Search bioRxiv⌕ Search

bioRxiv · 10.1101/353078

Yeast Ded1 promotes 48S translation pre-initiation complex assembly in an mRNA-specific and eIF4F-dependent manner

Abstract

DEAD-box RNA helicase Dedl is thought to resolve secondary structures in mRNA 5'-untranslated regions (5'-UTRs) that impede 48S preinitiation complex (PIC) formation at the initiation codon. We reconstituted Ded1 acceleration of 48S PIC assembly on native mRNAs in a pure system, and recapitulated increased Ded1-dependence of mRNAs that are Ded1-hyperdependent in vivo. Stem-loop (SL) structures in 5'-UTRs of native and synthetic mRNAs increased the Ded1 requirement to overcome their intrinsically low rates of 48S PIC recruitment. Ded1 acceleration of 48S assembly was greater in the presence of eIF4F, and domains mediating one or more Ded1 interactions with eIF4G or helicase eIF4A were required for efficient recruitment of all mRNAs; however, the relative importance of particular Ded1 and eIF4G domains were distinct for each mRNA. Our results account for the Ded1 hyper-dependence of mRNAs with structure-prone 5'-UTRs, and implicate an eIF4E{middle dot}eIF4G{middle dot}eIF4A{middle dot}Ded1 complex in accelerating 48S PIC assembly on native mRNAs.

Source connections

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Gupta, N., Lorsch, J. R., Hinnebusch, A. G.. 2018-06-21. Yeast Ded1 promotes 48S translation pre-initiation complex assembly in an mRNA-specific and eIF4F-dependent manner. https://doi.org/10.1101/353078

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Structure of influenza D virus NS1 reveals a novel Zn-binding site and ssRNA-binding activity

Influenza D virus (IDV) is an emerging pathogen associated with bovine respiratory disease and has potential for zoonotic transmission. Although nonstructural protein 1 (NS1) is a major virulence factor in influenza A and B viruses, the structure and function of IDV NS1 remain poorly defined. Here, we determined crystal structures of the IDV NS1 N-terminal RNA-binding domain (NTD) and C-terminal effector domain (CTD). The NTD retains the conserved homodimeric six-helix fold, whereas the CTD adopts a distinct architecture containing a novel Zn2+-binding site. IDV NS1 CTD preferentially binds single-stranded RNA, and mutagenesis identified lysine and arginine residues critical for this activity. Single-residue substitutions disrupting either the Zn2+-binding site or RNA-binding interface prevented recovery of infectious recombinant IDV. These findings reveal distinct structural and functional features of IDV NS1 and establish the importance of CTD integrity for viral replication. Conservation of key CTD residues in influenza C virus NS1 suggests shared structural features that distinguish influenza C and D virus NS1 proteins from their influenza A and B counterparts.

biochemistry↗

Recognition of the centromere-binding protein Ndc10 by Scm3HJURP directs Cse4CENP-A deposition at native centromeres

Kinetochores connect centromeres to spindle microtubules, ensuring accurate chromosome segregation. Kinetochore assembly at centromeres depends on deposition of CENP-A, a histone H3 variant. Despite considerable progress, how CENP-A is specifically assembled on native centromeres remains an open question. Centromere-specific assembly of CENP-A occurs spontaneously in a cell-free extract system from the yeast Saccharomyces cerevisiae, but with low efficiency, suggesting that one or more factors are limiting. Here, we show Scm3HJURP, a specific chaperone for the centromeric histone Cse4CENP-A, is one such limiting component. The addition of a complex of Scm3, Cse4 and histone H4 strongly stimulates Cse4 assembly in a centromeric DNA sequence- and dose-dependent manner; in addition, improvements in both Cse4 and kinetochore assembly were more prominent in mitotic versus interphase (G1) extracts. Using the complemented cell-free reconstitution system, we show that distinct Scm3 interfaces with Cse4 and with the Ndc10 subunit of the yeast centromere DNA sequence-recognizing CBF3 complex are essential for centromere-specific Cse4 assembly and cell viability. Thus, recognition of Ndc10 directs Scm3-dependent and locus-specific centromeric histone deposition.

biochemistry↗

Heterogeneous primary nucleation determines Aβ42 fibrilstructure.

The current developments in the field of amyloid fibril structure determination has revealed multiple structures for peptides of identical sequence. This may reflect variations in sample environment or similar nucleation barriers for multiple folds. Here we investigate the influence of aggregating surface and during fibril formation from monomeric amyloid {beta} peptide (A{beta}42). The fibril structures formed in identical solutions in glass vials / bottles and PEGylated polystyrene 96-well plates display very different monomer fold within the fibrils. This is a clear indication of extremely slow homogeneous primary nucleation. Instead, heterogeneous primary nucleation at vessel walls or at the three-line interface between air, water and vessel wall dictate the outcome in each solution, where the initially formed structure is propagated through elongation and secondary nucleation. The results further imply that the conversion towards the thermodynamically stable fibril structure one is slow for A{beta}42.

biochemistry↗