{"id":{"repo_id":"tdl","oai_identifier":"oai:tdl-ir.tdl.org:2152/77431"},"canonical_url":"https://search.dev.ndltd.org/etd/tdl/oai:tdl-ir.tdl.org:2152/77431","repository":{"repo_id":"tdl","name":"Texas Digital Library","base_url":"https://tdl-ir.tdl.org/server/oai/request"},"display":{"title":"TB-RBP protein : sitting at the crossroads of sex and disease","abstract":"The goal of the project was to determine the crystal structure of TB-RBP (Testis/Brain RNA binding protein) in complex with single stranded DNA. The secondary goal was to determine the crystal structure of TB-RBP in complex with Trax (translin associated factor X). Functions of TB-RBP is to suppresses translation of testicular mRNAs (Ex: protamines 1 and 2), attach mRNAs to microtubules for cellular transport of brain mRNAs and to mediate both temporal and spatial expression of certain mRNAs in male germ cell development. Translin is the human homologue of mouse TB-RBP. Translin is proposed to function as a DNA-binding protein that binds to specific DNA sequences at breakpoint junctions of chromosomal translocations of lymphoid malignancies. Trax, structural homologue of TB-RBP, has already been shown to interact with the single stranded DNA -/RNA - binding protein TB-RBP. Co-crystallization of TB-RBP/DNA complex may give us insight into sequence recognition at the breakpoint junctions of chromosomal translocation. Co-crystallization of a Trax/TB-RBP complex may provide insight into regulation of silenced mRNA.","abstract_html":"The goal of the project was to determine the crystal structure of TB-RBP (Testis/Brain RNA binding protein) in complex with single stranded DNA. The secondary goal was to determine the crystal structure of TB-RBP in complex with Trax (translin associated factor X). Functions of TB-RBP is to suppresses translation of testicular mRNAs (Ex: protamines 1 and 2), attach mRNAs to microtubules for cellular transport of brain mRNAs and to mediate both temporal and spatial expression of certain mRNAs in male germ cell development. Translin is the human homologue of mouse TB-RBP. Translin is proposed to function as a DNA-binding protein that binds to specific DNA sequences at breakpoint junctions of chromosomal translocations of lymphoid malignancies. Trax, structural homologue of TB-RBP, has already been shown to interact with the single stranded DNA -/RNA - binding protein TB-RBP. Co-crystallization of TB-RBP/DNA complex may give us insight into sequence recognition at the breakpoint junctions of chromosomal translocation. Co-crystallization of a Trax/TB-RBP complex may provide insight into regulation of silenced mRNA.","abstract_has_math":false,"creators":["Hoe, Warren"],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Robertus, Jon D."],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2004,"date_issued":"2004-08-16","date_published":"2004-08-16","updated_at":"2026-07-27T21:19:08Z","subjects":["TB-RBP","Chromosomal translocation","Translin"],"languages":["eng"],"rights":["Restricted","Copyright © is held by the author. Presentation of this material on the Libraries' web site by University Libraries, The University of Texas at Austin was made possible under a limited license grant from the author who has retained all copyrights in the works."],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["http://dx.doi.org/10.26153/tsw/4520"],"render_values":[{"text":"http://dx.doi.org/10.26153/tsw/4520","href":"http://dx.doi.org/10.26153/tsw/4520","code":true}]}]},"links":{"outbound_url":"https://hdl.handle.net/2152/77431","outbound_label":"Handle","outbound_source":"dc:identifier.uri"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Robertus, Jon D."]},{"key":"dc:creator","label":"Author","values":["Hoe, Warren"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.accessioned","label":"Dc Date Accessioned","values":["2019-10-24T22:21:49Z","2026-03-24T19:36:13Z"]},{"key":"dc:date.available","label":"Dc Date Available","values":["2019-10-24T22:21:49Z"]},{"key":"dc:date.issued","label":"Date","values":["2004-08-16"]},{"key":"dc:relation","label":"Dc Relation","values":["UT Electronic Theses and Dissertations"]},{"key":"dc:type","label":"Dc Type","values":["Thesis"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["TB-RBP","Chromosomal translocation","Translin"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["Restricted","Copyright © is held by the author. Presentation of this material on the Libraries' web site by University Libraries, The University of Texas at Austin was made possible under a limited license grant from the author who has retained all copyrights in the works."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://hdl.handle.net/2152/77431","http://dx.doi.org/10.26153/tsw/4520"]},{"key":"dc:identifier.uri","label":"Identifier URI","values":["https://hdl.handle.net/2152/77431"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["The goal of the project was to determine the crystal structure of TB-RBP (Testis/Brain RNA binding protein) in complex with single stranded DNA. The secondary goal was to determine the crystal structure of TB-RBP in complex with Trax (translin associated factor X). Functions of TB-RBP is to suppresses translation of testicular mRNAs (Ex: protamines 1 and 2), attach mRNAs to microtubules for cellular transport of brain mRNAs and to mediate both temporal and spatial expression of certain mRNAs in male germ cell development. Translin is the human homologue of mouse TB-RBP. Translin is proposed to function as a DNA-binding protein that binds to specific DNA sequences at breakpoint junctions of chromosomal translocations of lymphoid malignancies. Trax, structural homologue of TB-RBP, has already been shown to interact with the single stranded DNA -/RNA - binding protein TB-RBP. Co-crystallization of TB-RBP/DNA complex may give us insight into sequence recognition at the breakpoint junctions of chromosomal translocation. Co-crystallization of a Trax/TB-RBP complex may provide insight into regulation of silenced mRNA."]},{"key":"dc:title","label":"Title","values":["TB-RBP protein : sitting at the crossroads of sex and disease"]}]}],"canonical_facts":{"dc:contributor":["Robertus, Jon D."],"dc:creator":["Hoe, Warren"],"dc:date.accessioned":["2019-10-24T22:21:49Z","2026-03-24T19:36:13Z"],"dc:date.available":["2019-10-24T22:21:49Z"],"dc:date.issued":["2004-08-16"],"dc:description.abstract":["The goal of the project was to determine the crystal structure of TB-RBP (Testis/Brain RNA binding protein) in complex with single stranded DNA. The secondary goal was to determine the crystal structure of TB-RBP in complex with Trax (translin associated factor X). Functions of TB-RBP is to suppresses translation of testicular mRNAs (Ex: protamines 1 and 2), attach mRNAs to microtubules for cellular transport of brain mRNAs and to mediate both temporal and spatial expression of certain mRNAs in male germ cell development. Translin is the human homologue of mouse TB-RBP. Translin is proposed to function as a DNA-binding protein that binds to specific DNA sequences at breakpoint junctions of chromosomal translocations of lymphoid malignancies. Trax, structural homologue of TB-RBP, has already been shown to interact with the single stranded DNA -/RNA - binding protein TB-RBP. Co-crystallization of TB-RBP/DNA complex may give us insight into sequence recognition at the breakpoint junctions of chromosomal translocation. Co-crystallization of a Trax/TB-RBP complex may provide insight into regulation of silenced mRNA."],"dc:identifier":["https://hdl.handle.net/2152/77431","http://dx.doi.org/10.26153/tsw/4520"],"dc:identifier.uri":["https://hdl.handle.net/2152/77431"],"dc:language":["eng"],"dc:relation":["UT Electronic Theses and Dissertations"],"dc:rights":["Restricted","Copyright © is held by the author. Presentation of this material on the Libraries' web site by University Libraries, The University of Texas at Austin was made possible under a limited license grant from the author who has retained all copyrights in the works."],"dc:subject":["TB-RBP","Chromosomal translocation","Translin"],"dc:title":["TB-RBP protein : sitting at the crossroads of sex and disease"],"dc:type":["Thesis"]},"updated_at":"2026-07-27T21:19:08Z"}