Genome analysis deciphered Chryseobacterium indicum is a distinct species associated with freshwater pufferfish.

A bacterium, strain PS-8T of the genus Chryseobacterium, was isolated from the skin of freshwater pufferfish (Tetraodon cutcutia). Strain PS-8T is a Gram-negative, aerobic, non-motile, and rod-shaped bacterium. Colonies appear in yellowish-orange colors. The major cellular fatty acids were C15:0 iso, C17:0 iso 3OH, C15:0 iso 3OH, and C11:0 anteiso. The predominant polar lipids were phosphatidylethanolamine and amino lipids. The genome size is 4.83 Mb. The G + C content was 35.6%. The in silico dDDH homology, ANI, and AAI were below the cutoff value, 70% and 95% to 96%, respectively, suggesting that strain PS-8T represents a defined species. The phylogenetic tree based on core and the non-recombinant genes showed the strain PS-8T clustered with Chryseobacterium gambrini DSM 18014T. Genome-wide analysis decodes several virulence factors of the genus Chryseobacterium, including genes for adherence, biofilm and stability, proliferation, resistance to immune response, and host-defense evasion system. The cladogram of the virulence genes showed a phylogenetic relationship among the Chryseobacterium species. Knowledge of the association of Chryseobacterium with freshwater pufferfish adds a new ecological niche to this bacterium.

Chaperone client proteins evolve slower than non-client proteins.

Chaperones are important molecular machinery that assists proteins to attain their native three-dimensional structure crucial for function. Earlier studies using experimental evolution showed that chaperones impose a relaxation of sequence constraints on their "client" proteins, which may lead to the fixation of slightly deleterious mutations on the latter. However, we hypothesized that such a phenomenon might be harmful to the organism in a natural physiological condition. In this study, we investigated the evolutionary rates of chaperone client and non-client proteins in five model organisms from both prokaryotic and eukaryotic lineages. Our study reveals a slower evolutionary rate of chaperone client proteins in all five organisms. Additionally, the slower folding rate and lower aggregation propensity of chaperone client proteins reveal that the chaperone may play an essential role in rescuing the slightly disadvantageous effects due to random mutations and subsequent protein misfolding. However, the fixation of such mutations is less likely to be selected in the natural population.