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Structure paper

TitleTubulin acetyltransferases access and modify the microtubule luminal K40 residue through anchors in taxane-binding pockets.
Journal, issue, pagesNat Struct Mol Biol, Vol. 32, Issue 2, Page 358-368, Year 2025
Publish dateNov 4, 2024
AuthorsJingyi Luo / Wai Hei Lam / Daqi Yu / Victor C Chao / Marc Nicholas Zopfi / Chen Jing Khoo / Chang Zhao / Shan Yan / Zheng Liu / Xiang David Li / Chaogu Zheng / Yuanliang Zhai / Shih-Chieh Ti /
PubMed AbstractAcetylation at α-tubulin K40 is the sole post-translational modification preferred to occur inside the lumen of hollow cylindrical microtubules. However, how tubulin acetyltransferases access the ...Acetylation at α-tubulin K40 is the sole post-translational modification preferred to occur inside the lumen of hollow cylindrical microtubules. However, how tubulin acetyltransferases access the luminal K40 in micrometer-long microtubules remains unknown. Here, we use cryo-electron microscopy and single-molecule reconstitution assays to reveal the enzymatic mechanism for tubulin acetyltransferases to modify K40 in the lumen. One tubulin acetyltransferase spans across the luminal lattice, with the catalytic core docking onto two α-tubulins and the enzyme's C-terminal domain occupying the taxane-binding pockets of two β-tubulins. The luminal accessibility and enzyme processivity of tubulin acetyltransferases are inhibited by paclitaxel, a microtubule-stabilizing chemotherapeutic agent. Characterizations using recombinant tubulins mimicking preacetylated and postacetylated K40 show the crosstalk between microtubule acetylation states and the cofactor acetyl-CoA in enzyme turnover. Our findings provide crucial insights into the conserved multivalent interactions involving α- and β-tubulins to acetylate the confined microtubule lumen.
External linksNat Struct Mol Biol / PubMed:39496813
MethodsEM (single particle)
Resolution3.1 - 3.6 Å
Structure data

39076

8y9f

EMDB-39076, PDB-8y9f:
ATAT-2 bound MEC-12/MEC-7 microtubule
Method: EM (single particle) / Resolution: 3.3 Å

39100

8yaj

EMDB-39100, PDB-8yaj:
ATAT-2 bound MEC-12/MEC-7 microtubule without acetyl-CoA
Method: EM (single particle) / Resolution: 3.2 Å

39102

8yal

EMDB-39102, PDB-8yal:
ATAT-2 bound K40Q MEC-12/MEC-7 microtubule
Method: EM (single particle) / Resolution: 3.1 Å

39105

8yar

EMDB-39105, PDB-8yar:
ATAT-2 bound K40R MEC-12/MEC-7 microtubule
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

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

ChemComp-G2P:
PHOSPHOMETHYLPHOSPHONIC ACID GUANYLATE ESTER / GMP-CPP, energy-carrying molecule analogue*YM

ChemComp-PIN:
PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID) / pH buffer*YM

ChemComp-ACO:
ACETYL COENZYME *A

Source
  • caenorhabditis elegans (invertebrata)
KeywordsSTRUCTURAL PROTEIN / Microtubules / luminal enzymes / PTMs / Microtubule / luminal enzyme / PTM

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