{"id":{"repo_id":"kennesaw","oai_identifier":"oai:digitalcommons.kennesaw.edu:integrbiol_etd-1009"},"canonical_url":"https://search.dev.ndltd.org/etd/kennesaw/oai:digitalcommons.kennesaw.edu:integrbiol_etd-1009","repository":{"repo_id":"kennesaw","name":"Kennesaw State University","base_url":"https://digitalcommons.kennesaw.edu/do/oai/"},"display":{"title":"The HV1 proton channel of Lingulodinium polyedrum localizes to the bioluminescent scintillon","abstract":"<p>In 1972, J. Woodland Hastings and colleagues predicted the existence of a proton selective channel that opens in response to depolarizing voltage (H<sub>V</sub>1) across the vacuole membrane of bioluminescent dinoflagellates and conducts protons into specialized luminescence compartments (scintillons), thus causing the pH drop that triggers the light flash. RNA-Seq data from several luminescent dinoflagellate species provided candidate H<sub>V</sub>1 genes. When expressed in mammalian cells, the predicted H<sub>V</sub>1 from <em>Lingulodinium polyedrum </em>displays the hallmark properties of bona fide proton channels, including time-dependent opening with depolarization, perfect proton selectivity, and characteristic pH dependent gating. RT-PCR and Western blotting confirm expression of H<sub>V</sub>1 in <em>L. polyedrum</em> and isolated scintillons. Fluorescence confocal microscopy of <em>L. polyedrum </em>cells stained with antibodies to luminescence proteins luciferase (LCF), luciferin binding protein (LBP) and to H<sub>V</sub>1 (LpH<sub>V</sub>1) reveal structures consistent with H<sub>V</sub>1’s proposed function in bioluminescence. Isolated scintillons immunostained with antibody to LpH<sub>V</sub>1 displayed LpH<sub>V</sub>1 expression, showing that LpH<sub>V</sub>1 is present in this organelle. In addition, proteomics analysis demonstrated that isolated scintillon preparations contain peptides that map to LpH<sub>V</sub>1, including a portion of the epitope used to raise the antibody. These results indicate that LpH<sub>V</sub>1 is the voltage gated proton channel that triggers bioluminescence in <em>L. polyedrum</em>.</p>","abstract_html":"&lt;p&gt;In 1972, J. Woodland Hastings and colleagues predicted the existence of a proton selective channel that opens in response to depolarizing voltage (H&lt;sub&gt;V&lt;/sub&gt;1) across the vacuole membrane of bioluminescent dinoflagellates and conducts protons into specialized luminescence compartments (scintillons), thus causing the pH drop that triggers the light flash. RNA-Seq data from several luminescent dinoflagellate species provided candidate H&lt;sub&gt;V&lt;/sub&gt;1 genes. When expressed in mammalian cells, the predicted H&lt;sub&gt;V&lt;/sub&gt;1 from &lt;em&gt;Lingulodinium polyedrum &lt;/em&gt;displays the hallmark properties of bona fide proton channels, including time-dependent opening with depolarization, perfect proton selectivity, and characteristic pH dependent gating. RT-PCR and Western blotting confirm expression of H&lt;sub&gt;V&lt;/sub&gt;1 in &lt;em&gt;L. polyedrum&lt;/em&gt; and isolated scintillons. Fluorescence confocal microscopy of &lt;em&gt;L. polyedrum &lt;/em&gt;cells stained with antibodies to luminescence proteins luciferase (LCF), luciferin binding protein (LBP) and to H&lt;sub&gt;V&lt;/sub&gt;1 (LpH&lt;sub&gt;V&lt;/sub&gt;1) reveal structures consistent with H&lt;sub&gt;V&lt;/sub&gt;1’s proposed function in bioluminescence. Isolated scintillons immunostained with antibody to LpH&lt;sub&gt;V&lt;/sub&gt;1 displayed LpH&lt;sub&gt;V&lt;/sub&gt;1 expression, showing that LpH&lt;sub&gt;V&lt;/sub&gt;1 is present in this organelle. In addition, proteomics analysis demonstrated that isolated scintillon preparations contain peptides that map to LpH&lt;sub&gt;V&lt;/sub&gt;1, including a portion of the epitope used to raise the antibody. These results indicate that LpH&lt;sub&gt;V&lt;/sub&gt;1 is the voltage gated proton channel that triggers bioluminescence in &lt;em&gt;L. polyedrum&lt;/em&gt;.&lt;/p&gt;","abstract_has_math":false,"creators":["Rodriguez, Juan D."],"institution":null,"degree_name":"Master of Science in Integrative Biology (MSIB)","degree_level":"Thesis","degree_discipline":"Biology","degree_department":null,"school":null,"contributors":["Susan M.E. Smith","Donald J. McGarey","Scott J. Nowak"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2016,"date_issued":"2016-05-10T07:00:00Z","date_published":"2016-05-10T07:00:00Z","updated_at":"2026-07-24T02:43:09Z","subjects":["dinoflagellates","Lingulodinium polyedrum","scintillon","bioluminescent","LpHv1","Biology","Integrative Biology"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://digitalcommons.kennesaw.edu/integrbiol_etd/10","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Susan M.E. Smith","Donald J. McGarey","Scott J. Nowak"]},{"key":"dc:creator","label":"Author","values":["Rodriguez, Juan D."]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2017-02-22T08:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biology"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science in Integrative Biology (MSIB)"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["dinoflagellates","Lingulodinium polyedrum","scintillon","bioluminescent","LpHv1","Biology","Integrative Biology"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://digitalcommons.kennesaw.edu/integrbiol_etd/10"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["<p>In 1972, J. Woodland Hastings and colleagues predicted the existence of a proton selective channel that opens in response to depolarizing voltage (H<sub>V</sub>1) across the vacuole membrane of bioluminescent dinoflagellates and conducts protons into specialized luminescence compartments (scintillons), thus causing the pH drop that triggers the light flash. RNA-Seq data from several luminescent dinoflagellate species provided candidate H<sub>V</sub>1 genes. When expressed in mammalian cells, the predicted H<sub>V</sub>1 from <em>Lingulodinium polyedrum </em>displays the hallmark properties of bona fide proton channels, including time-dependent opening with depolarization, perfect proton selectivity, and characteristic pH dependent gating. RT-PCR and Western blotting confirm expression of H<sub>V</sub>1 in <em>L. polyedrum</em> and isolated scintillons. Fluorescence confocal microscopy of <em>L. polyedrum </em>cells stained with antibodies to luminescence proteins luciferase (LCF), luciferin binding protein (LBP) and to H<sub>V</sub>1 (LpH<sub>V</sub>1) reveal structures consistent with H<sub>V</sub>1’s proposed function in bioluminescence. Isolated scintillons immunostained with antibody to LpH<sub>V</sub>1 displayed LpH<sub>V</sub>1 expression, showing that LpH<sub>V</sub>1 is present in this organelle. In addition, proteomics analysis demonstrated that isolated scintillon preparations contain peptides that map to LpH<sub>V</sub>1, including a portion of the epitope used to raise the antibody. These results indicate that LpH<sub>V</sub>1 is the voltage gated proton channel that triggers bioluminescence in <em>L. polyedrum</em>.</p>"]},{"key":"dc:title","label":"Title","values":["The HV1 proton channel of Lingulodinium polyedrum localizes to the bioluminescent scintillon"]}]}],"canonical_facts":{"dc:contributor":["Susan M.E. Smith","Donald J. McGarey","Scott J. Nowak"],"dc:creator":["Rodriguez, Juan D."],"dc:date.available":["2017-02-22T08:00:00Z"],"dc:description.abstract":["<p>In 1972, J. Woodland Hastings and colleagues predicted the existence of a proton selective channel that opens in response to depolarizing voltage (H<sub>V</sub>1) across the vacuole membrane of bioluminescent dinoflagellates and conducts protons into specialized luminescence compartments (scintillons), thus causing the pH drop that triggers the light flash. RNA-Seq data from several luminescent dinoflagellate species provided candidate H<sub>V</sub>1 genes. When expressed in mammalian cells, the predicted H<sub>V</sub>1 from <em>Lingulodinium polyedrum </em>displays the hallmark properties of bona fide proton channels, including time-dependent opening with depolarization, perfect proton selectivity, and characteristic pH dependent gating. RT-PCR and Western blotting confirm expression of H<sub>V</sub>1 in <em>L. polyedrum</em> and isolated scintillons. Fluorescence confocal microscopy of <em>L. polyedrum </em>cells stained with antibodies to luminescence proteins luciferase (LCF), luciferin binding protein (LBP) and to H<sub>V</sub>1 (LpH<sub>V</sub>1) reveal structures consistent with H<sub>V</sub>1’s proposed function in bioluminescence. Isolated scintillons immunostained with antibody to LpH<sub>V</sub>1 displayed LpH<sub>V</sub>1 expression, showing that LpH<sub>V</sub>1 is present in this organelle. In addition, proteomics analysis demonstrated that isolated scintillon preparations contain peptides that map to LpH<sub>V</sub>1, including a portion of the epitope used to raise the antibody. These results indicate that LpH<sub>V</sub>1 is the voltage gated proton channel that triggers bioluminescence in <em>L. polyedrum</em>.</p>"],"dc:identifier":["https://digitalcommons.kennesaw.edu/integrbiol_etd/10"],"dc:subject":["dinoflagellates","Lingulodinium polyedrum","scintillon","bioluminescent","LpHv1","Biology","Integrative Biology"],"dc:title":["The HV1 proton channel of Lingulodinium polyedrum localizes to the bioluminescent scintillon"],"thesis:degree_discipline":["Biology"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["Master of Science in Integrative Biology (MSIB)"]},"updated_at":"2026-07-24T02:43:09Z"}