Assembly mechanisms of the bacterial cytoskeletal protein FilP
(2019) In Life Science Alliance 2(3).- Abstract
Despite low-sequence homology, the intermediate filament (IF)-like protein FilP from Streptomyces coelicolor displays structural and biochemical similarities to the metazoan nuclear IF lamin. FilP, like IF proteins, is composed of central coiled-coil domains interrupted by short linkers and flanked by head and tail domains. FilP polymerizes into repetitive filament bundles with paracrystalline properties. However, the cations Na+ and K+ are found to induce the formation of a FilP hexagonal meshwork with the same 60-nm repetitive unit as the filaments. Studies of polymerization kinetics, in combination with EM techniques, enabled visualization of the basic building block-a transiently soluble rod-shaped FilP molecule-and its assembly... (More)
Despite low-sequence homology, the intermediate filament (IF)-like protein FilP from Streptomyces coelicolor displays structural and biochemical similarities to the metazoan nuclear IF lamin. FilP, like IF proteins, is composed of central coiled-coil domains interrupted by short linkers and flanked by head and tail domains. FilP polymerizes into repetitive filament bundles with paracrystalline properties. However, the cations Na+ and K+ are found to induce the formation of a FilP hexagonal meshwork with the same 60-nm repetitive unit as the filaments. Studies of polymerization kinetics, in combination with EM techniques, enabled visualization of the basic building block-a transiently soluble rod-shaped FilP molecule-and its assembly into protofilaments and filament bundles. Cryoelectron tomography provided a 3D view of the FilP bundle structure and an original assembly model of an IF-like protein of prokaryotic origin, thereby enabling a comparison with the assembly of metazoan IF.
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- author
- Javadi, Ala ; Söderholm, Niklas ; Olofsson, Annelie ; Flärdh, Klas LU and Sandblad, Linda
- organization
- publishing date
- 2019
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Life Science Alliance
- volume
- 2
- issue
- 3
- publisher
- Rockefeller University Press
- external identifiers
-
- pmid:31243049
- scopus:85078179405
- ISSN
- 2575-1077
- DOI
- 10.26508/lsa.201800290
- language
- English
- LU publication?
- yes
- id
- 3539400b-5a41-41f2-8041-a94a38b48904
- date added to LUP
- 2020-02-03 15:17:59
- date last changed
- 2022-04-10 23:51:51
@article{3539400b-5a41-41f2-8041-a94a38b48904,
abstract = {{<p>Despite low-sequence homology, the intermediate filament (IF)-like protein FilP from Streptomyces coelicolor displays structural and biochemical similarities to the metazoan nuclear IF lamin. FilP, like IF proteins, is composed of central coiled-coil domains interrupted by short linkers and flanked by head and tail domains. FilP polymerizes into repetitive filament bundles with paracrystalline properties. However, the cations Na+ and K+ are found to induce the formation of a FilP hexagonal meshwork with the same 60-nm repetitive unit as the filaments. Studies of polymerization kinetics, in combination with EM techniques, enabled visualization of the basic building block-a transiently soluble rod-shaped FilP molecule-and its assembly into protofilaments and filament bundles. Cryoelectron tomography provided a 3D view of the FilP bundle structure and an original assembly model of an IF-like protein of prokaryotic origin, thereby enabling a comparison with the assembly of metazoan IF.</p>}},
author = {{Javadi, Ala and Söderholm, Niklas and Olofsson, Annelie and Flärdh, Klas and Sandblad, Linda}},
issn = {{2575-1077}},
language = {{eng}},
number = {{3}},
publisher = {{Rockefeller University Press}},
series = {{Life Science Alliance}},
title = {{Assembly mechanisms of the bacterial cytoskeletal protein FilP}},
url = {{http://dx.doi.org/10.26508/lsa.201800290}},
doi = {{10.26508/lsa.201800290}},
volume = {{2}},
year = {{2019}},
}