Escherichia coli (E. coli) is a nonhalophilic microbe and used to indicate faecal contamination. Salt (sodium chloride, NaCl) is a common food additive and is used in preservatives to encounter microbial growth. e effect of how E. coli interacts with the salt present in the human diet is unclear. us, it is important to investigate this relationship. In order to adapt and survive the changes in the environment, E. coli may undergo halophilization. In this study, we observed the genetic changes and growth kinetics of E. coli ATCC 8739 under 3%-11% NaCl over 80 passages. Our results suggest that E. coli adapted to 1% increase in NaCl every month with a successful adaptation to 11% NaCl. Gram staining and PCR/RFLP showed that the cultures are Gram negative and the DNA pro�les of all 4 replicates to be similar, suggesting that the cultures had not been contaminated.

Aquatic autotrophs that fix carbon using ribulose 1,5-bisphosphate carboxylase/oxygenase (Rubisco) frequently expend metabolic energy to pump inorganic carbon towards the enzyme’s active site. A central requirement of this strategy is the formation of highly concentrated Rubisco condensates known as carboxysomes and pyrenoids, which have convergently evolved multiple times in prokaryotes and eukaryotes respectively. Recent data indicates these condensates form by the mechanism of liquid- liquid phase separation (LLPS). LLPS requires networks of weak multivalent interactions typically mediated by intrinsically disordered scaffold proteins. Here we comparatively review recent rapid developments that detail the determinants and precise interactions that underlie diverse Rubisco condensates. The burgeoning field of biomolecular condensates has few examples where LLPS can be linked to clear phenotypic outcomes. When present, Rubisco condensates are essential for photosynthesis and growth, and they are thus emerging as powerful and tractable models to investigate the structure function relationship of phase separation in biology.

v 4.1.3 AfCsoS2N interacts with Rubisco and AfCsoS2M has potential interactions with CsoS1A .