Publications by authors named "Courtney Ozzello"

Ciliates, such as evolved complex mechanisms to determine both the location and dimensions of cortical organelles such as the oral apparatus (OA: involved in phagocytosis), cytoproct (Cyp: for eliminating wastes), and contractile vacuole pores (CVPs: involved in water expulsion). Mutations have been recovered in that affect both the localization of such organelles along anterior-posterior and circumferential body axes and their dimensions. Here we describe , a ciliate pattern gene that encodes a conserved Beige-BEACH domain-containing protein a with possible protein kinase A (PKA)-anchoring activity.

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The spindle pole body (SPB) serves as the sole microtubule-organizing center of the cell, nucleating both cytoplasmic and nuclear microtubules. Yeast pericentrin, Spc110, binds to and activates the γ-tubulin complex via its N terminus, allowing nuclear microtubule polymerization to occur. The Spc110 C terminus links the γ-tubulin complex to the central plaque of the SPB by binding to Spc42, Spc29, and calmodulin (Cmd1).

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Basal bodies (BBs) are microtubule-based organelles that act as a template for and stabilize cilia at the cell surface. Centrins ubiquitously associate with BBs and function in BB assembly, maturation and stability. Human POC5 (hPOC5) is a highly conserved centrin-binding protein that binds centrins through Sfi1p-like repeats and is required for building full-length, mature centrioles.

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Article Synopsis
  • During sexual reproduction in ciliates like Tetrahymena thermophila, specialized adhesion zones are formed to allow for the exchange of gametic pronuclei through a membrane called the mating junction.
  • The passage of pronuclei through this junction requires microtubules and results in two membrane breaches that need to be sealed post-fertilization.
  • Rather than simply growing new membrane from the edges like in other cells, the breaches transform into complex membrane structures that grow into the partner's cytoplasm and connect to the plasma membrane, revealing a unique mechanism for membrane restoration.
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HAP2, a male-gamete-specific protein conserved across vast evolutionary distances, has garnered considerable attention as a potential membrane fusogen required for fertilization in taxa ranging from protozoa and green algae to flowering plants and invertebrate animals [1-6]. However, its presence in Tetrahymena thermophila, a ciliated protozoan with seven sexes or mating types that bypasses the production of male gametes, raises interesting questions regarding the evolutionary origins of gamete-specific functions in sexually dimorphic species. Here we show that HAP2 is expressed in all seven mating types of T.

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Using serial-section transmission electron microscopy and three-dimensional (3D) electron tomography, we characterized membrane dynamics that accompany the construction of a nuclear exchange junction between mating cells in the ciliate Tetrahymena thermophila. Our methods revealed a number of previously unknown features. (i) Membrane fusion is initiated by the extension of hundreds of 50-nm-diameter protrusions from the plasma membrane.

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