The Plasmodium Class XIV Myosin, MyoB, Has a Distinct Subcellular Location in Invasive and Motile Stages of the Malaria Parasite and an Unusual Light Chain

Yusuf, Noor A; Green, Judith L; Wall, Richard J; Knuepfer, Ellen; Moon, Robert W; Schulte-Huxel, Christina; Limenitakis Stanway, Rebecca; Martin, Stephen R; Howell, Steven A; Douse, Christopher H; Cota, Ernesto; Tate, Edward W; Tewari, Rita; Holder, Anthony A (2015). The Plasmodium Class XIV Myosin, MyoB, Has a Distinct Subcellular Location in Invasive and Motile Stages of the Malaria Parasite and an Unusual Light Chain. Journal of biological chemistry, 290(19), pp. 12147-12164. American Society for Biochemistry and Molecular Biology 10.1074/jbc.M115.637694

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Myosin B (MyoB) is one of the two short class XIV myosins encoded in the Plasmodium genome. Class XIV myosins are characterized by a catalytic "head," a modified "neck," and the absence of a "tail" region. Myosin A (MyoA), the other class XIV myosin in Plasmodium, has been established as a component of the glideosome complex important in motility and cell invasion, but MyoB is not well characterized. We analyzed the properties of MyoB using three parasite species as follows: Plasmodium falciparum, Plasmodium berghei, and Plasmodium knowlesi. MyoB is expressed in all invasive stages (merozoites, ookinetes, and sporozoites) of the life cycle, and the protein is found in a discrete apical location in these polarized cells. In P. falciparum, MyoB is synthesized very late in schizogony/merogony, and its location in merozoites is distinct from, and anterior to, that of a range of known proteins present in the rhoptries, rhoptry neck or micronemes. Unlike MyoA, MyoB is not associated with glideosome complex proteins, including the MyoA light chain, myosin A tail domain-interacting protein (MTIP). A unique MyoB light chain (MLC-B) was identified that contains a calmodulin-like domain at the C terminus and an extended N-terminal region. MLC-B localizes to the same extreme apical pole in the cell as MyoB, and the two proteins form a complex. We propose that MLC-B is a MyoB-specific light chain, and for the short class XIV myosins that lack a tail region, the atypical myosin light chains may fulfill that role.

Item Type:

Journal Article (Original Article)

Division/Institute:

08 Faculty of Science > Department of Biology > Institute of Cell Biology
08 Faculty of Science > Department of Biology > Institute of Cell Biology > Malaria

UniBE Contributor:

Limenitakis Stanway, Rebecca

Subjects:

500 Science > 570 Life sciences; biology
500 Science

ISSN:

0021-9258

Publisher:

American Society for Biochemistry and Molecular Biology

Language:

English

Submitter:

Volker Heussler

Date Deposited:

10 Sep 2015 15:01

Last Modified:

10 Sep 2015 15:01

Publisher DOI:

10.1074/jbc.M115.637694

PubMed ID:

25802338

Uncontrolled Keywords:

Invasion, Malaria, Molecular Motor, Myosin, Parasite, Peptide Interaction, Plasmodium, Myosin Light Chain

BORIS DOI:

10.7892/boris.71393

URI:

https://boris.unibe.ch/id/eprint/71393

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