Chaperone mRNA secondary structure does not strongly track thermal adaptation in bacteria, but groL coding sequence shortens in its disordered C-terminal tail

GroL coding sequences in 50 phylum-matched bacterial strains are shorter in thermophiles than mesophiles (1626.5 vs 1636.3 nt), with length decreasing as growth temperature rises.

• Why it matters: Ribosomal and transfer RNAs show temperature-linked structure, but whether bacterial chaperone mRNAs share this adaptation signal at individual loci is largely unknown.
• What they did: The authors folded dnaK and groL coding sequences at 37°C and 55°C, computed fifteen structural descriptors, and compared thermophile versus mesophile groups while controlling dinucleotide composition using Altschul-Erickson shuffles.
• The result: After composition control, thermophile groL retained modestly more residual secondary structure, but the strongest pattern was a temperature-linked shortening concentrated in the terminal ~25 residues of GroEL’s disordered C-terminal tail.

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