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Publication Abstract from PubMed

Plant cells form microtubule arrays, called ;cortical microtubules', beneath the plasma membrane which are critical for cell-wall organization and directional cell growth. Cortical microtubules are nucleated independently of centrosomes. Spiral2 is a land-plant-specific microtubule minus-end-targeting protein that stabilizes the minus ends by inhibiting depolymerization of the filament. Spiral2 possesses an N-terminal microtubule-binding domain and a conserved C-terminal domain whose function is unknown. In this study, the crystal structure of the conserved C-terminal domain of Spiral2 was determined using the single-wavelength anomalous dispersion method. Refinement of the model to a resolution of 2.2 A revealed a helix-turn-helix fold with seven alpha-helices. The protein crystallized as a dimer, but SEC-MALS analysis showed the protein to be monomeric. A structural homology search revealed that the protein has similarity to the C-terminal domain of the katanin regulatory subunit p80. The structure presented here suggests that the C-terminal domain of Spiral2 represents a new class of microtubule dynamics modulator across the kingdom.

Crystal structure of the C-terminal domain of the plant-specific microtubule-associated protein Spiral2.,Ohno M, Higuchi Y, Hayashi I Acta Crystallogr F Struct Biol Commun. 2023 Jan 1;79(Pt 1):17-22. doi: , 10.1107/S2053230X22011815. Epub 2023 Jan 1. PMID:36598352^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.