Structural highlights
FunctionACT_YEAST Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. Publication Abstract from PubMedThe core component of the actin cytoskeleton is the globular protein G-actin, which reversibly polymerizes into filaments (F-actin). Budding yeast possesses a single actin that shares 87%-89% sequence identity with vertebrate actin isoforms. Previous structural studies indicate very close overlap of main-chain backbones. Intriguingly, however, substitution of yeast ACT1 with vertebrate beta-cytoplasmic actin severely disrupts cell function and the substitution with a skeletal muscle isoform is lethal. Here we report a 2.5 A structure of budding yeast F-actin. Previously unresolved side-chain information allows us to highlight four main differences in the comparison of yeast and vertebrate ADP F-actins: a more open nucleotide binding pocket; a more solvent exposed C-terminus; a rearrangement of inter-subunit binding interactions in the vicinity of the D loop and changes in the hydrogen bonding network in the vicinity of histidine 73 (yeast actin) and methyl-histidine 73 (vertebrate actin). Cryo-EM reconstruction of yeast ADP-actin filament at 2.5 A resolution. A comparison with vertebrate F-actin.,Stevenson SR, Tzokov SB, Lahiri I, Ayscough KR, Bullough PA Structure. 2025 Jan 2:S0969-2126(24)00543-4. doi: 10.1016/j.str.2024.12.008. PMID:39798573[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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