02454nas a2200277 4500008004100000245020000041210006900241260001200310300001400322490000800336520152000344653001501864653001401879653002501893653001801918653001701936653000801953100002401961700001601985700002102001700001902022700001802041700002302059700002902082856006502111 2022 eng d00aCyclic electron flow (CEF) and ascorbate pathway activity provide constitutive photoprotection for the photopsychrophile, Chlamydomonas sp. UWO 241 (renamed Chlamydomonas priscuii)0 aCyclic electron flow CEF and ascorbate pathway activity provide  c03/2022 a235 - 2500 v1513 a

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 (700 mM 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.

10aAntarctica10aascorbate10aCyclic electron flow10aPhotosystem I10aPsychrophile10aROS1 aStahl-Rommel, Sarah1 aKalra, Isha1 aD'Silva, Susanna1 aHahn, Mark, M.1 aPopson, Devon1 aCvetkovska, Marina1 aMorgan-Kiss, Rachael, M. uhttps://link.springer.com/article/10.1007/s11120-021-00877-502015nas a2200217 4500008004100000245016100041210006900202260001200271490000700283520122000290653001501510653001801525653002301543653003901566653001601605653003001621100002301651700002901674700002401703856007001727 2020 eng d00aGlycerol is an osmoprotectant in two Antarctic Chlamydomonas species from an ice-covered saline lake and is synthesized by an unusual bidomain enzyme0 aGlycerol is an osmoprotectant in two Antarctic IChlamydomonasI s c08/20200 v113 a

Glycerol, a compatible solute, has previously been found to act as an osmoprotectant in some marine Chlamydomonas species and several species of Dunaliella from hypersaline ponds. Recently, Chlamydomonas reinhardtii and Dunaliella salina were shown to make glycerol with an unusual bidomain enzyme, which appears to be unique to algae, that contains a phosphoserine phosphatase and glycerol-3-phosphate dehydrogenase. Here we report that two psychrophilic species of Chlamydomonas (C. spp. UWO241 and ICE-MDV) from Lake Bonney, Antarctica also produce high levels of glycerol to survive in the lake’s saline waters. Glycerol concentration increased linearly with salinity and at 1.3 M NaCl, exceeded 400 mM in C. sp. UWO241, the more salt-tolerant strain. We also show that both species expressed several isoforms of the bidomain enzyme. An analysis of one of the isoforms of C. sp. UWO241 showed that it was strongly upregulated by NaCl and is thus the likely source of glycerol. These results reveal another adaptation of the Lake Bonney Chlamydomonas species that allow them to survive in an extreme polar environment.

10aAntarctica10aChlamydomonas10aglycerol synthesis10aglycerol-3-phosphate dehydrogenase10aLake Bonney10aphosphoserine phosphatase1 aRaymond, James, A.1 aMorgan-Kiss, Rachael, M.1 aStahl-Rommel, Sarah uhttps://www.frontiersin.org/articles/10.3389/fpls.2020.01259/full