F-actin-like filaments formed by plasmid segregation protein ParM

Fusinita van den Ent, Jakob Møller-Jensen, Linda A. Amos, Kenn Gerdes, Jan Löwe

Research output: Contribution to journalJournal articleResearchpeer-review

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° 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.
Udgivelsesdato: Dec 16
Original languageEnglish
JournalThe EMBO Journal
Volume21
Issue number24
Pages (from-to)6935-6943
Number of pages8
DOIs
Publication statusPublished - 16. Dec 2002

Cite this

van den Ent, Fusinita ; Møller-Jensen, Jakob ; Amos, Linda A. ; Gerdes, Kenn ; Löwe, Jan. / F-actin-like filaments formed by plasmid segregation protein ParM. In: The EMBO Journal. 2002 ; Vol. 21, No. 24. pp. 6935-6943.
@article{12dadb30de1311dc860c000ea68e967b,
title = "F-actin-like filaments formed by plasmid segregation protein ParM",
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° 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. Udgivelsesdato: Dec 16",
author = "{van den Ent}, Fusinita and Jakob M{\o}ller-Jensen and Amos, {Linda A.} and Kenn Gerdes and Jan L{\"o}we",
note = "F.van den Ent and J.M{\o}ller-Jensen contributed equally to this work",
year = "2002",
month = "12",
day = "16",
doi = "10.1093/emboj/cdf672",
language = "English",
volume = "21",
pages = "6935--6943",
journal = "The EMBO Journal",
number = "24",

}

van den Ent, F, Møller-Jensen, J, Amos, LA, Gerdes, K & Löwe, J 2002, 'F-actin-like filaments formed by plasmid segregation protein ParM', The EMBO Journal, vol. 21, no. 24, pp. 6935-6943. https://doi.org/10.1093/emboj/cdf672

F-actin-like filaments formed by plasmid segregation protein ParM. / van den Ent, Fusinita; Møller-Jensen, Jakob; Amos, Linda A.; Gerdes, Kenn; Löwe, Jan.

In: The EMBO Journal, Vol. 21, No. 24, 16.12.2002, p. 6935-6943.

Research output: Contribution to journalJournal articleResearchpeer-review

TY - JOUR

T1 - F-actin-like filaments formed by plasmid segregation protein ParM

AU - van den Ent, Fusinita

AU - Møller-Jensen, Jakob

AU - Amos, Linda A.

AU - Gerdes, Kenn

AU - Löwe, Jan

N1 - F.van den Ent and J.Møller-Jensen contributed equally to this work

PY - 2002/12/16

Y1 - 2002/12/16

N2 - 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° 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. Udgivelsesdato: Dec 16

AB - 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° 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. Udgivelsesdato: Dec 16

U2 - 10.1093/emboj/cdf672

DO - 10.1093/emboj/cdf672

M3 - Journal article

VL - 21

SP - 6935

EP - 6943

JO - The EMBO Journal

JF - The EMBO Journal

IS - 24

ER -