The DEAD-Box Protein Ded1 Modulates Translation by the Formation and Resolution of an eIF4F-mRNA Complex

Hilliker, Angela K.; Gao, Zhaofeng; Jankowsky, Eckhard; Parker, Roy

doi:10.1016/j.molcel.2011.08.008

Cited by 219 publications

(364 citation statements)

References 37 publications

(67 reference statements)

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“…Ded1 binds the RNA3 motif at the C terminus of eIF4G1 (Hilliker et al 2011). While mutational inactivation of Ded1 inhibits translation initiation (Chuang et al 1997), its overexpression rescues eIF4E ts alleles (de la Cruz et al 1997).…”

Section: Mrna Recruitment Of the 43s Picmentioning

confidence: 99%

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

2016

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In this review, we provide an overview of protein synthesis in the yeast Saccharomyces cerevisiae. The mechanism of protein synthesis is well conserved between yeast and other eukaryotes, and molecular genetic studies in budding yeast have provided critical insights into the fundamental process of translation as well as its regulation. The review focuses on the initiation and elongation phases of protein synthesis with descriptions of the roles of translation initiation and elongation factors that assist the ribosome in binding the messenger RNA (mRNA), selecting the start codon, and synthesizing the polypeptide. We also examine mechanisms of translational control highlighting the mRNA cap-binding proteins and the regulation of GCN4 and CPA1 mRNAs.

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Section: Mrna Recruitment Of the 43s Picmentioning

confidence: 99%

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

2016

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“…One of these is additional eIF4A for which one might imagine a mechanism (60). The others represent different RNA helicases including DDX3, DDX41, DHX9, and DHX29 (61)(62)(63)(64). These alternate possibilities are extensively reviewed in Parsyan et al (65).…”

Section: Other Complicationsmentioning

confidence: 99%

eIF4F: A Retrospective

Merrick

2015

Journal of Biological Chemistry

148

156

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The original purification of the heterotrimeric eIF4F was published over 30 years ago (Grifo, J. A., Tahara, S. M., Morgan, M. A., Shatkin, A. J., and Merrick, W. C. (1983) J. Biol. Chem. 258, 5804 -5810). Since that time, numerous studies have been performed with the three proteins specifically required for the translation initiation of natural mRNAs, eIF4A, eIF4B, and eIF4F. These have involved enzymatic and structural studies of the proteins and a number of site-directed mutagenesis studies. The regulation of translation exhibited through the mammalian target of rapamycin (mTOR) pathway is predominately seen as the phosphorylation of 4E-BP, an inhibitor of protein synthesis that functions by binding to the cap binding subunit of eIF4F (eIF4E). A hypothesis that requires the disassembly of eIF4F during translation initiation to yield free subunits (eIF4A, eIF4E, and eIF4G) is presented. The Biology of eIF4FThe initial findings in the study of natural mRNA translation reflected the newly discovered m 7 G cap at the 5Ј end of eukaryotic mRNAs (2). mRNAs lacking this structure were translated with less efficiency than mRNAs that contained this structure (3). This unique structure allowed for specific assays or purifications, many established in the laboratory of Dr. Aaron Shatkin with assists from his colleagues. Two of note were the use of m 7 G-Sepharose for affinity purification (4, 5) and the crosslinking of periodate-oxidized mRNAs to proteins (6).The initial application of these methodologies identified two different molecular weight species (about 25,000 and at least 200,000), although the high molecular weight protein contained the small molecular weight component, now known as eIF4E (7). Given the size of several other known translation factors, the question was whether these contained the small molecular weight subunit (notably eIF3 and eIF4B) (8 -11). Ultimate purification of eIF4F indicated that neither of these were correct but that eIF4F would form stable complexes with either, thus being consistent with the eIF4E component tracking with them. At the same time, it was recognized that the 46,000 molecular weight subunit of eIF4F was eIF4A. By physical analysis, eIF4F was a heterotrimeric complex of eIF4A, eIF4E, and eIF4G (1).The next studies were to attempt to identify the functions of the various proteins required specifically for natural mRNA translation (eIF4A, eIF4B, and eIF4F). The characteristics of these three proteins were very different. In the absence of ATP, binding to RNA could only be well demonstrated with eIF4F (Table 1). eIF4A and eIF4F could hydrolyze ATP in the presence of single-stranded RNA, and eIF4B would enhance both of these activities (12). In terms of mechanism, the coupling of the binding of ATP and RNA was realized in recognizing that eIF4A or eIF4F had the ability to unwind duplex RNA. As noted in Table 1, the "strength" of the helicase activity was greater with eIF4F (14).As the ability to determine amino acid sequence from RNA sequence advanced, it was found that there...

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“…55,[58][59][60] In this process, these enzymes are delivered to the 5 0 end of the mRNA either by binding to a specific post-transcriptional element (PCE) in the case of RHA, as part of the eIF4F complex for Ded1, or together with the 40S ribosomal subunit for DHX29. [60][61][62] In the case of HIV-1, BorisLawrie and colleagues have addressed the role of DHX9/RHA in viral translation and they showed that the latter was required to promote RNP remodeling through the 5 0 UTR to ensure ribosome progression. 61 This occurs by the initial binding of RHA to the PCE element found in the HIV-1 5…”

Section: The Need For Additional Helicases In Hiv-1 Translationmentioning

confidence: 99%

Translation initiation of the HIV-1 mRNA

Ohlmann¹,

Mengardi²,

López-Lastra³

2014

translation

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Translation initiation of the full-length mRNA of the human immunodeficiency virus can occur via several different mechanisms to maintain production of viral structural proteins throughout the replication cycle. HIV-1 viral protein synthesis can occur by the use of both a capdependant and IRES-driven mechanism depending on the physiological conditions of the cell and the status of the ongoing infection. For both of these mechanisms there is a need for several viral and cellular co-factors for optimal translation of the viral mRNA. In this review we will describe the mechanism used by the full-length mRNA to initiate translation highlighting the role of co-factors within this process. A particular emphasis will be given to the role of the DDX3 RNA helicase in HIV-1 mRNA translation initiation.

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The DEAD-Box Protein Ded1 Modulates Translation by the Formation and Resolution of an eIF4F-mRNA Complex

Cited by 219 publications

References 37 publications

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae

eIF4F: A Retrospective

Translation initiation of the HIV-1 mRNA

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