychrophilic cytochrome f. Moreover, the heme of the psychrophilic form of cytochrome f was less stable upon heating than that of the mesophile. In contrast to C. raudensis, a C. reinhardtii DeltapetA mutant transformed with petA from C. raudensis exhibited the ability to undergo state transitions and a capacity for intersystem electron transport comparable to that of C. reinhardtii wild type. However, the C. reinhardtii petA transformants accumulated lower levels of cytochrome b ( 6 ) /f complexes and exhibited lower light saturated rates of O(2) evolution than C. reinhardtii wild type. We show that the presence of an altered form of cytochrome f in C. raudensis does not account for its inability to undergo state transitions or its impaired capacity for intersystem electron transport as previously suggested. A combined survey of the apparent molecular mass, thermal stability and amino acid sequences of cytochrome f from a broad range of mesophilic species shows unequivocally that the observed differences in cytochrome f structure are not related to psychrophilly. Thus, caution must be exercised in relating differences in amino acid sequence and thermal stability to adaptation to cold environments.

THE ANTARCTIC PSYCHROPHILE, CHLAMYDOMONAS RAUDENSIS ETTL (UWO241) (CHLOROPHYCEAE, CHLOROPHYTA), EXHIBITS A LIMITED CAPACITY TO PHOTOACCLIMATE TO RED LIGHT1

The psychrophilic Antarctic alga, Chlamydomonas raudensis Ettl (UWO241), grows under an extreme environment of low temperature and low irradiance of a limited spectral quality (blue‐green). We investigated the ability of C. raudensis to acclimate to long‐term imbalances in excitation caused by light quality through adjustments in photosystem stoichiometry. Log‐phase cultures of C. raudensis and C. reinhardtii grown under white light were shifted to either blue or red light for 12 h. Previously, we reported that C. raudensis lacks the ability to redistribute light energy via the short‐term mechanism of state transitions. However, similar to the model of mesophilic alga, C. reinhardtii, the psychrophile retained the capacity for long‐term adjustment in energy distribution between PSI and PSII by modulating the levels of PSI reaction center polypeptides, PsaA/PsaB, with minimal changes in the content of the PSII polypeptide, D1, in response to changes in light quality. The functional consequences of the modulation in PSI/PSII stoichiometry in the psychrophile were distinct from those observed in C. reinhardtii. Exposure of C. raudensis to red light caused 1) an inhibition of growth and photosynthetic rates, 2) an increased reduction state of the intersystem plastoquinone pool with concomitant increases in nonphotochemical quenching, 3) an uncoupling of the major light‐harvesting complex from the PSII core, and 4) differential thylakoid protein phosphorylation profiles compared with C. reinhardtii. We conclude that the characteristic low levels of PSI relative to PSII set the limit in the capacity of C. raudensis to photoacclimate to an environment enriched in red light.

IDENTIFICATION OF A PSYCHROPHILIC GREEN ALGA FROM LAKE BONNEY ANTARCTICA: CHLAMYDOMONAS RAUDENSIS ETTL. (UWO 241) CHLOROPHYCEAE1

An unusual psychrophilic green alga was isolated from the deepest portion of the photic zone (&lt;0.1% of incident PAR) at a depth of 17 m in the permanently ice‐covered lake, Lake Bonney, Antarctica. Here we identify and report the first detailed morphological and molecular examination of this Antarctic green alga, which we refer to as strain UWO 241. To determine the taxonomic identity, UWO 241 was examined using LM and TEM and partial sequences of the small subunit (SSU), internal transcribed spacer (ITS) 1 and ITS2 regions (including the 5.8S) of the ribosomal operon. These data were compared with those of previously described taxa. We identified UWO 241 as a strain of Chlamydomonas raudensis Ettl (SAG 49.72). Chlamydomonas raudensis is closely related to C. noctigama Korshikov (UTEX 2289) as well as foraminifer symbionts such as C. hedleyi Lee, Crockett, Hagen et Stone (ATCC 50216). In addition, its morphology, pigment complement, and phototactic response to temperature are reported. Chlamydomonas raudensis (UWO 241) contains relatively high levels of lutein and low chl a/b ratios (1.6±0.15), and the phototactic response was temperature dependent. The Antarctic isolate (UWO 241) included the typical photosynthetic pigments found in all chl a/b containing green algae. It possesses a small eyespot and, interestingly, was positively phototactic only at higher nonpermissive growth temperatures. Comparison of SSU and ITS rDNA sequences confirms the identification of the strain UWO 241 as C. raudensis Ettl and contradicts the previous designation as C. subcaudata Wille.