{"id":{"repo_id":"utswmed","oai_identifier":"oai:utswmed-ir.tdl.org:2152.5/358"},"canonical_url":"https://search.dev.ndltd.org/etd/utswmed/oai:utswmed-ir.tdl.org:2152.5/358","repository":{"repo_id":"utswmed","name":"University of Texas Southwestern Medical Center","base_url":"https://utswmed-ir.tdl.org/server/oai/request"},"display":{"title":"Discovery and Characterization of the Polycomb Repressive Complex 1 of C. Elegans","abstract":"unc-3 encodes the Caenorhabditis elegans homolog of the Olf-1/Early B cell factor family of transcription factors, which in vertebrates regulate development and differentiation of B lymphocytes, adipocytes, and cells of the nervous system. In the first chapter I analyze the role of unc-3 in determining the fates of neurons in ventral nerve cord (VNC). unc-3 mutants are uncoordinated in locomotion. I show that unc-3 represses a VC-like motor neuron program in the VA and VB motor neurons, which in wild-type animals control backwards and forwards locomotion, respectively. Our lab identified a physical interaction between UNC-3 and the C2H2 zinc finger transcription factor PAG-3, the mammalian homologs of which are coexpressed in olfactory epithelium and hematopoietic cells. Our data explain the locomotory defects of unc-3 mutants and suggest that interactions between unc-3 and pag-3 homologs in other species may be functionally important. The second chapter of the thesis is about the analysis of MIG-32 a RING protein similar to some Polycomb proteins that were identified in a yeast two hybrid screen with UNC-3 as bait. The Polycomb repression complex 2 (PRC2) methylates histone H3 lysine 27 at target genes to modify gene expression, and this mark is recognized by PRC1, which ubiquitylates histone H2A. In Caenorhabditis elegans, a complex of the MES-2, MES-3, and MES-6 proteins is functionally analogous to the PRC2 complex, but the functional analog of PRC1, and indeed whether C. elegans has such a complex, has been unclear. I describe here that MIG-32 is a homolog of BMI-1, a core component of PRC1. I also identify SPAT-3A as a homolog of Ring1B, a partner protein of BMI-1 in the PRC1 core complex. Mig-32 and spat-3 mutants have some defects that overlap with those of mes mutants. However, unlike the mes mutants, mig-32 and spat-3 mutants are fertile, despite lacking apparent H2A ubiquitylation. Migration and axon guidance of specific neurons were defective in mig-32 and spat-3 mutants. Our data suggest that mig-32 and spat-3 encode core components of a PRC1-like complex in C. elegans.","abstract_html":"unc-3 encodes the Caenorhabditis elegans homolog of the Olf-1/Early B cell factor family of transcription factors, which in vertebrates regulate development and differentiation of B lymphocytes, adipocytes, and cells of the nervous system. In the first chapter I analyze the role of unc-3 in determining the fates of neurons in ventral nerve cord (VNC). unc-3 mutants are uncoordinated in locomotion. I show that unc-3 represses a VC-like motor neuron program in the VA and VB motor neurons, which in wild-type animals control backwards and forwards locomotion, respectively. Our lab identified a physical interaction between UNC-3 and the C2H2 zinc finger transcription factor PAG-3, the mammalian homologs of which are coexpressed in olfactory epithelium and hematopoietic cells. Our data explain the locomotory defects of unc-3 mutants and suggest that interactions between unc-3 and pag-3 homologs in other species may be functionally important. The second chapter of the thesis is about the analysis of MIG-32 a RING protein similar to some Polycomb proteins that were identified in a yeast two hybrid screen with UNC-3 as bait. The Polycomb repression complex 2 (PRC2) methylates histone H3 lysine 27 at target genes to modify gene expression, and this mark is recognized by PRC1, which ubiquitylates histone H2A. In Caenorhabditis elegans, a complex of the MES-2, MES-3, and MES-6 proteins is functionally analogous to the PRC2 complex, but the functional analog of PRC1, and indeed whether C. elegans has such a complex, has been unclear. I describe here that MIG-32 is a homolog of BMI-1, a core component of PRC1. I also identify SPAT-3A as a homolog of Ring1B, a partner protein of BMI-1 in the PRC1 core complex. Mig-32 and spat-3 mutants have some defects that overlap with those of mes mutants. However, unlike the mes mutants, mig-32 and spat-3 mutants are fertile, despite lacking apparent H2A ubiquitylation. Migration and axon guidance of specific neurons were defective in mig-32 and spat-3 mutants. Our data suggest that mig-32 and spat-3 encode core components of a PRC1-like complex in C. elegans.","abstract_has_math":false,"creators":["Karakuzu, Ozgur"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Cameron, Scott"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2010,"date_issued":"2010-07-12T17:44:34Z","date_published":"2010-07-12T17:44:34Z","updated_at":"2026-07-24T05:52:29Z","subjects":["Caenorhabditis elegans","Carrier Proteins","Cell Movement"],"languages":["en"],"rights":[],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["754616644"],"render_values":[{"text":"754616644","href":null,"code":true}]}]},"links":{"outbound_url":"https://hdl.handle.net/2152.5/358","outbound_label":"Handle","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Cameron, Scott"]},{"key":"dc:creator","label":"Author","values":["Karakuzu, Ozgur"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2010-07-12T17:44:34Z","2009-06-17"]},{"key":"dc:type","label":"Dc Type","values":["Thesis","Text","dissertation"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Caenorhabditis elegans","Carrier Proteins","Cell Movement"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["en"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://hdl.handle.net/2152.5/358","754616644"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["unc-3 encodes the Caenorhabditis elegans homolog of the Olf-1/Early B cell factor family of transcription factors, which in vertebrates regulate development and differentiation of B lymphocytes, adipocytes, and cells of the nervous system. In the first chapter I analyze the role of unc-3 in determining the fates of neurons in ventral nerve cord (VNC). unc-3 mutants are uncoordinated in locomotion. I show that unc-3 represses a VC-like motor neuron program in the VA and VB motor neurons, which in wild-type animals control backwards and forwards locomotion, respectively. Our lab identified a physical interaction between UNC-3 and the C2H2 zinc finger transcription factor PAG-3, the mammalian homologs of which are coexpressed in olfactory epithelium and hematopoietic cells. Our data explain the locomotory defects of unc-3 mutants and suggest that interactions between unc-3 and pag-3 homologs in other species may be functionally important. The second chapter of the thesis is about the analysis of MIG-32 a RING protein similar to some Polycomb proteins that were identified in a yeast two hybrid screen with UNC-3 as bait. The Polycomb repression complex 2 (PRC2) methylates histone H3 lysine 27 at target genes to modify gene expression, and this mark is recognized by PRC1, which ubiquitylates histone H2A. In Caenorhabditis elegans, a complex of the MES-2, MES-3, and MES-6 proteins is functionally analogous to the PRC2 complex, but the functional analog of PRC1, and indeed whether C. elegans has such a complex, has been unclear. I describe here that MIG-32 is a homolog of BMI-1, a core component of PRC1. I also identify SPAT-3A as a homolog of Ring1B, a partner protein of BMI-1 in the PRC1 core complex. Mig-32 and spat-3 mutants have some defects that overlap with those of mes mutants. However, unlike the mes mutants, mig-32 and spat-3 mutants are fertile, despite lacking apparent H2A ubiquitylation. Migration and axon guidance of specific neurons were defective in mig-32 and spat-3 mutants. Our data suggest that mig-32 and spat-3 encode core components of a PRC1-like complex in C. elegans."]},{"key":"dc:format","label":"Dc Format","values":["Electronic","application/pdf","born digital"]},{"key":"dc:title","label":"Title","values":["Discovery and Characterization of the Polycomb Repressive Complex 1 of C. Elegans"]}]}],"canonical_facts":{"dc:contributor":["Cameron, Scott"],"dc:creator":["Karakuzu, Ozgur"],"dc:date":["2010-07-12T17:44:34Z","2009-06-17"],"dc:description":["unc-3 encodes the Caenorhabditis elegans homolog of the Olf-1/Early B cell factor family of transcription factors, which in vertebrates regulate development and differentiation of B lymphocytes, adipocytes, and cells of the nervous system. In the first chapter I analyze the role of unc-3 in determining the fates of neurons in ventral nerve cord (VNC). unc-3 mutants are uncoordinated in locomotion. I show that unc-3 represses a VC-like motor neuron program in the VA and VB motor neurons, which in wild-type animals control backwards and forwards locomotion, respectively. Our lab identified a physical interaction between UNC-3 and the C2H2 zinc finger transcription factor PAG-3, the mammalian homologs of which are coexpressed in olfactory epithelium and hematopoietic cells. Our data explain the locomotory defects of unc-3 mutants and suggest that interactions between unc-3 and pag-3 homologs in other species may be functionally important. The second chapter of the thesis is about the analysis of MIG-32 a RING protein similar to some Polycomb proteins that were identified in a yeast two hybrid screen with UNC-3 as bait. The Polycomb repression complex 2 (PRC2) methylates histone H3 lysine 27 at target genes to modify gene expression, and this mark is recognized by PRC1, which ubiquitylates histone H2A. In Caenorhabditis elegans, a complex of the MES-2, MES-3, and MES-6 proteins is functionally analogous to the PRC2 complex, but the functional analog of PRC1, and indeed whether C. elegans has such a complex, has been unclear. I describe here that MIG-32 is a homolog of BMI-1, a core component of PRC1. I also identify SPAT-3A as a homolog of Ring1B, a partner protein of BMI-1 in the PRC1 core complex. Mig-32 and spat-3 mutants have some defects that overlap with those of mes mutants. However, unlike the mes mutants, mig-32 and spat-3 mutants are fertile, despite lacking apparent H2A ubiquitylation. Migration and axon guidance of specific neurons were defective in mig-32 and spat-3 mutants. Our data suggest that mig-32 and spat-3 encode core components of a PRC1-like complex in C. elegans."],"dc:format":["Electronic","application/pdf","born digital"],"dc:identifier":["https://hdl.handle.net/2152.5/358","754616644"],"dc:language":["en"],"dc:subject":["Caenorhabditis elegans","Carrier Proteins","Cell Movement"],"dc:title":["Discovery and Characterization of the Polycomb Repressive Complex 1 of C. Elegans"],"dc:type":["Thesis","Text","dissertation"]},"updated_at":"2026-07-24T05:52:29Z"}