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TitleDiverse cytomotive actins and tubulins share a polymerization switch mechanism conferring robust dynamics.
Journal, issue, pagesSci Adv, Vol. 9, Issue 13, Page eadf3021, Year 2023
Publish dateMar 29, 2023
AuthorsJames Mark Wagstaff / Vicente José Planelles-Herrero / Grigory Sharov / Aisha Alnami / Frank Kozielski / Emmanuel Derivery / Jan Löwe /
PubMed AbstractProtein filaments are used in myriads of ways to organize other molecules within cells. Some filament-forming proteins couple the hydrolysis of nucleotides to their polymerization cycle, thus ...Protein filaments are used in myriads of ways to organize other molecules within cells. Some filament-forming proteins couple the hydrolysis of nucleotides to their polymerization cycle, thus powering the movement of other molecules. These filaments are termed cytomotive. Only members of the actin and tubulin protein superfamilies are known to form cytomotive filaments. We examined the basis of cytomotivity via structural studies of the polymerization cycles of actin and tubulin homologs from across the tree of life. We analyzed published data and performed structural experiments designed to disentangle functional components of these complex filament systems. Our analysis demonstrates the existence of shared subunit polymerization switches among both cytomotive actins and tubulins, i.e., the conformation of subunits switches upon assembly into filaments. These cytomotive switches can explain filament robustness, by enabling the coupling of kinetic and structural polarities required for cytomotive behaviors and by ensuring that single cytomotive filaments do not fall apart.
External linksSci Adv / PubMed:36989372 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 3.8 Å
Structure data

EMDB-14147, PDB-7quc:
D. melanogaster alpha/beta tubulin heterodimer in the GDP form
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-14148, PDB-7qud:
D. melanogaster alpha/beta tubulin heterodimer in the GTP form
Method: EM (single particle) / Resolution: 3.47 Å

EMDB-14150, PDB-7qup:
D. melanogaster 13-protofilament microtubule
Method: EM (single particle) / Resolution: 3.8 Å

EMDB-14151, PDB-7quq:
BtubA(R284G,K286D,F287G):BtubB bacterial tubulin M-loop mutant forming a single protofilament (Prosthecobacter dejongeii)
Method: EM (single particle) / Resolution: 2.6 Å

Chemicals

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

ChemComp-MG:
Unknown entry

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

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

Source
  • drosophila melanogaster (fruit fly)
  • prosthecobacter dejongeii (bacteria)
KeywordsCELL CYCLE / Cytyoskeleton / microtubules / cytomotive filaments / tubulin-like

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