SUI1/p16 Is Required for the Activity of Eukaryotic Translation Initiation Factor 3 in <i>Saccharomyces cerevisiae</i>

Naranda, Tatjana; Macmillan, S. E.; Donahue, Thomas F.

doi:10.1128/mcb.16.5.2307

Cited by 73 publications

(128 citation statements)

References 20 publications

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“…This is in agreement with previous studies also showing that isolated full-length eIF3b subunit does not bind RNA in vitro (7,26). Additionally, the yeast homologue, which shares 26% identity and 50% similarity with human eIF3b, also fails to bind RNA in vitro (27). Within 48 S complexes (28) or in binary internal ribosome entry site RNA⅐eIF3 complexes (29), RNA binding of mammalian full-length eIF3b has been evidenced by cross-linking to mRNA, indicating that eIF3b can interact with RNA only in the context of eIF3 complexes.…”

Section: Eif3b-rrm Resembles Noncanonical Rrms Of the U2afsupporting

confidence: 82%

Structure of eIF3b RNA Recognition Motif and Its Interaction with eIF3j

ElAntak¹,

Tzakos²,

Locker³

et al. 2007

Journal of Biological Chemistry

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Mammalian eIF3 is a 700-kDa multiprotein complex essential for initiation of protein synthesis in eukaryotic cells. It consists of 13 subunits (eIF3a to -m), among which eIF3b serves as a major scaffolding protein. Here we report the solution structure of the N-terminal RNA recognition motif of human eIF3b (eIF3b-RRM) determined by NMR spectroscopy. The structure reveals a noncanonical RRM with a negatively charged surface in the ␤-sheet area contradictory with potential RNA binding activity. Instead, eIF3j, which is required for stable 40 S ribosome binding of the eIF3 complex, specifically binds to the rear ␣-helices of the eIF3b-RRM, opposite to its ␤-sheet surface. Moreover, we identify that an N-terminal 69-amino acid peptide of eIF3j is sufficient for binding to eIF3b-RRM and that this interaction is essential for eIF3b-RRM recruitment to the 40 S ribosomal subunit. Our results provide the first structure of an important subdomain of a core eIF3 subunit and detailed insights into protein-protein interactions between two eIF3 subunits required for stable eIF3 recruitment to the 40 S subunit.

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Section: Eif3b-rrm Resembles Noncanonical Rrms Of the U2afsupporting

confidence: 82%

Structure of eIF3b RNA Recognition Motif and Its Interaction with eIF3j

ElAntak¹,

Tzakos²,

Locker³

et al. 2007

Journal of Biological Chemistry

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“…Sequencing of the isolated plasmids revealed that the ts phenotype of three of the four strains was suppressed by plasmids containing the SUI1 gene, which encodes eukaryotic translation initiation factor 1 (eIF1). 24) As expected, the His + phenotype of these strains was also suppressed by the same plasmid. Furthermore, the endogenous SUI1 gene of these three strains contained a mutation within the open reading frame (ORF) (A63T, A63V, or G66S; Table 1), indicating that their His + phenotype was caused by these mutations.…”

Section: Resultssupporting

confidence: 50%

“…30) As mentioned above, SUI1 and SUI3 encode the translation initiation factors eIF1 and eIF2β, respectively, which are involved in the recognition of initiation codons on mRNAs. [24][25][26] Despite the current lack of direct evidence, we speculate that the mutation of these factors might cause the His + phenotype by promoting translation of the His3 protein from codons, other than the AUG located within the region near the promoter. Given that mutations in the specific genes mentioned above were repeatedly isolated (note that more sui1 and sui3 mutants were isolated, but excluded from further analyses by testing whether plasmids containing the SUI1 or SUI3 gene suppressed the ts and His + phenotypes of the mutant strains), the genetic screen appeared to be saturated.…”

Section: Resultsmentioning

confidence: 99%

Both HMG boxes in Hmo1 are essential for DNA binding in vitro and in vivo

Higashino

Shiwa

Yoshikawa

et al. 2015

Bioscience, Biotechnology, and Biochemistry

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Hmo1, a member of the high mobility group B family proteins in Saccharomyces cerevisiae, associates with the promoters of ribosomal protein genes (RPGs) to direct accurate transcriptional initiation. Here, to identify factors involved in the binding of Hmo1 to its targets and the mechanism of Hmo1-dependent transcriptional initiation, we developed a novel reporter system using the promoter of the RPG RPS5. A genetic screen did not identify any factors that influence Hmo1 binding, but did identify a number of mutations in Hmo1 that impair its DNA binding activity in vivo and in vitro. These results suggest that Hmo1 binds to its target promoters autonomously without any aid of additional factors. Furthermore, characterization of Hmo1 mutants showed that the box A domain plays a pivotal role in DNA binding and may be required for the recognition of structural properties of target promoters that occur in native chromatin.

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“…25), GCD10p (15,26), eIF5 (15,22), and Sui1p (eIF1; Ref. 27), that are not present in the mammalian complex (11,24). TIF31 is not an essential gene in S. cerevisiae, and the role of the TIF31 protein in the eIF3 complex is not clear (25).…”

Section: Eukaryotic Initiation Factor 3 (Eif3)mentioning

confidence: 99%

Plant Initiation Factor 3 Subunit Composition Resembles Mammalian Initiation Factor 3 and Has a Novel Subunit

Burks

Bezerra

Le³

et al. 2001

Journal of Biological Chemistry

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Eukaryotic initiation factor 3 (eIF3) is a multisubunit complex that is required for binding of mRNA to 40 S ribosomal subunits, stabilization of ternary complex binding to 40 S subunits, and dissociation of 40 and 60 S subunits. These functions and the complex nature of eIF3 suggest multiple interactions with many components of the translational machinery. Recently, the subunits of mammalian and Saccharomyces cerevisiae eIF3 were identified, and substantial differences in the subunit composition of mammalian and S. cerevisiae were observed. Mammalian eIF3 consists of 11 nonidentical subunits, whereas S. cerevisiae eIF3 consists of up to eight nonidentical subunits. Only five of the subunits of mammalian and S. cerevisiae are shared in common, and these five subunits comprise a "core" complex in S. cerevisiae. eIF3 from wheat consists of at least 10 subunits, but their relationship to either the mammalian or S. cerevisiae eIF3 subunits is unknown. Peptide sequences derived from purified wheat eIF3 subunits were used to correlate each subunit with mammalian and/or S. cerevisiae subunits. The peptide sequences were also used to identify Arabidopsis thaliana cDNAs for each of the eIF3 subunits. We report seven new cDNAs for A. thaliana eIF3 subunits. A. thaliana eIF3 was purified and characterized to confirm that the subunit composition and activity of wheat and A. thaliana eIF3 were similar. We report that plant eIF3 closely resembles the subunit composition of mammalian eIF3, having 10 out of 11 subunits in common. Further, we find a novel subunit in the plant eIF3 complex not present in either mammalian or S. cerevisiae eIF3. These results suggest that plant and mammalian eIF3 evolved similarly, whereas S. cerevisiae has diverged. Eukaryotic initiation factor 3 (eIF3)1 is the most complex and least understood of the protein synthesis initiation factors. eIF3 has been purified from wheat germ (1-3), HeLa cells (4, 5), rabbit reticulocytes (6 -12), and Saccharomyces cerevisiae (13)(14)(15)(16). Depending upon the organism and method of purification, there are 6 -11 nonidentical subunits present in functional eIF3 complexes that have been isolated and characterized. Recently, the subunits from the human and S. cerevisiae eIF3 complex have all been identified and sequenced. Surprisingly, there are substantial differences in the subunit composition between mammalian and S. cerevisiae eIF3 complexes. The mammalian eIF3 complex composition varies depending upon the method of purification (6, 7, 9 -12); however, the mammalian eIF3 complex appears to contain 11 subunits, p170 (17), p116 (18), p110 (19), p66 (20), p44 (21, 22), p48 (23), p47 (20), p40 (20), p36 (19), p35 (21) and p28.2 The S. cerevisiae eIF3 complex was determined to consist of a core complex of five subunits, Tif32p, Prt1p, Nip1p, Tif35p,24) that correspond to mammalian subunits p170, p116, p110, p44, and p36, respectively (see Table II). There are other proteins associated with the S. cerevisiae eIF3 complex, TIF31p (Clu1p; Ref. 25), GCD10p (15,26), eI...

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SUI1/p16 Is Required for the Activity of Eukaryotic Translation Initiation Factor 3 in Saccharomyces cerevisiae

Cited by 73 publications

References 20 publications

Structure of eIF3b RNA Recognition Motif and Its Interaction with eIF3j

Structure of eIF3b RNA Recognition Motif and Its Interaction with eIF3j

Both HMG boxes in Hmo1 are essential for DNA binding in vitro and in vivo

Plant Initiation Factor 3 Subunit Composition Resembles Mammalian Initiation Factor 3 and Has a Novel Subunit

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