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TitleCryo-EM Structure of Actin Filaments from Pollen.
Journal, issue, pagesPlant Cell, Vol. 31, Issue 12, Page 2855-2867, Year 2019
Publish dateOct 18, 2019
AuthorsZhanhong Ren / Yan Zhang / Yi Zhang / Yunqiu He / Pingzhou Du / Zhanxin Wang / Fei Sun / Haiyun Ren /
PubMed AbstractActins are among the most abundant and conserved proteins in eukaryotic cells, where they form filamentous structures that perform vital roles in key cellular processes. Although large amounts of ...Actins are among the most abundant and conserved proteins in eukaryotic cells, where they form filamentous structures that 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 accumulated, their structural basis remains elusive. Here, we report a 3.9 Å structure of the plant actin filament from pollen (ZMPA) using cryo-electron microscopy. The structure shows a right-handed, double-stranded (two parallel strands) 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 bends farther outward, adopting an open conformation similar to that of the jasplakinolide- or beryllium fluoride (BeF)-stabilized rabbit skeletal muscle actin (RSMA) filament. Single-molecule magnetic tweezers analysis revealed that the ZMPA filament can resist a greater stretching force than the RSMA filament. Overall, these data provide evidence that plant actin filaments have greater stability than animal actin filaments, which might be important to their role as tracks for long-distance vesicle and organelle transportation.plantcell;31/12/2855/FX1F1fx1.
External linksPlant Cell / PubMed:31628168 / PubMed Central
MethodsEM (helical sym.)
Resolution3.9 Å
Structure data

EMDB-9734, PDB-6iug:
Cryo-EM structure of the plant actin filaments from Zea mays pollen
Method: EM (helical sym.) / Resolution: 3.9 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-MG:
Unknown entry

Source
  • zea mays (maize)
KeywordsPROTEIN FIBRIL / Microfilament / Helix / Actin

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