Abstract

Case studies of the evolution of molecular machines remain scarce. One of the most diverse and widespread homologous families of machines is the type IV filament (TFF) superfamily, comprised of type IV pili, type II secretion systems (T2SSs), archaella, and other less-well-characterized families. These families have functions including twitching motility, effector export, rotary propulsion, nutrient uptake, DNA uptake, and even electrical conductance, but it is unclear how such diversity evolved from a common ancestor. In this issue, Denise and colleagues take a significant step toward understanding evolution of the TFF superfamily by determining a global phylogeny and using it to infer an evolutionary pathway. Results reveal that the superfamily predates the divergence of Bacteria and Archaea, and show how duplications, acquisitions, and losses coincide with changes in function. Surprises include that tight adherence (Tad) pili were horizontally acquired from Archaea and that T2SSs were relatively recently repurposed from type IV pili. Results also enable better understanding of the function of the ATPase family that powers the superfamily. The study highlights the role of tinkering by exaptation—the repurposing of pre-existing functions for new roles—in the diversification of molecular machines.

Highlights

  • Their study builds on earlier work that analyzed type IV pili and type II secretion system (T2SS) [30], reviewed and surveyed homologies across species [9], and determined a phylogeny of archaeal type IV filament (TFF) superfamily members [31]

  • One conclusion is immediately clear: the superfamily splits into two broad clades representing Bacteria and Archaea, indicating that TFF are ancient and were present in the last universal common ancestor (LUCA). This suggests that the progenitor TFF superfamily member function was to take up DNA, consistent with horizontal gene transfer being commonplace at the dawn of cellular life [34]

  • The so-called T2SS from Chlamydia is chimaeric. These results distinguish these two “T2SSs” from true T2SSs. These unexpected results suggest that secretion systems evolved within the TFF superfamily multiple times, and are relatively modern innovations

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Summary

Introduction

Type II secretion systems (T2SSs) were discovered to be TFF superfamily members. The third conserved TFF component is a membrane platform protein made of three transmembrane domains that incorporates or removes pilins at the base of the pilus.

Results
Conclusion
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