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The relationship between the denaturation temperatures of proteins (T m  values) and the living temperatures of their host organisms (environmental temperatures: T ENV  values) is poorly understood. Since different proteins in the same organism may show widely different T m ’s, no simple universal relationship between T m  and T ENV  should hold, other than T m ≥T ENV . Yet, when analyzing a set of homologous proteins from different hosts, T m ’s are oftentimes found to correlate with T ENV ’s but this correlation is shifted upward on the T m  axis. Supporting this trend, we recently reported T m ’s for resurrected Precambrian thioredoxins that mirror a proposed environmental cooling over long geological time, while remaining a shocking ~50°C above the proposed ancestral ocean temperatures. Here, we show that natural selection for protein kinetic stability (denaturation rate) can produce a T m ↔T ENV  correlation with a large upward shift in T m . A model for protein stability evolution suggests a link between the T m  shift and the  in vivo  lifetime of a protein and, more specifically, allows us to estimate ancestral environmental temperatures from experimental denaturation rates for resurrected Precambrian thioredoxins. The T ENV  values thus obtained match the proposed ancestral ocean cooling, support comparatively high Archaean temperatures, and are consistent with a recent proposal for the environmental temperature (above 75°C) that hosted the last universal common ancestor. More generally, this work provides a framework for understanding how features of protein stability reflect the environmental temperatures of the host organisms.

Selection for Protein Kinetic Stability Connects Denaturation Temperatures to Organismal Temperatures and Provides Clues to Archaean Life