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SUI2 in Saccharomyces cerevisiae (S288c; ORF YJR007W) encodes the α subunit of eukaryotic translation initiation factor 2 (eIF2α), a core component of the heterotrimeric eIF2 complex (eIF2α/Sui2, eIF2β/Sui3, eIF2γ/Gcd11). This matches the UniProt description for P20459 (eukaryotic translation initiation factor 2 subunit alpha). (dever2016mechanismandregulation pages 6-7)
In eukaryotic translation initiation, eIF2 binds GTP and initiator Met-tRNAi(^Met) to form the ternary complex (TC), which is required to deliver initiator tRNA to the 40S ribosomal subunit and assemble the 43S/48S preinitiation complex (PIC). In yeast, this TC-dependent step is a central determinant of initiation rate and start-site selection. (dever2016mechanismandregulation pages 6-7)
After start-codon recognition, eIF2 hydrolyzes GTP and leaves the ribosome in a GDP-bound state. Reactivation requires the guanine nucleotide exchange factor eIF2B, which catalyzes GDP→GTP exchange on eIF2. This recycling is essential for continued rounds of initiation. (adomavicius2019thestructuralbasis pages 1-2)
A conserved translational-control mechanism in yeast is phosphorylation of eIF2α at Ser51 by the kinase Gcn2. This single-site phosphorylation changes eIF2 from an eIF2B substrate into an inhibitor of eIF2B, lowering eIF2-GTP and TC abundance and thereby decreasing general translation initiation. (dever2016mechanismandregulation pages 6-7, cherkasova2003translationalcontrolby pages 1-2, dever2016mechanismandregulation pages 27-28)
Beyond TC delivery, eIF2α contributes directly to start-codon selection fidelity during scanning. A high-quality yeast genetic/biochemical study built on cryo-EM PIC models shows that specific eIF2α residues contact rRNA and influence open/closed PIC conformations during scanning and AUG recognition. (thakur2020eif2αinteractionswith pages 12-13)
Key interaction concepts supported by the yeast PIC model:
- The unstructured N-terminal tail (NTT) of eIF2α interacts with eIF1 to stabilize the open/scanning PIC; upon AUG recognition, rearrangements disrupt this interaction and alter eIF2α contacts (e.g., with eIF5 domains), contributing to commitment to initiation. (thakur2020eif2αinteractionswith pages 2-2)
- Residue R53 of eIF2α contacts rRNA helix 23 in both open and closed py48S PIC states; an eIF2α mutation that reduces TC loading can derepress GCN4 translation even in gcn2Δ backgrounds by allowing bypass of inhibitory uORFs (mechanistic coupling of TC loading kinetics and uORF-controlled reinitiation). (thakur2020eif2αinteractionswith pages 12-13)
A yeast-focused synthesis of translation mechanisms describes eIF2α as composed of three domains: an N-terminal OB-fold, a central α-helical domain, and a C-terminal α/β domain that contacts eIF2γ. The regulatory Ser51 is located in a mobile loop within the OB-fold domain. (dever2016mechanismandregulation pages 6-7)
In budding yeast, amino acid limitation increases deacylated (uncharged) tRNAs, which activate Gcn2 (facilitated by Gcn1/Gcn20), causing Ser51 phosphorylation of eIF2α. This reduces TC abundance and globally represses initiation, while enabling selective translation of stress-response transcripts—classically GCN4, whose uORF architecture makes its translation inversely related to TC availability. (dever2016mechanismandregulation pages 27-28, romero2020globaltranslationalrepression pages 1-2)
A mechanistic description of the uORF-based control emphasizes:
- Under nutrient-replete conditions, high TC allows rapid reacquisition of TC by scanning 40S subunits after translating uORF1, promoting reinitiation at inhibitory uORFs and repression of the GCN4 ORF.
- Under starvation, eIF2α phosphorylation reduces TC, delaying reacquisition and enabling 40S subunits to bypass inhibitory uORFs and reinitiate at the GCN4 start codon. (dever2016mechanismandregulation pages 27-28)
TOR inhibition by rapamycin stimulates eIF2α Ser51 phosphorylation by Gcn2 and induces GCN4 translation; this response involves changes in Gcn2 regulatory phosphorylation (e.g., Ser577) and requires TAP42 and type-2A-related phosphatases, demonstrating cross-talk between TOR signaling and the Gcn2–eIF2α translational-control axis. (cherkasova2003translationalcontrolby pages 1-2)
Snf1 promotes eIF2α phosphorylation through two separable mechanisms:
- During histidine starvation of glucose-grown cells, Snf1 promotes Gcn2 activity (including activation-loop autophosphorylation on Gcn2) leading to higher eIF2α-P.
- Under some carbon-source conditions (e.g., galactose), Snf1 promotes eIF2α phosphorylation by inhibiting phosphatases Glc7 (PP1) and Sit4 (PP2A-like); both phosphatases physically interact with eIF2α, supporting direct dephosphorylation. (cherkasova2010snf1promotesphosphorylation pages 1-2)
Direct localization imaging for Sui2 was not present in the retrieved corpus; however, the mechanistic literature places Sui2/eIF2α functionally in the cytosolic translation initiation pathway:
- It operates on the 40S subunit within 43S/48S preinitiation complexes during scanning and start codon recognition. (thakur2020eif2αinteractionswith pages 2-2, thakur2020eif2αinteractionswith pages 12-13)
- It participates in the cytosolic eIF2↔eIF2B nucleotide exchange cycle controlling TC levels. (adomavicius2019thestructuralbasis pages 1-2)
Tool-based retrieval yielded limited 2023–2024 yeast Sui2-centric primary literature in the available corpus. The most relevant “recent” mechanistic advances available here are therefore anchored by:
- Cryo-EM structural mechanism explaining how phosphorylated versus unphosphorylated eIF2 engages eIF2B, with the conclusion that higher affinity of eIF2αP for eIF2B drives translational control; the paper also provides quantitative affinity values (Kd 3.5 nM phosphorylated vs 32.2 nM unphosphorylated in their cited measurements) and notes that partial phosphorylation can be sufficient because eIF2B is less abundant than eIF2. Publication date: May 2019; URL: https://doi.org/10.1038/s41467-019-10167-3. (adomavicius2019thestructuralbasis pages 1-2)
- Systems phosphoproteomics expanding the Gcn2-controlled network while retaining eIF2α phosphorylation dependence of GCN4 translational induction. Publication date: May 2021; URL: https://doi.org/10.1016/j.molcel.2021.02.037. (dokladal2021globalphosphoproteomicspinpoints pages 4-6)
Given the user request, this should be treated as an evidence-limited section rather than an assertion that no 2023–2024 work exists.
Sui2/eIF2α and its Ser51 phosphorylation are widely used as operational readouts of nutrient/stress-regulated translational control in yeast:
- Phospho-specific immunoblotting against eIF2α phosphorylated at Ser51 is used to quantify pathway activation (e.g., after rapamycin, amino acid stress, or other perturbations). (cherkasova2003translationalcontrolby pages 1-2)
- GCN4-lacZ reporter derepression assays are used as sensitive functional tests for translation initiation factor activity and for dependence on eIF2α phosphorylation. (dokladal2021globalphosphoproteomicspinpoints pages 4-6)
- Polysome profiling provides a global measure of translation initiation changes and is used alongside pathway mutants; in a Gcn2-centered phosphoproteomics study, specific phosphomutants in the upstream activator Gcn20 produced measurable changes in polysome:monosome (P:M) ratios under rapamycin (−7.6% or +8.6% changes in specific mutants/conditions). (dokladal2021globalphosphoproteomicspinpoints pages 4-6)
Applied/physiological contexts in yeast supported by the retrieved corpus include:
- Intracellular acid stress tolerance, where a phosphorylation-defective sui2-S51A mutant is acid-sensitive, implicating the eIF2α phosphorylation switch in adaptation. (hueso2012anovelrole pages 1-2)
- Iron deficiency, where the Gcn2/eIF2α pathway limits translation initiation during severe iron limitation, consistent with global translational repression as a stress response. (romero2020globaltranslationalrepression pages 1-2)
An authoritative yeast translation review integrates genetic, biochemical, and structural evidence to position Sui2/eIF2α as both (i) a core TC component for initiation and (ii) a conserved translational-control node whose Ser51 phosphorylation regulates global initiation and selective translation (e.g., GCN4) through TC availability. Publication date: May 2016; URL: https://doi.org/10.1534/genetics.115.186221. (dever2016mechanismandregulation pages 6-7, dever2016mechanismandregulation pages 27-28)
SUI2 (UniProt P20459) encodes yeast eIF2α, a non-enzymatic translation initiation factor whose primary molecular function is to contribute to formation and function of the eIF2·GTP·Met-tRNAi ternary complex and to participate directly in start-codon selection within the 43S/48S PIC through defined interactions with rRNA/mRNA and other initiation factors. (dever2016mechanismandregulation pages 6-7, thakur2020eif2αinteractionswith pages 2-2, thakur2020eif2αinteractionswith pages 12-13)
Its most prominent regulatory role is as the conserved substrate of Gcn2: Ser51 phosphorylation converts eIF2 into a potent functional inhibitor of eIF2B, decreasing TC availability and thereby globally repressing initiation while enabling selective translation programs such as GCN4 induction via uORF-mediated reinitiation control. This pathway is integrated with broader nutrient signaling networks including TOR/Tap42 phosphatase regulation and Snf1-mediated control of kinase/phosphatase activities. (cherkasova2003translationalcontrolby pages 1-2, cherkasova2010snf1promotesphosphorylation pages 1-2, dever2016mechanismandregulation pages 27-28)
| Aspect: identity/complex | Core molecular function | Key regulation/PTMs | Pathway context | Structural features/domains/residues | Representative evidence/assays | Key references with year and URL |
|---|---|---|---|---|---|---|
| SUI2 encodes the α subunit of heterotrimeric eIF2 in S. cerevisiae; partner subunits are Sui3/eIF2β and Gcd11/eIF2γ (dever2016mechanismandregulation pages 6-7) | eIF2 binds GTP and Met-tRNAi(^Met) to form the ternary complex (TC), delivering initiator tRNA to the 40S ribosome for 43S/48S preinitiation-complex assembly and start-codon recognition (dever2016mechanismandregulation pages 6-7) | Phosphorylation of eIF2α at conserved Ser51 by Gcn2 inhibits TC formation indirectly by converting eIF2 into an inhibitor of eIF2B-mediated GDP→GTP exchange (dever2016mechanismandregulation pages 6-7, cherkasova2003translationalcontrolby pages 1-2, dever2016mechanismandregulation pages 27-28) | Central node in translation initiation and the yeast general amino acid control / ISR-like stress response; reduced TC selectively derepresses GCN4 translation while lowering global initiation (dever2016mechanismandregulation pages 27-28) | eIF2α comprises an N-terminal OB-fold, a central α-helical domain, and a C-terminal α/β domain that contacts eIF2γ; Ser51 lies in a mobile loop in the OB-fold (dever2016mechanismandregulation pages 6-7) | Genetic suppressor analysis (Sui(^-) mutants), TC-binding/48S studies, cryo-EM-informed models, reporter assays for GCN4 control (dever2016mechanismandregulation pages 6-7, dever2016mechanismandregulation pages 27-28, adomavicius2019thestructuralbasis pages 1-2) | Dever et al., 2016, Genetics, https://doi.org/10.1534/genetics.115.186221; Adomavicius et al., 2019, Nat Commun, https://doi.org/10.1038/s41467-019-10167-3 |
| eIF2α/Sui2 acts directly within the scanning preinitiation complex (thakur2020eif2αinteractionswith pages 2-2, thakur2020eif2αinteractionswith pages 12-13) | Helps stabilize scanning/open and start-recognition/closed states of the PIC; contributes to accuracy of AUG selection versus near-cognate codons such as UUG (thakur2020eif2αinteractionswith pages 12-13, thakur2020eif2αinteractionswith pages 2-2, thakur2020eif2αinteractionswith pages 7-8) | No catalytic activity of its own; function is regulated by phosphorylation state and by residue-specific interactions with mRNA/rRNA/eIF1/eIF5 (thakur2020eif2αinteractionswith pages 2-2, thakur2020eif2αinteractionswith pages 12-13) | Part of the eIF2 cycle linking TC loading, scanning, start-codon recognition, and factor recycling by eIF2B/eIF5 (adomavicius2019thestructuralbasis pages 1-2, dever2016mechanismandregulation pages 27-28) | R53 contacts rRNA helix 23; Arg55/Arg57 contact mRNA context near the start site; unstructured N-terminal tail interacts with eIF1 in the open PIC and later with eIF5-CTD after AUG recognition (thakur2020eif2αinteractionswith pages 2-2, thakur2020eif2αinteractionswith pages 12-13) | HIS4-lacZ UUG:AUG reporters, growth phenotypes, plasmid-shuffle SUI2 alleles, β-gal assays, western blots, TC dissociation/recruitment measurements (thakur2020eif2αinteractionswith pages 7-8, thakur2020eif2αinteractionswith pages 5-6, thakur2020eif2αinteractionswith pages 12-13) | Thakur et al., 2020, Nucleic Acids Res, https://doi.org/10.1093/nar/gkaa761 |
| eIF2α is the canonical substrate of yeast Gcn2 kinase under amino acid stress and other nutrient stresses (cherkasova2010snf1promotesphosphorylation pages 1-2, romero2020globaltranslationalrepression pages 1-2) | When phosphorylated, lowers available TC so scanning 40S subunits reacquire TC more slowly, enabling bypass of inhibitory uORFs in GCN4 leader and translation of GCN4 ORF (dever2016mechanismandregulation pages 27-28) | Ser51 phosphorylation is promoted by uncharged tRNAs via Gcn1/Gcn20 and can be influenced upstream by TOR/Tap42, Snf1, and phosphatases Glc7/Sit4 acting on the pathway (cherkasova2010snf1promotesphosphorylation pages 1-2, cherkasova2003translationalcontrolby pages 1-2, romero2020globaltranslationalrepression pages 1-2) | Integrates amino acid starvation, TOR inhibition/rapamycin response, iron deficiency, and intracellular acid stress into translational control (cherkasova2003translationalcontrolby pages 1-2, romero2020globaltranslationalrepression pages 1-2, hueso2012anovelrole pages 1-2) | Ser51 is the key phospho-acceptor residue; phosphorylation increases affinity of eIF2 for eIF2B, explaining inhibitory sequestration of the GEF (adomavicius2019thestructuralbasis pages 1-2, cherkasova2003translationalcontrolby pages 1-2) | Phospho-specific western blots, GCN4-lacZ derepression assays, polysome profiling, toeprinting, genetic epistasis with gcn2Δ/gcn1Δ and S51A mutants (dever2016mechanismandregulation pages 27-28, dokladal2021globalphosphoproteomicspinpoints pages 4-6, cherkasova2003translationalcontrolby pages 1-2) | Cherkasova & Hinnebusch, 2003, Genes Dev, https://doi.org/10.1101/gad.1069003; Romero et al., 2020, Sci Rep, https://doi.org/10.1038/s41598-019-57132-0 |
| SUI2 participates in stress-adaptive translational control beyond classic amino acid starvation (hueso2012anovelrole pages 1-2, romero2020globaltranslationalrepression pages 1-2) | Supports selective translation programs that help cells adapt to nutrient and physicochemical stress while globally repressing bulk translation (hueso2012anovelrole pages 1-2, romero2020globaltranslationalrepression pages 1-2) | S51A phospho-dead Sui2 abolishes this regulatory switch in tested stress settings (hueso2012anovelrole pages 1-2, uppala2018phosphorylationoftranslation pages 9-12) | Shown for intracellular acid stress and iron deficiency, highlighting broad stress responsiveness of the Gcn2–eIF2α axis in yeast (hueso2012anovelrole pages 1-2, romero2020globaltranslationalrepression pages 1-2) | Same conserved Ser51-centered regulatory loop underlies distinct stress outputs (hueso2012anovelrole pages 1-2, uppala2018phosphorylationoftranslation pages 9-12) | Acid-stress growth phenotyping of sui2-S51A; iron-starvation analyses of global translation initiation dependence on Gcn2/eIF2α pathway (hueso2012anovelrole pages 1-2, romero2020globaltranslationalrepression pages 1-2) | Hueso et al., 2012, Biochem J, https://doi.org/10.1042/BJ20111264; Uppala et al., 2018, FEBS Lett, https://doi.org/10.1002/1873-3468.13214 |
| Recent systems-level work extends the eIF2α-centered network to additional Gcn2 targets while retaining Sui2/eIF2α phosphorylation as the core output (dokladal2021globalphosphoproteomicspinpoints pages 4-6) | Confirms eIF2α phosphorylation-dependent derepression of GCN4 and identifies cooperating translational regulators (e.g., Sui3/eIF2β, Gcn20) (dokladal2021globalphosphoproteomicspinpoints pages 4-6) | In 2021 phosphoproteomics, Sui2-Ser52, Sui3-Ser80, and Gcn20 Thr94/Ser95 were robust Gcn2-dependent sites in rapamycin-treated or leucine-starved cells (dokladal2021globalphosphoproteomicspinpoints pages 4-6) | Places SUI2 within a broader Gcn2-regulated phospho-network affecting translation initiation under TOR inhibition and amino acid stress (dokladal2021globalphosphoproteomicspinpoints pages 4-6) | Sui2 phosphosite is adjacent to the canonical Ser51 numbering convention used in many studies/antibodies; evidence supports conserved regulatory-site assignment in yeast datasets (dokladal2021globalphosphoproteomicspinpoints pages 4-6, romero2020globaltranslationalrepression pages 1-2) | Quantitative phosphoproteomics, in vitro kinase assays, GCN4-lacZ reporter derepression, and polysome P:M measurements (e.g., Gcn20 phosphomutants changing P:M ratios by −10.6%, −7.6%, or +8.6% in specified conditions) (dokladal2021globalphosphoproteomicspinpoints pages 4-6) | Dokládal et al., 2021, Molecular Cell, https://doi.org/10.1016/j.molcel.2021.02.037 |
Table: This table compactly summarizes the verified identity, molecular function, regulation, structural features, pathway roles, and supporting evidence for yeast SUI2/eIF2α (UniProt P20459). It is useful as a citation-ready functional annotation artifact grounded only in the gathered evidence and context IDs.
References
(dever2016mechanismandregulation pages 6-7): TE Dever, TG Kinzy, and GD Pavitt. Mechanism and regulation of protein synthesis in saccharomyces cerevisiae. Genetics, 203:107-65, May 2016. URL: https://doi.org/10.1534/genetics.115.186221, doi:10.1534/genetics.115.186221. This article has 207 citations and is from a domain leading peer-reviewed journal.
(adomavicius2019thestructuralbasis pages 1-2): Tomas Adomavicius, Margherita Guaita, Yu Zhou, Martin D. Jennings, Zakia Latif, Alan M. Roseman, and Graham D. Pavitt. The structural basis of translational control by eif2 phosphorylation. Nature Communications, May 2019. URL: https://doi.org/10.1038/s41467-019-10167-3, doi:10.1038/s41467-019-10167-3. This article has 223 citations and is from a highest quality peer-reviewed journal.
(cherkasova2003translationalcontrolby pages 1-2): Vera A. Cherkasova and Alan G. Hinnebusch. Translational control by tor and tap42 through dephosphorylation of eif2alpha kinase gcn2. Genes & development, 17 7:859-72, Apr 2003. URL: https://doi.org/10.1101/gad.1069003, doi:10.1101/gad.1069003. This article has 393 citations and is from a highest quality peer-reviewed journal.
(dever2016mechanismandregulation pages 27-28): TE Dever, TG Kinzy, and GD Pavitt. Mechanism and regulation of protein synthesis in saccharomyces cerevisiae. Genetics, 203:107-65, May 2016. URL: https://doi.org/10.1534/genetics.115.186221, doi:10.1534/genetics.115.186221. This article has 207 citations and is from a domain leading peer-reviewed journal.
(thakur2020eif2αinteractionswith pages 12-13): Anil Thakur, Swati Gaikwad, Anil K Vijjamarri, and Alan G Hinnebusch. Eif2α interactions with mrna control accurate start codon selection by the translation preinitiation complex. Nucleic acids research, 48:10280-10296, Sep 2020. URL: https://doi.org/10.1093/nar/gkaa761, doi:10.1093/nar/gkaa761. This article has 27 citations and is from a highest quality peer-reviewed journal.
(thakur2020eif2αinteractionswith pages 2-2): Anil Thakur, Swati Gaikwad, Anil K Vijjamarri, and Alan G Hinnebusch. Eif2α interactions with mrna control accurate start codon selection by the translation preinitiation complex. Nucleic acids research, 48:10280-10296, Sep 2020. URL: https://doi.org/10.1093/nar/gkaa761, doi:10.1093/nar/gkaa761. This article has 27 citations and is from a highest quality peer-reviewed journal.
(romero2020globaltranslationalrepression pages 1-2): Antonia María Romero, Lucía Ramos-Alonso, Paula Alepuz, Sergi Puig, and María Teresa Martínez-Pastor. Global translational repression induced by iron deficiency in yeast depends on the gcn2/eif2α pathway. Scientific Reports, Jan 2020. URL: https://doi.org/10.1038/s41598-019-57132-0, doi:10.1038/s41598-019-57132-0. This article has 45 citations and is from a peer-reviewed journal.
(cherkasova2010snf1promotesphosphorylation pages 1-2): Vera Cherkasova, Hongfang Qiu, and Alan G. Hinnebusch. Snf1 promotes phosphorylation of the α subunit of eukaryotic translation initiation factor 2 by activating gcn2 and inhibiting phosphatases glc7 and sit4. Jun 2010. URL: https://doi.org/10.1128/mcb.00183-10, doi:10.1128/mcb.00183-10. This article has 75 citations and is from a domain leading peer-reviewed journal.
(dokladal2021globalphosphoproteomicspinpoints pages 4-6): Ladislav Dokládal, Michael Stumpe, Benjamin Pillet, Zehan Hu, Guillermo Miguel Garcia Osuna, Dieter Kressler, Jörn Dengjel, and Claudio De Virgilio. Global phosphoproteomics pinpoints uncharted gcn2-mediated mechanisms of translational control. Molecular Cell, 81:1879-1889.e6, May 2021. URL: https://doi.org/10.1016/j.molcel.2021.02.037, doi:10.1016/j.molcel.2021.02.037. This article has 40 citations and is from a highest quality peer-reviewed journal.
(hueso2012anovelrole pages 1-2): Guillem Hueso, Rafael Aparicio-Sanchis, Consuelo Montesinos, Silvia Lorenz, José R. Murguía, and Ramón Serrano. A novel role for protein kinase gcn2 in yeast tolerance to intracellular acid stress. Biochemical Journal, 441(1):255-264, Dec 2012. URL: https://doi.org/10.1042/bj20111264, doi:10.1042/bj20111264. This article has 62 citations and is from a domain leading peer-reviewed journal.
(thakur2020eif2αinteractionswith pages 7-8): Anil Thakur, Swati Gaikwad, Anil K Vijjamarri, and Alan G Hinnebusch. Eif2α interactions with mrna control accurate start codon selection by the translation preinitiation complex. Nucleic acids research, 48:10280-10296, Sep 2020. URL: https://doi.org/10.1093/nar/gkaa761, doi:10.1093/nar/gkaa761. This article has 27 citations and is from a highest quality peer-reviewed journal.
(thakur2020eif2αinteractionswith pages 5-6): Anil Thakur, Swati Gaikwad, Anil K Vijjamarri, and Alan G Hinnebusch. Eif2α interactions with mrna control accurate start codon selection by the translation preinitiation complex. Nucleic acids research, 48:10280-10296, Sep 2020. URL: https://doi.org/10.1093/nar/gkaa761, doi:10.1093/nar/gkaa761. This article has 27 citations and is from a highest quality peer-reviewed journal.
(uppala2018phosphorylationoftranslation pages 9-12): Jagadeesh Kumar Uppala, Chandrima Ghosh, Leena Sathe, and Madhusudan Dey. Phosphorylation of translation initiation factor eif2α at ser51 depends on site‐ and context‐specific information. FEBS Letters, 592:3116-3125, Sep 2018. URL: https://doi.org/10.1002/1873-3468.13214, doi:10.1002/1873-3468.13214. This article has 22 citations and is from a peer-reviewed journal.