Conserved GTPase mechanism in bacterial FtsZ and archaeal tubulin filaments

Self‐assembling protein filaments are at the heart of cell function. Among them, tubulin‐like proteins are essential for cell division, DNA segregation and cytoskeletal functions across the domains of life. FtsZ and tubulin share their core structures, a characteristic nucleotide‐binding pocket and...

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Bibliographic Details
Published in:The FEBS journal 2023-07, Vol.290 (14), p.3527-3532
Main Authors: Andreu, José M., Ruiz, Federico M., Fernández‐Tornero, Carlos
Format: Article
Language:English
Subjects:
Cations
Cell division
Cytoskeleton
Deoxyribonucleic acid
DNA
Dynamic structural analysis
evolution
Filaments
FtsZ
GTPase
Magnesium
mechanism
Nucleotides
Proteins
Self-assembly
Tubulin
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Summary:Self‐assembling protein filaments are at the heart of cell function. Among them, tubulin‐like proteins are essential for cell division, DNA segregation and cytoskeletal functions across the domains of life. FtsZ and tubulin share their core structures, a characteristic nucleotide‐binding pocket and similar protofilament architecture. GTP hydrolysis between consecutive subunits drives their assembly dynamics. Two recent studies provide previously missing, filament atomic structures of bacterial FtsZ and a recently discovered archaeal tubulin in their nucleotide triphosphate‐bound states. Both filament structures reveal strikingly conserved interfacial GTPase active sites, with Mg2+ and K+/Na+ cations and an NxDxxD/E triad of catalytic residues, probably inherited from the common ancestor of FtsZs and tubulins. Moreover, both proteins exhibit nucleotide‐regulated subunit association mediated by interfacial water bridges, as well as polymerization‐induced structural changes, likely enabling related dynamic assembly mechanisms. Tubulin‐like proteins form cytomotive filaments essential for cellular life. This Structural Snapshot compares two recently reported atomic structures of bacterial FtsZ filaments and archaeal tubulin filaments, revealing striking similarities between their GTPase active sites at the subunit association interface, likely inherited from the FtsZ/tubulin ancestor, as well as related dynamic assembly mechanisms. The graph is a cartoon of the FtsZ active site.
ISSN:1742-464X
1742-4658
DOI:10.1111/febs.16675