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The Neurospora plasma membrane Ca2+ pump.

P Stroobant, J B Dame, G A Scarborough

    Federation Proceedings
    |May 15, 1980
    PubMed
    Summary
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    Neurospora crassa plasma membrane vesicles actively transport calcium using a proton-translocating ATPase and a calcium/proton antiporter. This mechanism suggests a calcium exit pump function in intact cells.

    Area of Science:

    • Cell Biology
    • Biochemistry
    • Molecular Biology

    Background:

    • Calcium ions (Ca2+) are crucial signaling molecules in eukaryotic cells.
    • Understanding Ca2+ transport mechanisms is vital for cellular homeostasis.
    • Neurospora crassa is a model organism for studying eukaryotic cell functions.

    Purpose of the Study:

    • To investigate the mechanism of Mg2+-ATP-dependent Ca2+ transport in Neurospora crassa plasma membrane vesicles.
    • To elucidate the components and energy transduction involved in Ca2+ accumulation.
    • To explore the functional role of this Ca2+ transport system in intact cells.

    Main Methods:

    • Isolation of plasma membrane vesicles from Neurospora crassa using the concanavalin A method.
    • Measurement of Mg2+-ATP-dependent 45Ca2+ accumulation in isolated vesicles.

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  • Analysis of the components involved in Ca2+ transport, including ATPase and antiporter activities.

    • Main Results:

    • Plasma membrane vesicles demonstrated Mg2+-ATP-dependent 45Ca2+ uptake.
    • The Ca2+ transport system was identified to involve a proton-translocating ATPase (EC 3.6.1.3) and a Ca2+/H+ antiporter.
    • Vesicle orientation suggests a Ca2+ exit pump mechanism in the intact cell.

    Conclusions:

    • The Ca2+ transport system in Neurospora crassa utilizes both an electrogenic ATPase and a Ca2+/H+ antiporter.
    • This coupled system generates a transmembrane electrical potential and pH gradient to drive Ca2+ transport.
    • Findings provide insights into Ca2+ pump mechanisms in other eukaryotic cells.