Pivotal and distinct role for Plasmodium actin capping protein alpha during blood infection of the malaria parasite
Ganter, Markus ; Rizopoulos, Zaira ; Schüler, Herwig LU
and Matuschewski, Kai
(2015)
In Molecular Microbiology
96(1).
p.84-94
- Abstract
Accurate regulation of microfilament dynamics is central to cell growth, motility and response to environmental stimuli. Stabilizing and depolymerizing proteins control the steady-state levels of filamentous (F-) actin. Capping protein (CP) binds to free barbed ends, thereby arresting microfilament growth and restraining elongation to remaining free barbed ends. In all CPs characterized to date, alpha and beta subunits form the active heterodimer. Here, we show in a eukaryotic parasitic cell that the two CP subunits can be functionally separated. Unlike the beta subunit, the CP alpha subunit of the apicomplexan parasite Plasmodium is refractory to targeted gene deletion during blood infection in the mammalian host. Combinatorial... (More)
Accurate regulation of microfilament dynamics is central to cell growth, motility and response to environmental stimuli. Stabilizing and depolymerizing proteins control the steady-state levels of filamentous (F-) actin. Capping protein (CP) binds to free barbed ends, thereby arresting microfilament growth and restraining elongation to remaining free barbed ends. In all CPs characterized to date, alpha and beta subunits form the active heterodimer. Here, we show in a eukaryotic parasitic cell that the two CP subunits can be functionally separated. Unlike the beta subunit, the CP alpha subunit of the apicomplexan parasite Plasmodium is refractory to targeted gene deletion during blood infection in the mammalian host. Combinatorial complementation of Plasmodium berghei CP genes with the orthologs from Plasmodium falciparum verified distinct activities of CP alpha and CP alpha/beta during parasite life cycle progression. Recombinant Plasmodium CP alpha could be produced in Escherichia coli in the absence of the beta subunit and the protein displayed F-actin capping activity. Thus, the functional separation of two CP subunits in a parasitic eukaryotic cell and the F-actin capping activity of CP alpha expand the repertoire of microfilament regulatory mechanisms assigned to CPs.
(Less)
- author
- Ganter, Markus
; Rizopoulos, Zaira
; Schüler, Herwig
LU
and Matuschewski, Kai
- publishing date
- 2015-04
- type
- Contribution to journal
- publication status
- published
- keywords
- Actin Capping Proteins/metabolism, Actin Cytoskeleton/genetics, Actins/metabolism, Gene Expression Profiling, Malaria/blood, Microfilament Proteins/genetics, Models, Molecular, Plasmodium berghei/genetics, Plasmodium falciparum/genetics, Protein Binding, Protein Subunits/metabolism, Protozoan Proteins/metabolism, Real-Time Polymerase Chain Reaction, Recombinant Proteins/metabolism
- in
- Molecular Microbiology
- volume
- 96
- issue
- 1
- pages
- 11 pages
- publisher
- Wiley-Blackwell
- external identifiers
-
- scopus:84925358937
- pmid:25565321
- ISSN
- 1365-2958
- DOI
- 10.1111/mmi.12922
- language
- English
- LU publication?
- no
- additional info
- © 2015 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.
- id
- ae47837d-80ae-431e-bcbf-c0b807b4a65b
- date added to LUP
- 2024-11-21 17:54:58
- date last changed
- 2025-02-14 11:29:59
@article{ae47837d-80ae-431e-bcbf-c0b807b4a65b,
abstract = {{<p>Accurate regulation of microfilament dynamics is central to cell growth, motility and response to environmental stimuli. Stabilizing and depolymerizing proteins control the steady-state levels of filamentous (F-) actin. Capping protein (CP) binds to free barbed ends, thereby arresting microfilament growth and restraining elongation to remaining free barbed ends. In all CPs characterized to date, alpha and beta subunits form the active heterodimer. Here, we show in a eukaryotic parasitic cell that the two CP subunits can be functionally separated. Unlike the beta subunit, the CP alpha subunit of the apicomplexan parasite Plasmodium is refractory to targeted gene deletion during blood infection in the mammalian host. Combinatorial complementation of Plasmodium berghei CP genes with the orthologs from Plasmodium falciparum verified distinct activities of CP alpha and CP alpha/beta during parasite life cycle progression. Recombinant Plasmodium CP alpha could be produced in Escherichia coli in the absence of the beta subunit and the protein displayed F-actin capping activity. Thus, the functional separation of two CP subunits in a parasitic eukaryotic cell and the F-actin capping activity of CP alpha expand the repertoire of microfilament regulatory mechanisms assigned to CPs.</p>}},
author = {{Ganter, Markus and Rizopoulos, Zaira and Schüler, Herwig and Matuschewski, Kai}},
issn = {{1365-2958}},
keywords = {{Actin Capping Proteins/metabolism; Actin Cytoskeleton/genetics; Actins/metabolism; Gene Expression Profiling; Malaria/blood; Microfilament Proteins/genetics; Models, Molecular; Plasmodium berghei/genetics; Plasmodium falciparum/genetics; Protein Binding; Protein Subunits/metabolism; Protozoan Proteins/metabolism; Real-Time Polymerase Chain Reaction; Recombinant Proteins/metabolism}},
language = {{eng}},
number = {{1}},
pages = {{84--94}},
publisher = {{Wiley-Blackwell}},
series = {{Molecular Microbiology}},
title = {{Pivotal and distinct role for Plasmodium actin capping protein alpha during blood infection of the malaria parasite}},
url = {{http://dx.doi.org/10.1111/mmi.12922}},
doi = {{10.1111/mmi.12922}},
volume = {{96}},
year = {{2015}},
}