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Eukaryotic Initiation Factor 3 Interactions with Structural Elements of Barley Yellow Dwarf Virus UTRs Reveal Details of a New Cap-Independent Translation Initiation Model.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Eukaryotic Initiation Factor 3 Interactions with Structural Elements of Barley Yellow Dwarf Virus UTRs Reveal Details of a New Cap-Independent Translation Initiation Model./
作者:	Powell, Paul.
面頁冊數:	1 online resource (107 pages)
附註:	Source: Dissertations Abstracts International, Volume: 83-05, Section: B.
Contained By:	Dissertations Abstracts International83-05B.
標題:	Biophysics. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=28771814click for full text (PQDT)
ISBN:	9798492776626

Eukaryotic Initiation Factor 3 Interactions with Structural Elements of Barley Yellow Dwarf Virus UTRs Reveal Details of a New Cap-Independent Translation Initiation Model.
Powell, Paul.

Eukaryotic Initiation Factor 3 Interactions with Structural Elements of Barley Yellow Dwarf Virus UTRs Reveal Details of a New Cap-Independent Translation Initiation Model. - 1 online resource (107 pages)

Source: Dissertations Abstracts International, Volume: 83-05, Section: B.

Thesis (Ph.D.)--City University of New York, 2022.

Includes bibliographical references

Barley Yellow Dwarf Virus (BYDV) is a positive strand RNA plant virus that translates without using a 5' 7-methylguanosine cap or a 3' poly-adenosine tail, features that are required for canonical mRNA translation. BYDV's non-canonical translation relies on RNA structures in the 5' and 3' untranslated regions (UTRs) to recruit eukaryotic initiation factors (eIFs) and ribosomes.BYDV's 3' translation enhancer (BTE) is a cruciform structure capable of recruiting the cap-binding complex eIF4F, the large scaffolding complex eIF3, and the 40S ribosomal subunit. Together eIF3, eIF4F, and BTE influence factor binding and 40S recruitment on the 5' UTR and play a key role in facilitating BYDV translation. This report focuses on eIF3 by providing and analyzing data that suggest novel eIF3 functionality and that expand upon the previous model of BYDV translation initiation to include eIF3 interactions with the UTRs and other factors. Specifically, we show that eIF3 can act as a dynamic, eIF4F-responsive bridge between specific loops found in both ofBYDV's UTRs. This report also provides insight into some of the broader applications of these discoveries by highlighting both parallels and distinctions between eIF-RNA interactions of BYDV and similar interactions found in other, non-canonically translating viral mRNAs and cellular mRNAs.

Electronic reproduction.
Ann Arbor, Mich. :
ProQuest,
2023

Mode of access: World Wide Web

ISBN: 9798492776626Subjects--Topical Terms:

518360
Biophysics.
Subjects--Index Terms:

Cap-independent translation InitiationIndex Terms--Genre/Form:

542853
Electronic books.

Eukaryotic Initiation Factor 3 Interactions with Structural Elements of Barley Yellow Dwarf Virus UTRs Reveal Details of a New Cap-Independent Translation Initiation Model.
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520 $a Barley Yellow Dwarf Virus (BYDV) is a positive strand RNA plant virus that translates without using a 5' 7-methylguanosine cap or a 3' poly-adenosine tail, features that are required for canonical mRNA translation. BYDV's non-canonical translation relies on RNA structures in the 5' and 3' untranslated regions (UTRs) to recruit eukaryotic initiation factors (eIFs) and ribosomes.BYDV's 3' translation enhancer (BTE) is a cruciform structure capable of recruiting the cap-binding complex eIF4F, the large scaffolding complex eIF3, and the 40S ribosomal subunit. Together eIF3, eIF4F, and BTE influence factor binding and 40S recruitment on the 5' UTR and play a key role in facilitating BYDV translation. This report focuses on eIF3 by providing and analyzing data that suggest novel eIF3 functionality and that expand upon the previous model of BYDV translation initiation to include eIF3 interactions with the UTRs and other factors. Specifically, we show that eIF3 can act as a dynamic, eIF4F-responsive bridge between specific loops found in both ofBYDV's UTRs. This report also provides insight into some of the broader applications of these discoveries by highlighting both parallels and distinctions between eIF-RNA interactions of BYDV and similar interactions found in other, non-canonically translating viral mRNAs and cellular mRNAs.
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