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TitleStructural basis for α-tubulin-specific and modification state-dependent glutamylation.
Journal, issue, pagesNat Chem Biol, Vol. 20, Issue 11, Page 1493-1504, Year 2024
Publish dateApr 24, 2024
AuthorsKishore K Mahalingan / Danielle A Grotjahn / Yan Li / Gabriel C Lander / Elena A Zehr / Antonina Roll-Mecak /
PubMed AbstractMicrotubules have spatiotemporally complex posttranslational modification patterns. Tubulin tyrosine ligase-like (TTLL) enzymes introduce the most prevalent modifications on α-tubulin and β-tubulin. ...Microtubules have spatiotemporally complex posttranslational modification patterns. Tubulin tyrosine ligase-like (TTLL) enzymes introduce the most prevalent modifications on α-tubulin and β-tubulin. How TTLLs specialize for specific substrate recognition and ultimately modification-pattern generation is largely unknown. TTLL6, a glutamylase implicated in ciliopathies, preferentially modifies tubulin α-tails in microtubules. Cryo-electron microscopy, kinetic analysis and single-molecule biochemistry reveal an unprecedented quadrivalent recognition that ensures simultaneous readout of microtubule geometry and posttranslational modification status. By binding to a β-tubulin subunit, TTLL6 modifies the α-tail of the longitudinally adjacent tubulin dimer. Spanning two tubulin dimers along and across protofilaments (PFs) ensures fidelity of recognition of both the α-tail and the microtubule. Moreover, TTLL6 reads out and is stimulated by glutamylation of the β-tail of the laterally adjacent tubulin dimer, mediating crosstalk between α-tail and β-tail. This positive feedback loop can generate localized microtubule glutamylation patterns. Our work uncovers general principles that generate tubulin chemical and topographic complexity.
External linksNat Chem Biol / PubMed:38658656 / PubMed Central
MethodsEM (single particle)
Resolution3.6 - 7.2 Å
Structure data

41018

8t42

EMDB-41018: Microtubule-TTLL6 map
PDB-8t42: Model of TTLL6 MTBH1-2 bound to microtubule
Method: EM (single particle) / Resolution: 3.6 Å

EMDB-41022: Map of Tubulin Tyrosine Ligase Like 6
Method: EM (single particle) / Resolution: 7.2 Å

41090

8u3z

EMDB-41090: Composite map of TTLL6 bound to unmodified human microtubule
PDB-8u3z: Model of TTLL6 bound to microtubule from composite map
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-42884: Microtubule-TTLL6 map
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

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

ChemComp-MG:
Unknown entry

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

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsLIGASE / tubulin post-translational modifications / microtubules / TTLL / tubulin / post-translational modifications / Tubulin Tyrosine Ligase Like family enzymes

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