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Cryo-EM Structure of Actin Filaments from Zea mays Pollen.
Plant Cell 2019; 31(12):2855-2867PC

Abstract

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 Zea mays 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 (BeFx)-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.

Authors+Show Affiliations

Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, Center for Biological Science and Technology, College of Life Sciences, Beijing Normal University, Zhuhai 519087, China feisun@ibp.ac.cn hren@bnu.edu.cn.National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, Center for Biological Science and Technology, College of Life Sciences, Beijing Normal University, Zhuhai 519087, China.Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, Center for Biological Science and Technology, College of Life Sciences, Beijing Normal University, Zhuhai 519087, China.Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, Center for Biological Science and Technology, College of Life Sciences, Beijing Normal University, Zhuhai 519087, China feisun@ibp.ac.cn hren@bnu.edu.cn.Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, Center for Biological Science and Technology, College of Life Sciences, Beijing Normal University, Zhuhai 519087, China.National Laboratory of Biomacromolecules, CAS Center for Excellence in Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China feisun@ibp.ac.cn hren@bnu.edu.cn. University of Chinese Academy of Sciences, Beijing 100049, China. Center for Biological Imaging, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China.Key Laboratory of Cell Proliferation and Regulation Biology of Ministry of Education, Center for Biological Science and Technology, College of Life Sciences, Beijing Normal University, Zhuhai 519087, China feisun@ibp.ac.cn hren@bnu.edu.cn.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31628168

Citation

Ren, Zhanhong, et al. "Cryo-EM Structure of Actin Filaments From Zea Mays Pollen." The Plant Cell, vol. 31, no. 12, 2019, pp. 2855-2867.
Ren Z, Zhang Y, Zhang Y, et al. Cryo-EM Structure of Actin Filaments from Zea mays Pollen. Plant Cell. 2019;31(12):2855-2867.
Ren, Z., Zhang, Y., Zhang, Y., He, Y., Du, P., Wang, Z., ... Ren, H. (2019). Cryo-EM Structure of Actin Filaments from Zea mays Pollen. The Plant Cell, 31(12), pp. 2855-2867. doi:10.1105/tpc.18.00973.
Ren Z, et al. Cryo-EM Structure of Actin Filaments From Zea Mays Pollen. Plant Cell. 2019;31(12):2855-2867. PubMed PMID: 31628168.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Cryo-EM Structure of Actin Filaments from Zea mays Pollen. AU - Ren,Zhanhong, AU - Zhang,Yan, AU - Zhang,Yi, AU - He,Yunqiu, AU - Du,Pingzhou, AU - Wang,Zhanxin, AU - Sun,Fei, AU - Ren,Haiyun, Y1 - 2019/10/18/ PY - 2019/01/02/received PY - 2019/09/17/revised PY - 2019/10/16/accepted PY - 2019/10/20/pubmed PY - 2019/10/20/medline PY - 2019/10/20/entrez SP - 2855 EP - 2867 JF - The Plant cell JO - Plant Cell VL - 31 IS - 12 N2 - 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 Zea mays 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 (BeFx)-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. SN - 1532-298X UR - https://www.unboundmedicine.com/medline/citation/31628168/Cryo-EM_Structure_of_Actin_Filaments_from_Zea_mays_Pollen L2 - http://www.plantcell.org/cgi/pmidlookup?view=long&pmid=31628168 DB - PRIME DP - Unbound Medicine ER -