![](/client/images/blank.gif)
Eylem Seç
![Mapping Protein- Protein Interactions Between Translation Initiation Factors in Giardia lamblia Using Yeast Two-Hybrid Assay için kapak resmi Mapping Protein- Protein Interactions Between Translation Initiation Factors in Giardia lamblia Using Yeast Two-Hybrid Assay için kapak resmi](/client/assets/d79c3e4af2b6d196/ctx/images/no_image.png)
Mapping Protein- Protein Interactions Between Translation Initiation Factors in Giardia lamblia Using Yeast Two-Hybrid Assay
Başlık:
Mapping Protein- Protein Interactions Between Translation Initiation Factors in Giardia lamblia Using Yeast Two-Hybrid Assay
Yazar:
Adedoja, Adebanjo Najeem, author.
ISBN:
9780355966367
Yazar Ek Girişi:
Fiziksel Tanımlama:
1 electronic resource (87 pages)
Genel Not:
Source: Masters Abstracts International, Volume: 57-06M(E).
Advisors: Srinivas Garlapati Committee members: Ann Findley; Allison Wiedemeier.
Özet:
Cap binding protein eIF4E is an important factor for translation initiation and regulation in eukaryotic cells. It interacts with the 5'cap structure of mRNA and eIF4G which also serves as an important binding protein for other translation initiation factors and recruits the 43S pre-initiation complex to mRNA. Diverged homologs of eIF4E have been identified in Giardia, but the organism lacks a functional homolog of eIF4G. This raises a fundamental question of how the 43S pre-initiation complex is recruited to the 5' end of Giardia mRNA. Giardia is an early and deep branching eukaryote during evolution and as such, deviates from the typical eukaryotic profile. With short mRNA 5' UTRs and a lack of eIF4G, it is believed that the pre-initiation complex is recruited directly to the start codon without a scanning process. Using a yeast-two hybrid assay, GleIF4E2 and other initiation proteins in Giardia were tested for binary protein-protein interactions (PPIs). The results of this study showed that the cap binding protein eIF4E2 can interact with GleIF2beta. This observation was significant because it directly links the 5'UTR to the pre-initiation complex. Given the proximity of GleIF4E2 to the initiation codon, the results indicated that without an eIF4G homolog, ribosomes can be recruited to the mRNA without scanning. The results also indicated that other proteins may play non-canonical roles in ribosome recruitment. Surprisingly, an interaction was also observed for GleIF4A, an mRNA helicase, and GleIF3i, a subunit of a larger protein involved in several aspects of translation initiation. Future studies of these PPIs will be essential for further understanding the molecular basis of translation initiation in Giardia..
Notlar:
School code: 1352
Konu Başlığı:
Tüzel Kişi Ek Girişi:
Mevcut:*
Yer Numarası | Demirbaş Numarası | Shelf Location | Lokasyon / Statüsü / İade Tarihi |
---|---|---|---|
XX(691551.1) | 691551-1001 | Proquest E-Tez Koleksiyonu | Arıyor... |
On Order
Liste seç
Bunu varsayılan liste yap.
Öğeler başarıyla eklendi
Öğeler eklenirken hata oldu. Lütfen tekrar deneyiniz.
:
Select An Item
Data usage warning: You will receive one text message for each title you selected.
Standard text messaging rates apply.