"Two of them, MAHS and ATPM1, showed mitochondrial localization (Fig. 4a, S3 Fig.)."

"Although purified MAHS protein was recovered in the soluble fraction after heat treatment, the heat-treated MAHS protein showed relatively slower migration in sodium dodecyl sulphate-polyacrylamide gel electrophoresis (Fig. 4b), indicating a possible conformational change induced by heat treatment."

"cells expressing MAHS also had significantly increased metabolic activities at 150 mM and 200 mM sucrose. The best improvement by MAHS (~20%) was observed at 200 mM sucrose, which is close to the EC50 value (179 mM) of untransfected cells (Fig. 5)."

"Sequence comparison among putative tardigrade MAHS proteins revealed a conserved region in the middle of the protein (S4 Fig.), and this region was partially predicted to form an alpha-helix by PORTER predication software (Fig. 4c-d), potentially with an amphipathic property (Fig. 4e), implying that MAHS proteins have a role similar to that of LEA proteins in anhydrobiosis."

"A BLASTP search in non-redundant (nr) database retrieved no sequences, and TBLASTN searches in EST/TSA databases retrieved only two sequences of other tardigrades (e-value < 1); one from the EST database of Hypsibius dujardini and the other from the TSA database of Milnesium tardigradum. No LEA proteins were retrieved in the search and also no LEA-like motif was found by either a InterProScan search or manual inspection."

"To date, three tardigrade-unique heat-soluble protein families have been identified, MAHS, CAHS, and SAHS. Their subcellular localizations are mutually exclusive and together they cover most cellular components: MAHS in the mitochondria, CAHS in the cytoplasm and nucleus, and SAHS in the extracellular space and secretory organelles."

"Extremotolerant tardigrade genome and improved radiotolerance of human cultured cells by tardigrade-unique protein."