A Plasmodium actin-depolymerizing factor that binds exclusively to actin monomers
Schüler, Herwig LU
; Mueller, Ann-Kristin
and Matuschewski, Kai
(2005)
In Molecular Biology of the Cell
16(9).
p.23-4013
- Abstract
ADF/cofilins (AC) are essential F- and G-actin binding proteins that modulate microfilament turnover. The genome of Plasmodium falciparum, the parasite causing malaria, contains two members of the AC family. Interestingly, P. falciparum ADF1 lacks the F-actin binding residues of the AC consensus. Reverse genetics in the rodent malaria model system suggest that ADF1 performs vital functions during the pathogenic red blood cell stages, whereas ADF2 is not present in these stages. We show that recombinant PfADF1 interacts with monomeric actin but does not bind to actin polymers. Although other AC proteins inhibit nucleotide exchange on monomeric actin, the Plasmodium ortholog stimulates nucleotide exchange. Thus, PfADF1 differs in its... (More)
ADF/cofilins (AC) are essential F- and G-actin binding proteins that modulate microfilament turnover. The genome of Plasmodium falciparum, the parasite causing malaria, contains two members of the AC family. Interestingly, P. falciparum ADF1 lacks the F-actin binding residues of the AC consensus. Reverse genetics in the rodent malaria model system suggest that ADF1 performs vital functions during the pathogenic red blood cell stages, whereas ADF2 is not present in these stages. We show that recombinant PfADF1 interacts with monomeric actin but does not bind to actin polymers. Although other AC proteins inhibit nucleotide exchange on monomeric actin, the Plasmodium ortholog stimulates nucleotide exchange. Thus, PfADF1 differs in its biochemical properties from previously known AC proteins and seems to promote turnover exclusively by interaction with actin monomers. These findings provide important insights into the low cytosolic abundance and unique turnover characteristics of actin polymers in parasites of the phylum Apicomplexa.
(Less)
- author
- Schüler, Herwig
LU
; Mueller, Ann-Kristin
and Matuschewski, Kai
- publishing date
- 2005-09
- type
- Contribution to journal
- publication status
- published
- keywords
- Actins/metabolism, Amino Acid Sequence, Animals, Binding Sites, Kinetics, Malaria, Falciparum/metabolism, Molecular Sequence Data, Plasmodium falciparum/metabolism, Protein Binding/physiology, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Temperature
- in
- Molecular Biology of the Cell
- volume
- 16
- issue
- 9
- pages
- 11 pages
- publisher
- American Society for Cell Biology
- external identifiers
-
- pmid:15975905
- scopus:24344440631
- ISSN
- 1059-1524
- DOI
- 10.1091/mbc.e05-02-0086
- language
- English
- LU publication?
- no
- id
- d01b7d4f-ff7e-45bd-be4d-29c967998aec
- date added to LUP
- 2024-11-21 18:06:34
- date last changed
- 2025-02-14 11:36:29
@article{d01b7d4f-ff7e-45bd-be4d-29c967998aec,
abstract = {{<p>ADF/cofilins (AC) are essential F- and G-actin binding proteins that modulate microfilament turnover. The genome of Plasmodium falciparum, the parasite causing malaria, contains two members of the AC family. Interestingly, P. falciparum ADF1 lacks the F-actin binding residues of the AC consensus. Reverse genetics in the rodent malaria model system suggest that ADF1 performs vital functions during the pathogenic red blood cell stages, whereas ADF2 is not present in these stages. We show that recombinant PfADF1 interacts with monomeric actin but does not bind to actin polymers. Although other AC proteins inhibit nucleotide exchange on monomeric actin, the Plasmodium ortholog stimulates nucleotide exchange. Thus, PfADF1 differs in its biochemical properties from previously known AC proteins and seems to promote turnover exclusively by interaction with actin monomers. These findings provide important insights into the low cytosolic abundance and unique turnover characteristics of actin polymers in parasites of the phylum Apicomplexa.</p>}},
author = {{Schüler, Herwig and Mueller, Ann-Kristin and Matuschewski, Kai}},
issn = {{1059-1524}},
keywords = {{Actins/metabolism; Amino Acid Sequence; Animals; Binding Sites; Kinetics; Malaria, Falciparum/metabolism; Molecular Sequence Data; Plasmodium falciparum/metabolism; Protein Binding/physiology; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Temperature}},
language = {{eng}},
number = {{9}},
pages = {{23--4013}},
publisher = {{American Society for Cell Biology}},
series = {{Molecular Biology of the Cell}},
title = {{A <i>Plasmodium </i>actin-depolymerizing factor that binds exclusively to actin monomers}},
url = {{http://dx.doi.org/10.1091/mbc.e05-02-0086}},
doi = {{10.1091/mbc.e05-02-0086}},
volume = {{16}},
year = {{2005}},
}