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1 eIF5B did not influence factor release in the absence of
2 eIF5B has also been shown to promote the translation of
3 eIF5B promotes 60S ribosome subunit joining and pre-40S
4 eIF5B, the eukaryotic ortholog of IF2, is a GTPase that
5 on initiation factor 5B/initiation factor 2 (eIF5B/IF2) impair yeast cell growth due to failure to di
7 eukaryotic translation initiation factor 5B (eIF5B) binds to the factor eIF1A and catalyzes ribosomal
8 eukaryotic translation initiation factor 5B (eIF5B) from Saccharomyces cerevisiae impaired cell growt
11 initiation, eukaryotic initiation factor 5B (eIF5B) promotes the 60S subunit joining with the 40S ini
12 eukaryotic translation initiation factor 5B (eIF5B), the eukaryotic ortholog of bacterial initiation
15 wo protein factors, IF1 (a/eIF1A) and IF2 (a/eIF5B), are conserved among all three kingdoms of life a
17 cate that the interactions between eIF1A and eIF5B are being continuously rearranged during translati
19 e binding between the C termini of eIF1A and eIF5B has implications for eukaryote-specific mechanisms
22 intramolecular interactions within eIF1A and eIF5B interfere with one or both eIF5B/eIF1A contact int
23 e evolutionarily conserved factors eIF1A and eIF5B plays an important role in translation initiation,
25 s is more complex and accordingly, eIF1A and eIF5B seem to have acquired a number of new functions wh
27 ation, and in vitro binding assays eIF1A and eIF5B were found to interact directly, and the eIF1A bin
31 of 48S complexes assembled by eIF2/eIF3- and eIF5B/eIF3-mediated mechanisms to eIF1-induced destabili
32 S complexes assembled both by eIF2/eIF3- and eIF5B/eIF3-mediated Met-tRNA(iMet) recruitment were dest
35 c suppressors restored yeast cell growth and eIF5B nucleotide-binding, GTP hydrolysis, and subunit jo
36 irs elongation factor function, the rRNA and eIF5B suppressor mutations provide in vivo evidence supp
38 ciation of eIF2*GDP from initiator tRNA, and eIF5B is then required to stabilize the initiator tRNA i
39 s an antagonist of G0 and G0-like states, as eIF5B depletion reduces maturation of G0-like, immature
42 IF1A: (i) a second binding interface between eIF5B and eIF1A; (ii) a dynamic intramolecular interacti
43 rolysis by eIF5B enables the release of both eIF5B and eIF1A, and the ribosome enters the elongation
44 n eIF1A and eIF5B interfere with one or both eIF5B/eIF1A contact interfaces, but are disrupted on the
45 Following subunit joining, GTP hydrolysis by eIF5B alters the conformation of the final initiation co
46 ing 80S complex formation, GTP hydrolysis by eIF5B enables the release of both eIF5B and eIF1A, and t
47 sent a kinetic analysis of GTP hydrolysis by eIF5B in the context of the translation initiation pathw
48 A(i)(Met) binding and that GTP hydrolysis by eIF5B is a checkpoint monitoring 80S ribosome assembly i
49 dicate that stimulation of GTP hydrolysis by eIF5B requires the completion of early steps in translat
53 man eIF5B GTP-binding domain to Asn converts eIF5B to an XTPase and introduces an XTP requirement for
57 These findings support the idea that eIF1A-eIF5B association is instrumental in releasing eIF1A fro
59 show that the cleavage of initiation factor eIF5B during enteroviral infection, along with the viral
60 Eukaryotic translation initiation factor eIF5B is a ribosome-dependent GTPase that is responsible
61 Eukaryotic translation initiation factor eIF5B is a ribosome-dependent GTPase that mediates displ
65 on-like cycle whereby the translation factor eIF5B, a GTPase, promotes joining of large (60S) subunit
68 guanine nucleotides dissociated rapidly from eIF5B (k-1mant-GTP approximately 22-28 s-1, k-1mant-GDP
69 We show that either the absence of Fun12p (eIF5B), or a defect in eIF5, proteins involved in 60S ri
73 Mutation of the conserved Asp-759 in human eIF5B GTP-binding domain to Asn converts eIF5B to an XTP
75 universal translation initiation factor IF2/eIF5B have been determined in three states: free enzyme,
78 st five residues in eIF1A (eIF1A-5A) impairs eIF5B binding to eIF1A in cell extracts and to 40S compl
79 structure reveals conformational changes in eIF5B, initiator tRNA, and the ribosome that provide ins
80 itical requirement for this Switch II Gly in eIF5B, intragenic suppressors were identified in the Swi
82 The increased eIF5B levels lead to increased eIF5B complexes with tRNA-Met(i) upon serum starvation o
83 bosomal subunit binding to eIF3, and inhibit eIF5B-dependent steps downstream of start codon recognit
84 we report three novel interactions involving eIF5B and eIF1A: (i) a second binding interface between
95 cleavage data also indicate that binding of eIF5B might induce conformational changes in both subuni
96 ropose that eIF1A facilitates the binding of eIF5B to the 40S subunit to promote subunit joining.
101 nit and intragenic mutations in domain II of eIF5B suppress the toxic effects associated with express
110 us of eIF1A interacts with the C-terminus of eIF5B, a factor that stimulates 40S-60S subunit joining,
112 gest a rapid spontaneous GTP/GDP exchange on eIF5B and are therefore consistent with it having no req
115 60S subunits to form 80S ribosomes requires eIF5B, which has an essential ribosome-dependent GTPase
120 7 microM) than for mant-GTP, indicating that eIF5B tolerates modifications of the triphosphate moiety
124 e site, impairing nucleotide binding and the eIF5B domain movements associated with GTP binding.
127 py (cryo-EM) to determine a structure of the eIF5B initiation complex to 6.6 angstrom resolution from
128 ic effects associated with expression of the eIF5B-H480I GTPase-deficient mutant in yeast by lowering
130 he kinetics of guanine nucleotide binding to eIF5B by a fluorescent stopped-flow technique using fluo
132 e resulting 80 S initiation complex triggers eIF5B to hydrolyze its bound GTP, reducing the affinity
134 interaction of the C terminus of eIF1A with eIF5B promotes ribosomal subunit joining and possibly pr
135 ning through its C-terminal interaction with eIF5B, and eIF1A release from the initiating ribosome, w
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