Genomic, Proteomic, and Structural Insights Into the Transition of FtsZ From Thermophiles to Mesophiles Across the Prokaryotic Kingdom

Understanding how cellular macromolecules adapt in thermophilic and mesophilic organisms across different thermal environments provides important insights into evolutionary mechanisms. These mechanisms enable early life forms to maintain essential biological processes in diverse ecological niches. FtsZ, an important protein for bacterial and archaeal cell division, has evolved to function across different thermal environments. The present study investigates the genomic, proteomic, and structural adaptations of the pivotal bacterial cell division protein FtsZ during the transition from thermophilic to mesophilic bacteria across the prokaryotic kingdom. Through comprehensive analyses, we reveal intricate evolutionary dynamics, shedding light on the molecular strategies that underlie bacterial adaptation to diverse thermal environments. Our genomic exploration unveils key genetic variations correlating with temperature preferences, while proteomic investigations elucidate distinct expression patterns of FtsZ in response to thermal shifts. Structural insights show temperature-dependent alterations in the conformation of these proteins, providing a nuanced understanding of their functional adaptations. These findings collectively contribute to our comprehension of the molecular mechanisms governing bacterial evolution and highlight the importance of FtsZ in temperature-driven adaptations across prokaryotes. We found that three amino acids, namely lysine (K), leucine (L), and isoleucine (I), are particularly enriched in thermophilic FtsZ protein sequences compared with those of mesophiles. In addition, the mutational changes occurred in the thermophilic FtsZ protein structure to understand the thermal stability of the protein. Simultaneously, the B-factor and Tm value, these two essential parameters, established that the mutant FtsZ structures were thermodynamically unstable for losing those distinct amino acids.