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A Plasmodium multi-domain protein possesses multiple inositol phosphate kinase activities.

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A Plasmodium multi-domain protein possesses multiple inositol phosphate kinase activities. / Stritzke, Carina; Nalaskowski, Marcus; Fanick, Werner; Lin, Hongying; Mayr, Georg W.

in: MOL BIOCHEM PARASIT, Jahrgang 186, Nr. 2, 2, 2012, S. 134-138.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Stritzke, C, Nalaskowski, M, Fanick, W, Lin, H & Mayr, GW 2012, 'A Plasmodium multi-domain protein possesses multiple inositol phosphate kinase activities.', MOL BIOCHEM PARASIT, Jg. 186, Nr. 2, 2, S. 134-138. <http://www.ncbi.nlm.nih.gov/pubmed/23123170?dopt=Citation>

APA

Stritzke, C., Nalaskowski, M., Fanick, W., Lin, H., & Mayr, G. W. (2012). A Plasmodium multi-domain protein possesses multiple inositol phosphate kinase activities. MOL BIOCHEM PARASIT, 186(2), 134-138. [2]. http://www.ncbi.nlm.nih.gov/pubmed/23123170?dopt=Citation

Vancouver

Stritzke C, Nalaskowski M, Fanick W, Lin H, Mayr GW. A Plasmodium multi-domain protein possesses multiple inositol phosphate kinase activities. MOL BIOCHEM PARASIT. 2012;186(2):134-138. 2.

Bibtex

@article{eafe82ed5af74e219ca193b696b29dd6,
title = "A Plasmodium multi-domain protein possesses multiple inositol phosphate kinase activities.",
abstract = "The synchronization of intraerythrocytic maturation of Plasmodium parasites is an important factor in the malaria infection process. Synchronization is mediated by inositol phosphate (InsP(x))-induced Ca(2+)-release from internal stores. To further investigate the InsP(x) metabolism in these parasites a Plasmodium protein possessing inositol phosphate kinase (IPK) activity was recombinantly expressed, purified and enzymatically characterized for the first time. Its main activity is the conversion of the Ca(2+)-releasing second messenger Ins(1,4,5)P(3) to Ins(1,3,4,5)P(4), an important factor in chromatin remodeling and also in Ca(2+)-release. This protein possesses several additional IPK activities pointing to a potential role as inositol phosphate multikinase. Interestingly, we have also identified three putative subdomains of histone deacetylase in this protein possibly linking InsP(x)- and acetylation-mediated transcription regulation. Furthermore, we examined the inhibitory potential of >40 polyphenolic substances against its kinase activity. Because of the important role of InsP(x)-induced Ca(2+)-release in the development of Plasmodium parasites, IPKs are interesting targets for novel antimalarial approaches.",
keywords = "Animals, Humans, Amino Acid Sequence, Molecular Sequence Data, Sequence Alignment, Inhibitory Concentration 50, Enzyme Activation/drug effects, Enzyme Inhibitors/pharmacology, Phosphotransferases (Alcohol Group Acceptor)/antagonists & inhibitors/genetics/*metabolism, Plasmodium/genetics/*metabolism, Polyphenols/pharmacology, Protein Interaction Domains and Motifs/genetics, Protozoan Proteins/chemistry/genetics/*metabolism, Recombinant Proteins/chemistry/genetics/metabolism, Animals, Humans, Amino Acid Sequence, Molecular Sequence Data, Sequence Alignment, Inhibitory Concentration 50, Enzyme Activation/drug effects, Enzyme Inhibitors/pharmacology, Phosphotransferases (Alcohol Group Acceptor)/antagonists & inhibitors/genetics/*metabolism, Plasmodium/genetics/*metabolism, Polyphenols/pharmacology, Protein Interaction Domains and Motifs/genetics, Protozoan Proteins/chemistry/genetics/*metabolism, Recombinant Proteins/chemistry/genetics/metabolism",
author = "Carina Stritzke and Marcus Nalaskowski and Werner Fanick and Hongying Lin and Mayr, {Georg W.}",
year = "2012",
language = "English",
volume = "186",
pages = "134--138",
journal = "MOL BIOCHEM PARASIT",
issn = "0166-6851",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - A Plasmodium multi-domain protein possesses multiple inositol phosphate kinase activities.

AU - Stritzke, Carina

AU - Nalaskowski, Marcus

AU - Fanick, Werner

AU - Lin, Hongying

AU - Mayr, Georg W.

PY - 2012

Y1 - 2012

N2 - The synchronization of intraerythrocytic maturation of Plasmodium parasites is an important factor in the malaria infection process. Synchronization is mediated by inositol phosphate (InsP(x))-induced Ca(2+)-release from internal stores. To further investigate the InsP(x) metabolism in these parasites a Plasmodium protein possessing inositol phosphate kinase (IPK) activity was recombinantly expressed, purified and enzymatically characterized for the first time. Its main activity is the conversion of the Ca(2+)-releasing second messenger Ins(1,4,5)P(3) to Ins(1,3,4,5)P(4), an important factor in chromatin remodeling and also in Ca(2+)-release. This protein possesses several additional IPK activities pointing to a potential role as inositol phosphate multikinase. Interestingly, we have also identified three putative subdomains of histone deacetylase in this protein possibly linking InsP(x)- and acetylation-mediated transcription regulation. Furthermore, we examined the inhibitory potential of >40 polyphenolic substances against its kinase activity. Because of the important role of InsP(x)-induced Ca(2+)-release in the development of Plasmodium parasites, IPKs are interesting targets for novel antimalarial approaches.

AB - The synchronization of intraerythrocytic maturation of Plasmodium parasites is an important factor in the malaria infection process. Synchronization is mediated by inositol phosphate (InsP(x))-induced Ca(2+)-release from internal stores. To further investigate the InsP(x) metabolism in these parasites a Plasmodium protein possessing inositol phosphate kinase (IPK) activity was recombinantly expressed, purified and enzymatically characterized for the first time. Its main activity is the conversion of the Ca(2+)-releasing second messenger Ins(1,4,5)P(3) to Ins(1,3,4,5)P(4), an important factor in chromatin remodeling and also in Ca(2+)-release. This protein possesses several additional IPK activities pointing to a potential role as inositol phosphate multikinase. Interestingly, we have also identified three putative subdomains of histone deacetylase in this protein possibly linking InsP(x)- and acetylation-mediated transcription regulation. Furthermore, we examined the inhibitory potential of >40 polyphenolic substances against its kinase activity. Because of the important role of InsP(x)-induced Ca(2+)-release in the development of Plasmodium parasites, IPKs are interesting targets for novel antimalarial approaches.

KW - Animals

KW - Humans

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Sequence Alignment

KW - Inhibitory Concentration 50

KW - Enzyme Activation/drug effects

KW - Enzyme Inhibitors/pharmacology

KW - Phosphotransferases (Alcohol Group Acceptor)/antagonists & inhibitors/genetics/metabolism

KW - Plasmodium/genetics/metabolism

KW - Polyphenols/pharmacology

KW - Protein Interaction Domains and Motifs/genetics

KW - Protozoan Proteins/chemistry/genetics/metabolism

KW - Recombinant Proteins/chemistry/genetics/metabolism

KW - Animals

KW - Humans

KW - Amino Acid Sequence

KW - Molecular Sequence Data

KW - Sequence Alignment

KW - Inhibitory Concentration 50

KW - Enzyme Activation/drug effects

KW - Enzyme Inhibitors/pharmacology

KW - Phosphotransferases (Alcohol Group Acceptor)/antagonists & inhibitors/genetics/metabolism

KW - Plasmodium/genetics/metabolism

KW - Polyphenols/pharmacology

KW - Protein Interaction Domains and Motifs/genetics

KW - Protozoan Proteins/chemistry/genetics/metabolism

KW - Recombinant Proteins/chemistry/genetics/metabolism

M3 - SCORING: Journal article

VL - 186

SP - 134

EP - 138

JO - MOL BIOCHEM PARASIT

JF - MOL BIOCHEM PARASIT

SN - 0166-6851

IS - 2

M1 - 2

ER -