02015nas 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/full02036nas a2200145 4500008004100000245014100041210006900182260001200251490000700263520148900270100002301759700002901782700001701811856006201828 2017 eng d00aMultiple ice-binding proteins of probable prokaryotic origin in an Antarctic lake alga, Chlamydomonas sp. ICE-MDV (Chlorophyceae)0 aMultiple icebinding proteins of probable prokaryotic origin in a c08/20170 v533 a

Ice‐associated algae produce ice‐binding proteins (IBPs) to prevent freezing damage. The IBPs of the three chlorophytes that have been examined so far share little similarity across species, making it likely that they were acquired by horizontal gene transfer (HGT). To clarify the importance and source of IBPs in chlorophytes, we sequenced the IBP genes of another Antarctic chlorophyte, Chlamydomonas sp. ICE‐MDV (Chlamy‐ICE). Genomic DNA and total RNA were sequenced and screened for known ice‐associated genes. Chlamy‐ICE has as many as 50 IBP isoforms, indicating that they have an important role in survival. The IBPs are of the DUF3494 type and have similar exon structures. The DUF3494 sequences are much more closely related to prokaryotic sequences than they are to sequences in other chlorophytes, and the chlorophyte IBP and ribosomal 18S phylogenies are dissimilar. The multiple IBP isoforms found in Chlamy‐ICE and other algae may allow the algae to adapt to a greater variety of ice conditions than prokaryotes, which typically have a single IBP gene. The predicted structure of the DUF3494 domain has an ice‐binding face with an orderly array of hydrophilic side chains. The results indicate that Chlamy‐ICE acquired its IBP genes by HGT in a single event. The acquisitions of IBP genes by this and other species of Antarctic algae by HGT appear to be key evolutionary events that allowed algae to extend their ranges into polar environments.

1 aRaymond, James, A.1 aMorgan-Kiss, Rachael, M.1 aValentin, K. uhttps://onlinelibrary.wiley.com/doi/abs/10.1111/jpy.12550