FhCaBP1 (FH22): a Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

Charlotte M. Thomas, Sarah Cheung, David Timson

Research output: Contribution to journalArticle

Abstract

FH22 has been previously identified as a calcium-bindingprotein from the common liver fluke, Fasciola hepatica. It is part of a family of at least four proteins in this organism which combine an EF- hand containing N-terminal domain with a C-terminal dynein light chain- like domain. Here we report further biochemical properties of FH22, which we propose should be renamed FhCaBP1 for consistency with other family members. Molecular modelling predicted that the two domains are linked by a flexible region and that the second EF-hand in the N-terminal domain is most likely the calcium ion binding site. Native gel electrophoresis demonstrated that the protein binds both calcium and manganese ions, but not cadmium, magnesium, strontium, barium, cobalt, copper(II), iron (II), nickel, zinc, lead or potassium ions. Calcium ion binding alters the conformation of the protein and increases its stability towards thermal denaturation. FhCaBP1 is a dimer in solution and calcium ions have no detectable effect on the protein's ability to dimerise. FhCaBP1 binds to the calmodulin antagonists trifluoperazine and chlorpromazine. Overall, the FhCaBP1's biochemical properties are most similar to FhCaBP2 a fact consistent with the close sequence andpredicted structural similarity between the two proteins.
Original languageEnglish
Pages (from-to)109-115
Number of pages7
JournalExperimental Parasitology
Volume170
DOIs
Publication statusPublished - 28 Sep 2016

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Dyneins
Calcium-Binding Proteins
Ions
Calcium
Proteins
Trifluoperazine
Strontium
Denaturation
Molecular modeling
Chlorpromazine
Barium
Calmodulin
Manganese
Cobalt
Nickel
Electrophoresis
Cadmium
Dimers
Liver
Magnesium

Bibliographical note

© 2016. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/.

Keywords

  • Neglected tropical disease
  • EF-hand
  • Dynein light chain
  • Calcium binding
  • Liver fluke
  • Trematode protein

Cite this

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title = "FhCaBP1 (FH22): a Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains",
abstract = "FH22 has been previously identified as a calcium-bindingprotein from the common liver fluke, Fasciola hepatica. It is part of a family of at least four proteins in this organism which combine an EF- hand containing N-terminal domain with a C-terminal dynein light chain- like domain. Here we report further biochemical properties of FH22, which we propose should be renamed FhCaBP1 for consistency with other family members. Molecular modelling predicted that the two domains are linked by a flexible region and that the second EF-hand in the N-terminal domain is most likely the calcium ion binding site. Native gel electrophoresis demonstrated that the protein binds both calcium and manganese ions, but not cadmium, magnesium, strontium, barium, cobalt, copper(II), iron (II), nickel, zinc, lead or potassium ions. Calcium ion binding alters the conformation of the protein and increases its stability towards thermal denaturation. FhCaBP1 is a dimer in solution and calcium ions have no detectable effect on the protein's ability to dimerise. FhCaBP1 binds to the calmodulin antagonists trifluoperazine and chlorpromazine. Overall, the FhCaBP1's biochemical properties are most similar to FhCaBP2 a fact consistent with the close sequence andpredicted structural similarity between the two proteins.",
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FhCaBP1 (FH22): a Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains. / Thomas, Charlotte M.; Cheung, Sarah; Timson, David.

In: Experimental Parasitology, Vol. 170, 28.09.2016, p. 109-115.

Research output: Contribution to journalArticle

TY - JOUR

T1 - FhCaBP1 (FH22): a Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains

AU - Thomas, Charlotte M.

AU - Cheung, Sarah

AU - Timson, David

N1 - © 2016. This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/.

PY - 2016/9/28

Y1 - 2016/9/28

N2 - FH22 has been previously identified as a calcium-bindingprotein from the common liver fluke, Fasciola hepatica. It is part of a family of at least four proteins in this organism which combine an EF- hand containing N-terminal domain with a C-terminal dynein light chain- like domain. Here we report further biochemical properties of FH22, which we propose should be renamed FhCaBP1 for consistency with other family members. Molecular modelling predicted that the two domains are linked by a flexible region and that the second EF-hand in the N-terminal domain is most likely the calcium ion binding site. Native gel electrophoresis demonstrated that the protein binds both calcium and manganese ions, but not cadmium, magnesium, strontium, barium, cobalt, copper(II), iron (II), nickel, zinc, lead or potassium ions. Calcium ion binding alters the conformation of the protein and increases its stability towards thermal denaturation. FhCaBP1 is a dimer in solution and calcium ions have no detectable effect on the protein's ability to dimerise. FhCaBP1 binds to the calmodulin antagonists trifluoperazine and chlorpromazine. Overall, the FhCaBP1's biochemical properties are most similar to FhCaBP2 a fact consistent with the close sequence andpredicted structural similarity between the two proteins.

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