Striated muscle UNC-45 (SM UNC-45) protein acts as a chaperone for cardiac and skeletal muscle myosins; regulating their folding, assembly into thick filaments, interaction with other sarcomeric proteins, and degradation. GATA4 is an important transcription factor that regulates the expression of several cardiac muscle proteins, including myosin. A previous study demonstrated for the first time that SM UNC-45 (also known as UNC-45B) physically interacted with GATA4. The major revelation from this study is that SM UNC-45 has the potential to exert both short-term (protein level) and long-term (gene level) controls over myosin and therefore muscle structure and function. The aim of this study was to identify the specific domain in UNC-45 that interacted with GATA4 using protein-protein interaction techniques. Pull down assays suggested that GATA4 bound to the UCS domain of SM UNC-45, and possibly required flanking sequence in the central domain. Understanding this interaction can provide important mechanistic insight into how the SM UNC-45/GATA4 complex modulates muscle structure, function, and perhaps myopathies.
","abstract_html":"<p>Striated muscle UNC-45 (SM UNC-45) protein acts as a chaperone for cardiac and skeletal muscle myosins; regulating their folding, assembly into thick filaments, interaction with other sarcomeric proteins, and degradation. GATA4 is an important transcription factor that regulates the expression of several cardiac muscle proteins, including myosin. A previous study demonstrated for the first time that SM UNC-45 (also known as UNC-45B) physically interacted with GATA4. The major revelation from this study is that SM UNC-45 has the potential to exert both short-term (protein level) and long-term (gene level) controls over myosin and therefore muscle structure and function. The aim of this study was to identify the specific domain in UNC-45 that interacted with GATA4 using protein-protein interaction techniques. Pull down assays suggested that GATA4 bound to the UCS domain of SM UNC-45, and possibly required flanking sequence in the central domain. Understanding this interaction can provide important mechanistic insight into how the SM UNC-45/GATA4 complex modulates muscle structure, function, and perhaps myopathies.</p>","abstract_has_math":false,"creators":["Anderson, Morgan"],"institution":null,"degree_name":"Master of Science - Natural Sciences","degree_level":"Thesis","degree_discipline":"College of Science and Mathematics","degree_department":null,"school":null,"contributors":["Odutayo Odunuga","Michele Harris","Kefa Onchoke"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2019,"date_issued":"2019-05-18T07:00:00Z","date_published":"2019-05-18T07:00:00Z","updated_at":"2026-07-24T04:30:22Z","subjects":["UNC-45","GATA4","protein interaction","chaperone","domain","pull-down assay","Biochemistry"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://scholarworks.sfasu.edu/etds/269","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Odutayo Odunuga","Michele Harris","Kefa Onchoke"]},{"key":"dc:creator","label":"Author","values":["Anderson, Morgan"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2024-05-20T07:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["College of Science and Mathematics"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Thesis"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Master of Science - Natural Sciences"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["UNC-45","GATA4","protein interaction","chaperone","domain","pull-down assay","Biochemistry"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://scholarworks.sfasu.edu/etds/269"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Striated muscle UNC-45 (SM UNC-45) protein acts as a chaperone for cardiac and skeletal muscle myosins; regulating their folding, assembly into thick filaments, interaction with other sarcomeric proteins, and degradation. GATA4 is an important transcription factor that regulates the expression of several cardiac muscle proteins, including myosin. A previous study demonstrated for the first time that SM UNC-45 (also known as UNC-45B) physically interacted with GATA4. The major revelation from this study is that SM UNC-45 has the potential to exert both short-term (protein level) and long-term (gene level) controls over myosin and therefore muscle structure and function. The aim of this study was to identify the specific domain in UNC-45 that interacted with GATA4 using protein-protein interaction techniques. Pull down assays suggested that GATA4 bound to the UCS domain of SM UNC-45, and possibly required flanking sequence in the central domain. Understanding this interaction can provide important mechanistic insight into how the SM UNC-45/GATA4 complex modulates muscle structure, function, and perhaps myopathies.
"]},{"key":"dc:title","label":"Title","values":["GENERATION OF FULL-LENGTH WILD-TYPE GATA4 PROTEIN AND CHARACTERIZATION OF ITS BINDING TO UNC-45 DOMAINS"]}]}],"canonical_facts":{"dc:contributor":["Odutayo Odunuga","Michele Harris","Kefa Onchoke"],"dc:creator":["Anderson, Morgan"],"dc:date.available":["2024-05-20T07:00:00Z"],"dc:description.abstract":["Striated muscle UNC-45 (SM UNC-45) protein acts as a chaperone for cardiac and skeletal muscle myosins; regulating their folding, assembly into thick filaments, interaction with other sarcomeric proteins, and degradation. GATA4 is an important transcription factor that regulates the expression of several cardiac muscle proteins, including myosin. A previous study demonstrated for the first time that SM UNC-45 (also known as UNC-45B) physically interacted with GATA4. The major revelation from this study is that SM UNC-45 has the potential to exert both short-term (protein level) and long-term (gene level) controls over myosin and therefore muscle structure and function. The aim of this study was to identify the specific domain in UNC-45 that interacted with GATA4 using protein-protein interaction techniques. Pull down assays suggested that GATA4 bound to the UCS domain of SM UNC-45, and possibly required flanking sequence in the central domain. Understanding this interaction can provide important mechanistic insight into how the SM UNC-45/GATA4 complex modulates muscle structure, function, and perhaps myopathies.
"],"dc:identifier":["https://scholarworks.sfasu.edu/etds/269"],"dc:subject":["UNC-45","GATA4","protein interaction","chaperone","domain","pull-down assay","Biochemistry"],"dc:title":["GENERATION OF FULL-LENGTH WILD-TYPE GATA4 PROTEIN AND CHARACTERIZATION OF ITS BINDING TO UNC-45 DOMAINS"],"thesis:degree_discipline":["College of Science and Mathematics"],"thesis:degree_level":["Thesis"],"thesis:degree_name":["Master of Science - Natural Sciences"]},"updated_at":"2026-07-24T04:30:22Z"}