The potential use of Spirulina subsalsa in marine cultivation is important for biomass and phycocyanin production; however, little is known about its mechanism of salt adaptation. Here we present a draft genome sequence for the halotolerant cyanobacterium Spirulina subsalsa FACHB-351 (5.3 Mbp). The sequence is predominantly distributed in signal transduction, cell growth and adaptation, and carbohydrate metabolism, which possibly allows the strong salt adaptation of FACHB-351. No genes directly related to bacterial toxins suggests a low risk of FACHB-351 threatening human or animal health. A set of genes annotated in the GO database were not assigned in the KEGG database, and some genes of essential enzymes, like HO and DVR for phycocyanin and chlorophyll, were not found, which suggests a presence of possible yet-to-be-discovered pathways in FACHB-351. The availability of a genome sequence will facilitate investigations into S. subsalsa phycocyanin biosynthesis and permit optimal strategies to improve commercial phycocyanin production.

The 90 kDa Heat Shock Protein (Hsp90) is an essential and highly conserved molecular chaperone that supports the folding and maturation of a diverse array of client proteins across prokaryotic and eukaryotic organisms. In bacteria, HtpG, the Hsp90 homolog, plays a central role in stress response and protein homeostasis, particularly under high-temperature and other stress conditions. Despite extensive studies on HtpG from E. coli , the biochemical properties and functional roles of cyanobacterial HtpG remain poorly characterized. Here, we focus on HtpG from the cyanobacterium Synechococcus elongatus PCC 7942 (seHtpG), a model organism for photosynthesis and circadian rhythm research. We developed a method for the overexpression and purification of seHtpG in E. coli , achieving high purity and yield suitable for biochemical and structural studies. Biophysical and biochemical assays show that seHtpG forms dimers and hydrolyzes ATP and a rate of 1.8 ATP/min, faster than that of E. coli HtpG. This work establishes seHtpG as a model for studying the roles of HtpG in cyanobacterial protein homeostasis, photosynthesis, and stress response, enabling further exploration of cyanobacterial Hsp90 in ecosystem dynamics and biotechnological applications. Highlights: HtpG from S. elongatus PCC 7942 (seHtpG) was recombinantly overexpressed. seHtpG was purified to high homogeneity using chromatography techniques. Like other members of the Hsp90 family, seHtpG forms a dimeric structure. seHtpG exhibits ATPase activity of 1.8 ATP/min at 37°C.

The 90 kDa Heat Shock Protein (Hsp90) is an essential and highly conserved molecular chaperone that supports the folding and maturation of a diverse array of client proteins across prokaryotic and eukaryotic organisms. In bacteria, HtpG, the Hsp90 homolog, plays a central role in stress response and protein homeostasis, particularly under high-temperature and other stress conditions. Despite extensive studies on HtpG from E. coli, the biochemical properties and functional roles of cyanobacterial HtpG remain poorly characterized. Here, we focus on HtpG from the cyanobacterium Synechococcus elongatus PCC 7942 (seHtpG), a model organism for photosynthesis and circadian rhythm research. We developed a method for the overexpression and purification of seHtpG in E. coli, achieving high purity and yield suitable for biochemical and structural studies. Biophysical and biochemical assays show that seHtpG forms dimers and hydrolyzes ATP at a rate of 1.9 ATP/min, 4-fold faster than that of E. coli HtpG. This work establishes seHtpG as a model for studying the roles of HtpG in cyanobacterial protein homeostasis, photosynthesis, and stress response, enabling further exploration of cyanobacterial Hsp90 in ecosystem dynamics and biotechnological applications.