F-actin-like Filaments Formed by Plasmid Segregation Protein ParM

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 2002 Dec 18

PMID 12486014

Citations 105

Authors

Fusinita van den Ent

Jakob Moller-Jensen

Linda A Amos

Kenn Gerdes

Jan Lowe

Affiliations

Soon will be listed here.

Abstract

It was the general belief that DNA partitioning in prokaryotes is independent of a cytoskeletal structure, which in eukaryotic cells is indispensable for DNA segregation. Recently, however, immunofluorescence microscopy revealed highly dynamic, filamentous structures along the longitudinal axis of Escherichia coli formed by ParM, a plasmid-encoded protein required for accurate segregation of low-copy-number plasmid R1. We show here that ParM polymerizes into double helical protofilaments with a longitudinal repeat similar to filamentous actin (F-actin) and MreB filaments that maintain the cell shape of non-spherical bacteria. The crystal structure of ParM with and without ADP demonstrates that it is a member of the actin family of proteins and shows a domain movement of 25 degrees upon nucleotide binding. Furthermore, the crystal structure of ParM reveals major differences in the protofilament interface compared with F-actin, despite the similar arrangement of the subunits within the filaments. Thus, there is now evidence for cytoskeletal structures, formed by actin-like filaments that are involved in plasmid partitioning in E.coli.

Citing Articles

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Catching a Walker in the Act-DNA Partitioning by ParA Family of Proteins.

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Detection of Osmotic Shock-Induced Extracellular Nucleotide Release with a Genetically Encoded Fluorescent Sensor of ADP and ATP.

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Plasmid Localization and Partition in .

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Conservation of conformational dynamics across prokaryotic actins.

Ng N, Shi H, Colavin A, Huang K PLoS Comput Biol. 2019; 15(4):e1006683.

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