National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
R35GM122510
United States
Citation
Journal: Cell Rep Phys Sci / Year: 2020 Title: Artificial Intracellular Filaments. Authors: Zhaoqianqi Feng / Huaimin Wang / Fengbin Wang / Younghoon Oh / Cristina Berciu / Qiang Cui / Edward H Egelman / Bing Xu / Abstract: Intracellular protein filaments are ubiquitous for cellular functions, but forming bona fide biomimetic intracellular filaments of small molecules in living cells remains elusive. Here, we report the ...Intracellular protein filaments are ubiquitous for cellular functions, but forming bona fide biomimetic intracellular filaments of small molecules in living cells remains elusive. Here, we report the formation of self-limiting intracellular filaments of a small peptide via enzymatic morphological transition of a phosphorylated and trimethylated heterochiral tetrapeptide. Enzymatic dephosphorylation reduces repulsive intermolecular electrostatic interactions and converts the peptidic nanoparticles into filaments, which exhibit distinct types of cross-β structures with either C7 or C2 symmetries, with the hydrophilic C-terminal residues at the periphery of the helix. Macromolecular crowding promotes the peptide filaments to form bundles, which extend from the plasma membrane to nuclear membrane and hardly interact with endogenous components, including cytoskeletons. Stereochemistry and post-translational modification (PTM) of peptides are critical for generating the intracellular bundles. This work may offer a way to gain lost functions or to provide molecular insights for understanding normal and aberrant intracellular filaments.
Evidence: microscopy, helical filament was observed by negative staining and Cryo-EM
Type
Name
Symmetry operation
Number
identity operation
1_555
1
Symmetry
Helical symmetry: (Circular symmetry: 7 / Dyad axis: no / N subunits divisor: 1 / Num. of operations: 10 / Rise per n subunits: 4.9 Å / Rotation per n subunits: 2.3 °)
-
Components
#1: Polypeptide(D)
... 1-KMe3peptide-likefibril
Mass: 880.965 Da / Num. of mol.: 70 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human)
Has ligand of interest
Y
-
Experimental details
-
Experiment
Experiment
Method: ELECTRON MICROSCOPY
EM experiment
Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction
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