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Publication Abstract from PubMed

Actins are among the most abundant and conserved proteins in plant, mammalian and other eukaryotic cells, where they form filamentous structures to perform vital roles in key cellular processes. Although large amounts of data on the biochemical activities, dynamic behaviors and important cellular functions of plant actin filaments have been accumulated, their structural basis is still elusive. Here, we report a 3.9 A structure of the plant actin filament (ZMPA) from Zea mays pollen using cryo-electron microscopy. The structure shows a right-handed, parallel and staggered architecture that is stabilized by intra- and interstrand interactions. While the overall structure resembles that of other actin filaments, its DNase I-binding loop (D-loop) bends further outward, adopting an open conformation similar to that of the jasplakinolide- or BeFx-stabil1ized rabbit skeleton muscle actin (RSMA) filament. Single-molecule magnetic tweezers analysis revealed that the ZMPA filament can resist greater stretching force than the RSMA filament. Overall, these data provide evidence that plant actin filaments have greater stability than animal actin filaments, which is important for their roles as tracks for long-distance vesicle and organelle transportation.

Cryo-EM Structure of Actin Filaments from Zea mays Pollen.,Ren Z, Zhang Y, Zhang Y, He Y, Du P, Wang Z, Sun F, Ren H Plant Cell. 2019 Oct 18. pii: tpc.18.00973. doi: 10.1105/tpc.18.00973. PMID:31628168^[1]

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