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TitleMechanistic basis of temperature adaptation in microtubule dynamics across frog species.
Journal, issue, pagesCurr Biol, Vol. 35, Issue 3, Page 612-628.e6, Year 2025
Publish dateFeb 3, 2025
AuthorsLuca Troman / Ella de Gaulejac / Abin Biswas / Jennifer Stiens / Benno Kuropka / Carolyn A Moores / Simone Reber /
PubMed AbstractCellular processes are remarkably effective across diverse temperature ranges, even with highly conserved proteins. In the context of the microtubule cytoskeleton, which is critically involved in a ...Cellular processes are remarkably effective across diverse temperature ranges, even with highly conserved proteins. In the context of the microtubule cytoskeleton, which is critically involved in a wide range of cellular activities, this is particularly striking, as tubulin is one of the most conserved proteins while microtubule dynamic instability is highly temperature sensitive. Here, we leverage the diversity of natural tubulin variants from three closely related frog species that live at different temperatures. We determine the microtubule structure across all three species at between 3.0 and 3.6 Å resolution by cryo-electron microscopy and find small differences at the β-tubulin lateral interactions. Using in vitro reconstitution assays and quantitative biochemistry, we show that tubulin's free energy scales inversely with temperature. The observed weakening of lateral contacts and the low apparent activation energy for tubulin incorporation provide an explanation for the overall stability and higher growth rates of microtubules in cold-adapted frog species. This study thus broadens our conceptual framework for understanding microtubule dynamics and provides insights into how conserved cellular processes are tailored to different ecological niches.
External linksCurr Biol / PubMed:39798564
MethodsEM (single particle)
Resolution3.0 - 3.6 Å
Structure data

EMDB-50811, PDB-9fvj:
Xenopus borealis undecorated microtubule - 15 protofilament, 3-start helix
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-50941, PDB-9g0o:
Xenopus borealis undecorated microtubule - 14 protofilament, 3-start helix
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-50942, PDB-9g0p:
Xenopus laevis undecorated microtubule - 14 protofilament, 3-start helix
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-50943, PDB-9g0q:
Xenopus laevis undecorated microtubule - 15 protofilament, 3-start helix
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-50945, PDB-9g0r:
Xenopus laevis undecorated microtubule - 15 protofilament, 4-start helix
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-50946, PDB-9g0s:
Xenopus tropicalis undecorated microtubule - 14 protofilament, 3-start helix
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-50947, PDB-9g0t:
Xenopus tropicalis undecorated microtubule - 15 protofilament, 3-start helix
Method: EM (single particle) / Resolution: 3.5 Å

Chemicals

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

Source
  • xenopus borealis (Kenyan clawed frog)
  • xenopus laevis (African clawed frog)
  • xenopus tropicalis (tropical clawed frog)
KeywordsPROTEIN FIBRIL / Microtubule Tubulin Cytoskeleton Filament

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