Barley Yellow Dwarf Virus (BYDV) lacks a 5’ (7-methyl guanosine) cap as well as a 3’poly A tail. Like many plant viruses, BYDV contains a cap independent translation element (CITE) in the 3’ untranslated region of the viral mRNA. BTE (Barley Yellow Dwarf Virus like cap-independent translation element) is one of the well characterized CITEs. BTE mediated translation primarily depends on eukaryotic initiation factor eIF4G. BTE binds to eIF4G; however, the details of BTE initiated translation are still unclear. Three eIF4G deletion mutants with different domain organization were used to investigate BTE interaction with eIF4G: eIF4G601-1196 is the eIF4G fragment containing amino acid residues from 601 to 1196, including binding domains for eIF4E, central eIF4A, eIF4B and the possible BTE binding region; eIF4G601-1488 is a longer fragment with one additional C-terminal eIF4A binding domain; eIF4G742-1196 is a shorter deletion mutant lacking the eIF4E binding sequence. eIF4G601-1196 binds BTE as efficiently as wild type eIF4G and supports translation. Translation initiation factor eIF4A and eIF4B with ATP (helicase complex) stimulate eIF4G601-1196 binding with BTE but not eIF4G601-1488, suggesting that the helicase complex function relies on the eIF4G central eIF4A binding domain, not the C-terminal eIF4A binding domain. This suggests that, similar to human eIF4G, the wheat eIF4A binding site may serve a regulatory role. eIF4E, upon binding with eIF4G mutants which have the eIF4E binding region, significantly increases the binding to BTE. This indicates that the smaller eIF4G mutant has a more flexible structure that can be positively influenced by eIF4E.
","abstract_html":"<p>Barley Yellow Dwarf Virus (BYDV) lacks a 5’ (7-methyl guanosine) cap as well as a 3’poly A tail. Like many plant viruses, BYDV contains a cap independent translation element (CITE) in the 3’ untranslated region of the viral mRNA. BTE (Barley Yellow Dwarf Virus like cap-independent translation element) is one of the well characterized CITEs. BTE mediated translation primarily depends on eukaryotic initiation factor eIF4G. BTE binds to eIF4G; however, the details of BTE initiated translation are still unclear. Three eIF4G deletion mutants with different domain organization were used to investigate BTE interaction with eIF4G: eIF4G601-1196 is the eIF4G fragment containing amino acid residues from 601 to 1196, including binding domains for eIF4E, central eIF4A, eIF4B and the possible BTE binding region; eIF4G601-1488 is a longer fragment with one additional C-terminal eIF4A binding domain; eIF4G742-1196 is a shorter deletion mutant lacking the eIF4E binding sequence. eIF4G601-1196 binds BTE as efficiently as wild type eIF4G and supports translation. Translation initiation factor eIF4A and eIF4B with ATP (helicase complex) stimulate eIF4G601-1196 binding with BTE but not eIF4G601-1488, suggesting that the helicase complex function relies on the eIF4G central eIF4A binding domain, not the C-terminal eIF4A binding domain. This suggests that, similar to human eIF4G, the wheat eIF4A binding site may serve a regulatory role. eIF4E, upon binding with eIF4G mutants which have the eIF4E binding region, significantly increases the binding to BTE. This indicates that the smaller eIF4G mutant has a more flexible structure that can be positively influenced by eIF4E.</p>","abstract_has_math":false,"creators":["Zhao, Pei"],"institution":"The Graduate School and University Center of The City University of New York","degree_name":"Doctor of Philosophy","degree_level":"Doctoral","degree_discipline":"Biochemistry","degree_department":null,"school":null,"contributors":[],"advisors":["Dixie J. Goss"],"committee_chairs":[],"committee_members":["Lesley Davenport","Frida E. Kleiman","Richard Magliozzo","Mandë Holford"],"year":2016,"date_issued":"2016-02-01T08:00:00Z","date_published":"2016-02-01T08:00:00Z","updated_at":"2026-07-24T01:59:21Z","subjects":["Biochemistry","Biophysics","Molecular Biology","Protein RNA Interaction","Virus RNA Translation"],"languages":[],"rights":[],"rights_urls":[],"identifier_entries":[]},"links":{"outbound_url":"https://academicworks.cuny.edu/gc_etds/732","outbound_label":"Repository record","outbound_source":"dc:identifier"},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor.advisor","label":"Advisor","values":["Dixie J. Goss"]},{"key":"dc:contributor.committeemember","label":"Committee Member","values":["Lesley Davenport","Frida E. Kleiman","Richard Magliozzo","Mandë Holford"]},{"key":"dc:creator","label":"Author","values":["Zhao, Pei"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date.available","label":"Dc Date Available","values":["2017-01-25T08:00:00Z"]},{"key":"thesis:degree_discipline","label":"Discipline","values":["Biochemistry"]},{"key":"thesis:degree_level","label":"Degree Level","values":["Doctoral"]},{"key":"thesis:degree_name","label":"Degree Name","values":["Doctor of Philosophy"]},{"key":"thesis:institution_name","label":"Thesis Institution Name","values":["The Graduate School and University Center of The City University of New York"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Biochemistry","Biophysics","Molecular Biology","Protein RNA Interaction","Virus RNA Translation"]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["https://academicworks.cuny.edu/gc_etds/732"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description.abstract","label":"Abstract","values":["Barley Yellow Dwarf Virus (BYDV) lacks a 5’ (7-methyl guanosine) cap as well as a 3’poly A tail. Like many plant viruses, BYDV contains a cap independent translation element (CITE) in the 3’ untranslated region of the viral mRNA. BTE (Barley Yellow Dwarf Virus like cap-independent translation element) is one of the well characterized CITEs. BTE mediated translation primarily depends on eukaryotic initiation factor eIF4G. BTE binds to eIF4G; however, the details of BTE initiated translation are still unclear. Three eIF4G deletion mutants with different domain organization were used to investigate BTE interaction with eIF4G: eIF4G601-1196 is the eIF4G fragment containing amino acid residues from 601 to 1196, including binding domains for eIF4E, central eIF4A, eIF4B and the possible BTE binding region; eIF4G601-1488 is a longer fragment with one additional C-terminal eIF4A binding domain; eIF4G742-1196 is a shorter deletion mutant lacking the eIF4E binding sequence. eIF4G601-1196 binds BTE as efficiently as wild type eIF4G and supports translation. Translation initiation factor eIF4A and eIF4B with ATP (helicase complex) stimulate eIF4G601-1196 binding with BTE but not eIF4G601-1488, suggesting that the helicase complex function relies on the eIF4G central eIF4A binding domain, not the C-terminal eIF4A binding domain. This suggests that, similar to human eIF4G, the wheat eIF4A binding site may serve a regulatory role. eIF4E, upon binding with eIF4G mutants which have the eIF4E binding region, significantly increases the binding to BTE. This indicates that the smaller eIF4G mutant has a more flexible structure that can be positively influenced by eIF4E.
"]},{"key":"dc:title","label":"Title","values":["The Interaction Between Eukaryotic Translation Initiation Factor eIF4G and 3’ Cap Independent Translation Element of Barley Yellow Dwarf Virus Is Affected by Multiple Initiation Factors"]}]}],"canonical_facts":{"dc:contributor.advisor":["Dixie J. Goss"],"dc:contributor.committeemember":["Lesley Davenport","Frida E. Kleiman","Richard Magliozzo","Mandë Holford"],"dc:creator":["Zhao, Pei"],"dc:date.available":["2017-01-25T08:00:00Z"],"dc:description.abstract":["Barley Yellow Dwarf Virus (BYDV) lacks a 5’ (7-methyl guanosine) cap as well as a 3’poly A tail. Like many plant viruses, BYDV contains a cap independent translation element (CITE) in the 3’ untranslated region of the viral mRNA. BTE (Barley Yellow Dwarf Virus like cap-independent translation element) is one of the well characterized CITEs. BTE mediated translation primarily depends on eukaryotic initiation factor eIF4G. BTE binds to eIF4G; however, the details of BTE initiated translation are still unclear. Three eIF4G deletion mutants with different domain organization were used to investigate BTE interaction with eIF4G: eIF4G601-1196 is the eIF4G fragment containing amino acid residues from 601 to 1196, including binding domains for eIF4E, central eIF4A, eIF4B and the possible BTE binding region; eIF4G601-1488 is a longer fragment with one additional C-terminal eIF4A binding domain; eIF4G742-1196 is a shorter deletion mutant lacking the eIF4E binding sequence. eIF4G601-1196 binds BTE as efficiently as wild type eIF4G and supports translation. Translation initiation factor eIF4A and eIF4B with ATP (helicase complex) stimulate eIF4G601-1196 binding with BTE but not eIF4G601-1488, suggesting that the helicase complex function relies on the eIF4G central eIF4A binding domain, not the C-terminal eIF4A binding domain. This suggests that, similar to human eIF4G, the wheat eIF4A binding site may serve a regulatory role. eIF4E, upon binding with eIF4G mutants which have the eIF4E binding region, significantly increases the binding to BTE. This indicates that the smaller eIF4G mutant has a more flexible structure that can be positively influenced by eIF4E.
"],"dc:identifier":["https://academicworks.cuny.edu/gc_etds/732"],"dc:subject":["Biochemistry","Biophysics","Molecular Biology","Protein RNA Interaction","Virus RNA Translation"],"dc:title":["The Interaction Between Eukaryotic Translation Initiation Factor eIF4G and 3’ Cap Independent Translation Element of Barley Yellow Dwarf Virus Is Affected by Multiple Initiation Factors"],"thesis:degree_discipline":["Biochemistry"],"thesis:degree_level":["Doctoral"],"thesis:degree_name":["Doctor of Philosophy"],"thesis:institution_name":["The Graduate School and University Center of The City University of New York"]},"updated_at":"2026-07-24T01:59:21Z"}