Artificial Intracellular Filaments

Zhaoqianqi Feng; Huaimin Wang; Fengbin Wang; Younghoon Oh; Cristina Berciu; Qiang Cui; Edward H. Egelman; Bing Xu

Cell Reports Physical Science (Jul 2020)

Artificial Intracellular Filaments

Zhaoqianqi Feng,
Huaimin Wang,
Fengbin Wang,
Younghoon Oh,
Cristina Berciu,
Qiang Cui,
Edward H. Egelman,
Bing Xu

Affiliations

Zhaoqianqi Feng: Department of Chemistry, Brandeis University, 415 South Street, Waltham, MA 02454, USA
Huaimin Wang: Department of Chemistry, Brandeis University, 415 South Street, Waltham, MA 02454, USA
Fengbin Wang: Department of Biochemistry and Molecular Genetics, University of Virginia, Box 800733, Charlottesville, VA 22908-0733, USA
Younghoon Oh: Department of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, MA 02215, USA; Rafik B. Hariri Institute for Computing and Computational Science & Engineering, Boston University, 111 Cummington Mall, Boston, MA 02215, USA; Department of Chemistry and Research Institute for Basic Science, Sogang University, Seoul 04107, Republic of Korea
Cristina Berciu: Microscopy Core Facility, McLean Hospital, Belmont, MA 02478, USA
Qiang Cui: Department of Chemistry, Boston University, 590 Commonwealth Avenue, Boston, MA 02215, USA; Corresponding author
Edward H. Egelman: Department of Biochemistry and Molecular Genetics, University of Virginia, Box 800733, Charlottesville, VA 22908-0733, USA; Corresponding author
Bing Xu: Department of Chemistry, Brandeis University, 415 South Street, Waltham, MA 02454, USA; Corresponding author

Journal volume & issue: Vol. 1, no. 7
p. 100085

Abstract

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Summary: 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 in situ 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.

Published in Cell Reports Physical Science

ISSN: 2666-3864 (Online)
Publisher: Elsevier
Country of publisher: United States
LCC subjects: Science: Physics
Website: https://www.cell.com/cell-reports-physical-science

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