T611135 Anti-EIF2S2/EIF2B Rabbit Pab

Total Page：16

File Type：pdf, Size：1020Kb

T611135 Anti-EIF2S2/EIF2B Rabbit pAb Order 021-34695924 [email protected] Support 400-6123-828 50ul [email protected] 100 uL √ √ Web www.ab-mart.com.cn Product Information Description EIF2S2 rabbit polyclonal Protein full name Eukaryotic translation initiation factor 2 subunit 2 Synonyms eIF-2-beta, Eif2s2, Eukaryotic translation initiation factor 2 subunit beta Immunogen Recombinant protein corresponding to Mouse EIF2S2 Isotype IgG Purity Affinity purification Subcellular location Cytoplasm Predicted MW. 38 kDa Observed MW. 50 kDa Uniprot ID P20042, Q99L45 Applications Applications WB IHC IF Species Human, Mouse, Rat Human, Rat Human, Rat Dilution 1: 500-1: 1000 1: 1000-1: 2000 1: 500-1: 1000 Positive tissue lung, colon, small colon, lung, placenta colon, brain intestine Background Eukaryotic translation initiation factor 2 (eIF2) is composed of three subunits, eIF2 alpha, eIF2 beta (EIF2S2), and eIF2 gamma, which are present in equal molar amounts. eIF2 beta plays a central role in the maintenance of what is generally considered a rate-limiting step in mRNA translation. In the early steps of protein synthesis, eIF2 beta binds GTP and Met-tRNA and transfers Met-tRNA to the 40S ribosomal subunit. At the end of the initiation process, GTP bound to eIF2 beta is hydrolyzed to GDP and the eIF2/GDP complex is released from the ribosome. The exchange of GDP bound to eIF2 beta for GTP is a prerequisite to binding Met-tRNA and is mediated by eIF2 beta, which recycles the eIF2 complex for another round of initiation. Images Western blot analysis of EIF2S2 (T611135M) at dilution of 1: 1000 Lane 1: HT29 cell lysate Lane 2: L1299 cell lysate Lane 3: CaCO2 cell lysate Lane 4: Mouse lung tissue lysate Lane 5: Mouse colon tissue lysate Lane 6: Mouse small intestine tissue lysate Lane 7: Rat lung tissue lysate Immunohistochemistry analysis of paraffin- embedded human colon using EIF2S2 (T611135M) at dilution of 1: 1000 Immunohistochemistry analysis of paraffin- embedded rat lung using EIF2S2 (T611135M) at dilution of 1: 2000 ? Immunohistochemistry analysis of paraffin- embedded rat placenta using EIF2S2 (T611135M) at dilution of 1: 1000 Immunofluorescent analysis of paraffin- embedded human colon using EIF2S2 (T611135M) at dilution of 1: 1000 Immunofluorescent analysis of paraffin- embedded rat brain using EIF2S2 (T611135M) at dilution of 1: 1000 Storage Storage Store at -20 ℃ for one year. Avoid repeated freeze/ thaw cycles. Storage Buffer PBS with 0.02% sodium azide, 100 μg/ml BSA and 50% glycerol. NOTE: This product is intended for research only. .

Copy Link

Recommended publications

Translational Resistance of Late Alphavirus Mrna to Eif2␣ Phosphorylation: a Strategy to Overcome the Antiviral Effect of Protein Kinase PKR
Downloaded from genesdev.cshlp.org on September 29, 2021 - Published by Cold Spring Harbor Laboratory Press Translational resistance of late alphavirus mRNA to eIF2␣ phosphorylation: a strategy to overcome the antiviral effect of protein kinase PKR Iván Ventoso,1,3 Miguel Angel Sanz,2 Susana Molina,2 Juan José Berlanga,2 Luis Carrasco,2 and Mariano Esteban1 1Departamento de Biología Molecular y Celular, Centro Nacional de Biotecnología/CSIC, Cantoblanco, E-28049 Madrid, Spain; 2Centro de Biología Molecular Severo Ochoa (CSIC-UAM), Facultad de Ciencias, Cantoblanco, E-28049 Madrid, Spain The double-stranded RNA-dependent protein kinase (PKR) is one of the four mammalian kinases that phosphorylates the translation initiation factor 2␣ in response to virus infection. This kinase is induced by interferon and activated by double-stranded RNA (dsRNA). Phosphorylation of eukaryotic initiation factor 2␣ (eIF2␣) blocks translation initiation of both cellular and viral mRNA, inhibiting virus replication. To counteract this effect, most viruses express inhibitors that prevent PKR activation in infected cells. Here we report that PKR is highly activated following infection with alphaviruses Sindbis (SV) and Semliki Forest virus (SFV), leading to the almost complete phosphorylation of eIF2␣. Notably, subgenomic SV 26S mRNA is translated efficiently in the presence of phosphorylated eIF2␣. This modification of eIF2 does not restrict viral replication; SV 26S mRNA initiates translation with canonical methionine in the presence of high levels of phosphorylated eIF2␣. Genetic and biochemical data showed a highly stable RNA hairpin loop located downstream of the AUG initiator codon that is necessary to provide translational resistance to eIF2␣ phosphorylation. This structure can stall the ribosomes on the correct site to initiate translation of SV 26S mRNA, thus bypassing the requirement for a functional eIF2.
[Show full text]
Universal Conservation in Translation Initiation Revealed By
Proc. Natl. Acad. Sci. USA Vol. 96, pp. 4342–4347, April 1999 Biochemistry Universal conservation in translation initiation revealed by human and archaeal homologs of bacterial translation initiation factor IF2 (eukaryotic translation initiation factoryFUN12yinitiator tRNA) JOON H. LEE*, SANG KI CHOI*, ANTONINA ROLL-MECAK†,STEPHEN K. BURLEY†‡, AND THOMAS E. DEVER*§ *Laboratory of Eukaryotic Gene Regulation, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-2716; and †Laboratories of Molecular Biophysics and ‡Howard Hughes Medical Institute, The Rockefeller University, New York, NY 10021 Communicated by Igor B. Dawid, National Institute of Child Health and Human Development, Bethesda, MD, February 11, 1999 (received for review September 22, 1998) ABSTRACT Binding of initiator methionyl-tRNA to ribo- romyces cerevisiae (7) revealed the presence of IF2 homologs somes is catalyzed in prokaryotes by initiation factor (IF) IF2 in addition to all three eIF2 subunits in this archaeon and and in eukaryotes by eIF2. The discovery of both IF2 and eIF2 eukaryote, respectively. The identification of both IF2 and homologs in yeast and archaea suggested that these microbes eIF2 homologs in archaea was surprising and contributed to possess an evolutionarily intermediate protein synthesis ap- speculation that archaea may possess a translation apparatus paratus. We describe the identification of a human IF2 intermediate between prokaryotes and eukaryotes (8). The homolog, and we demonstrate by using in vivo and in vitro presence of the IF2 homolog in yeast suggests instead that IF2 assays that human IF2 functions as a translation factor. In has been conserved throughout the evolution of microbes from addition, we show that archaea IF2 can substitute for its yeast bacteria to the lower eukaryotes.
[Show full text]
Initiation Factor Eif5b Catalyzes Second GTP-Dependent Step in Eukaryotic Translation Initiation
Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation Joon H. Lee*†, Tatyana V. Pestova†‡§, Byung-Sik Shin*, Chune Cao*, Sang K. Choi*, and Thomas E. Dever*¶ *Laboratory of Gene Regulation and Development, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-2716; ‡Department of Microbiology and Immunology, State University of New York Health Science Center, Brooklyn, NY 11203; and §A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, Russia Edited by Harry F. Noller, University of California, Santa Cruz, CA, and approved October 31, 2002 (received for review September 19, 2002) Initiation factors IF2 in bacteria and eIF2 in eukaryotes are GTPases In addition, when nonhydrolyzable GDPNP was substituted Met that bind Met-tRNAi to the small ribosomal subunit. eIF5B, the for GTP, eIF5B catalyzed subunit joining; however, the factor eukaryotic ortholog of IF2, is a GTPase that promotes ribosomal was unable to dissociate from the 80S ribosome after subunit subunit joining. Here we show that eIF5B GTPase activity is re- joining (7). quired for protein synthesis. Mutation of the conserved Asp-759 in To dissect the function of the eIF5B G domain and test the human eIF5B GTP-binding domain to Asn converts eIF5B to an model that two GTP molecules are required in translation XTPase and introduces an XTP requirement for subunit joining and initiation, we mutated conserved residues in the eIF5B G translation initiation. Thus, in contrast to bacteria where the single domain and tested the function of the mutant proteins in GTPase IF2 is sufﬁcient to catalyze translation initiation, eukaryotic translation initiation.
[Show full text]
EIF2S1 Antibody Cat
EIF2S1 Antibody Cat. No.: 57-063 EIF2S1 Antibody Confocal immunofluorescent analysis of EIF2S1 Antibody EIF2S1 Antibody immunohistochemistry analysis in with Hela cell followed by Alexa Fluor 488-conjugated goat formalin fixed and paraffin embedded human stomach anti-rabbit lgG (green). DAPI was used to stain the cell tissue followed by peroxidase conjugation of the nuclear (blue). secondary antibody and DAB staining. Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Mouse Predicted species reactivity based on immunogen sequence: Rat, Chicken, Yeast, Bovine, HOMOLOGY: Drosophila This EIF2S1 antibody is generated from rabbits immunized with a KLH conjugated IMMUNOGEN: synthetic peptide between 60-89 amino acids from the N-terminal region of human EIF2S1. TESTED APPLICATIONS: IF, IHC-P, WB September 30, 2021 1 https://www.prosci-inc.com/eif2s1-antibody-57-063.html For WB starting dilution is: 1:1000 APPLICATIONS: For IF starting dilution is: 1:10~50 For IHC-P starting dilution is: 1:10~50 PREDICTED MOLECULAR 36 kDa WEIGHT: Properties This antibody is purified through a protein A column, followed by peptide affinity PURIFICATION: purification. CLONALITY: Polyclonal ISOTYPE: Rabbit Ig CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: Supplied in PBS with 0.09% (W/V) sodium azide. CONCENTRATION: batch dependent Store at 4˚C for three months and -20˚C, stable for up to one year. As with all antibodies STORAGE CONDITIONS: care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures. Additional Info OFFICIAL SYMBOL: EIF2S1 Eukaryotic translation initiation factor 2 subunit 1, Eukaryotic translation initiation factor 2 ALTERNATE NAMES: subunit alpha, eIF-2-alpha, eIF-2A, eIF-2alpha, EIF2S1, EIF2A ACCESSION NO.: P05198 PROTEIN GI NO.: 124200 GENE ID: 1965 USER NOTE: Optimal dilutions for each application to be determined by the researcher.
[Show full text]
Rps3/Us3 Promotes Mrna Binding at the 40S Ribosome Entry Channel and Stabilizes Preinitiation Complexes at Start Codons
Rps3/uS3 promotes mRNA binding at the 40S ribosome entry channel and stabilizes preinitiation complexes at start codons Jinsheng Donga, Colin Echeverría Aitkenb, Anil Thakura, Byung-Sik Shina, Jon R. Lorschb,1, and Alan G. Hinnebuscha,1 aLaboratory of Gene Regulation and Development, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892; and bLaboratory on the Mechanism and Regulation of Protein Synthesis, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892 Contributed by Alan G. Hinnebusch, January 24, 2017 (sent for review December 15, 2016; reviewed by Jamie H. D. Cate and Matthew S. Sachs) Met The eukaryotic 43S preinitiation complex (PIC) bearing Met-tRNAi rearrangement to PIN at both near-cognate start codons (e.g., in a ternary complex (TC) with eukaryotic initiation factor (eIF)2-GTP UUG) and cognate (AUG) codons in poor Kozak context; hence scans the mRNA leader for an AUG codon in favorable “Kozak” eIF1 must dissociate from the 40S subunit for start-codon rec- context. AUG recognition provokes rearrangement from an open ognition (Fig. 1A). Consistent with this, structural analyses of PIC conformation with TC bound in a state not fully engaged with partial PICs reveal that eIF1 and eIF1A promote rotation of the “ ” the P site ( POUT ) to a closed, arrested conformation with TC tightly 40S head relative to the body (2, 3), thought to be instrumental bound in the “P ” state. Yeast ribosomal protein Rps3/uS3 resides IN in TC binding in the POUT conformation, but that eIF1 physically in the mRNA entry channel of the 40S subunit and contacts mRNA Met clashes with Met-tRNAi in the PIN state (2, 4), and is both via conserved residues whose functional importance was unknown.
[Show full text]
Relevance of Translation Initiation in Diffuse Glioma Biology and Its
cells Review Relevance of Translation Initiation in Diﬀuse Glioma Biology and its Therapeutic Potential Digregorio Marina 1, Lombard Arnaud 1,2, Lumapat Paul Noel 1, Scholtes Felix 1,2, Rogister Bernard 1,3 and Coppieters Natacha 1,* 1 Laboratory of Nervous System Disorders and Therapy, GIGA-Neurosciences Research Centre, University of Liège, 4000 Liège, Belgium; [email protected] (D.M.); [email protected] (L.A.); [email protected] (L.P.N.); [email protected] (S.F.); [email protected] (R.B.) 2 Department of Neurosurgery, CHU of Liège, 4000 Liège, Belgium 3 Department of Neurology, CHU of Liège, 4000 Liège, Belgium * Correspondence: [email protected] Received: 18 October 2019; Accepted: 26 November 2019; Published: 29 November 2019 Abstract: Cancer cells are continually exposed to environmental stressors forcing them to adapt their protein production to survive. The translational machinery can be recruited by malignant cells to synthesize proteins required to promote their survival, even in times of high physiological and pathological stress. This phenomenon has been described in several cancers including in gliomas. Abnormal regulation of translation has encouraged the development of new therapeutics targeting the protein synthesis pathway. This approach could be meaningful for glioma given the fact that the median survival following diagnosis of the highest grade of glioma remains short despite current therapy. The identiﬁcation of new targets for the development of novel therapeutics is therefore needed in order to improve this devastating overall survival rate. This review discusses current literature on translation in gliomas with a focus on the initiation step covering both the cap-dependent and cap-independent modes of initiation.
[Show full text]
Eif2s2) (R31277
EIF2B Antibody (EIF2S2) (R31277) Catalog No. Formulation Size R31277 0.5mg/ml if reconstituted with 0.2ml sterile DI water 100 ug Bulk quote request Availability 1-3 business days Species Reactivity Human, Mouse, Rat Format Antigen affinity purified Clonality Polyclonal (rabbit origin) Isotype Rabbit IgG Purity Antigen affinity Buffer Lyophilized from 1X PBS with 2.5% BSA and 0.025% sodium azide/thimerosal UniProt P20042 Applications Western blot : 0.5-1ug/ml Limitations This EIF2B antibody is available for research use only. Western blot testing of EIF2B antibody and Lane 1: M451; 2: Jurkat; 3: HeLa; 4: 293T cell lysate. Expected/observed size ~38KD Description Eukaryotic translation initiation factor 2 subunit 2, also called EIF2B, is a protein that in humans is encoded by the EIF2S2 gene. This gene belongs to the EIF-2-beta family. Eukaryotic translation initiation factor 2 (EIF2) functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA and binding to a 40S ribosomal subunit. EIF2 is composed of three subunits, alpha, beta, and gamma, with the protein encoded by this gene representing the beta subunit. The beta subunit catalyzes the exchange of GDP for GTP, which recycles the EIF2 complex for another round of initiation. Application Notes The stated application concentrations are suggested starting amounts. Titration of the EIF2B antibody may be required due to differences in protocols and secondary/substrate sensitivity. Immunogen An amino acid sequence from the C-terminus of human EIF2 beta (FQAVTGKRAQLRAKAN) was used as the immunogen for this EIF2B antibody (100% homologous in human, mouse and rat).
[Show full text]
Fail-Safe Control of Translation Initiation by Dissociation of Eif2a
RESEARCH ARTICLE Fail-safe control of translation initiation by dissociation of eIF2a phosphorylated ternary complexes Martin D Jennings1,2, Christopher J Kershaw1,2, Tomas Adomavicius1,2, Graham D Pavitt1,2* 1Division of Molecular and Cellular Function, Faculty of Biology Medicine and Health, The University of Manchester, Manchester, United Kingdom; 2Manchester Academic Health Science Centre, The University of Manchester, Manchester, United Kingdom Abstract Phosphorylation of eIF2a controls translation initiation by restricting the levels of active eIF2-GTP/Met-tRNAi ternary complexes (TC). This modulates the expression of all eukaryotic mRNAs and contributes to the cellular integrated stress response. Key to controlling the activity of eIF2 are translation factors eIF2B and eIF5, thought to primarily function with eIF2-GDP and TC respectively. Using a steady-state kinetics approach with purified proteins we demonstrate that eIF2B binds to eIF2 with equal affinity irrespective of the presence or absence of competing guanine nucleotides. We show that eIF2B can compete with Met-tRNAi for eIF2-GTP and can destabilize TC. When TC is formed with unphosphorylated eIF2, eIF5 can out-compete eIF2B to stabilize TC/eIF5 complexes. However when TC/eIF5 is formed with phosphorylated eIF2, eIF2B outcompetes eIF5 and destabilizes TC. These data uncover competition between eIF2B and eIF5 for TC and identify that phosphorylated eIF2-GTP translation initiation intermediate complexes can be inhibited by eIF2B. DOI: 10.7554/eLife.24542.001 *For correspondence: graham. [email protected] Competing interests: The Introduction authors declare that no In eukaryotic translation initiation, initiator tRNA (Met-tRNAi) recognises AUG start codons in mRNA competing interests exist.
[Show full text]
Crystal Structure of Eukaryotic Translation Initiation Factor 2B K
Life Science Research Frontiers 2016 Research Frontiers 2016 Crystal structure of eukaryotic translation initiation factor 2B The eukaryotic translation initiation factor 2B eIF2B subunits that are essential for these regulatory (eIF2B) is the guanine nucleotide exchange factor for and catalytic interactions with eIF2. However, the eIF2. eIF2 carries the methionylated initiator tRNA molecular mechanisms of these interactions have (Met-tRNAi) to the ribosome in a GTP-dependent hardly been described since the tertiary structure of manner and is released from the ribosome as the the eIF2B decamer was unknown. GDP-bound form after the recognition of an initiation Toward structural analysis, our group established codon. To participate in the next round of translation a bacterial expression system for the large-scale initiation events, eIF2 must be converted into the production of Schizosaccharomyces pombe eIF2B, GTP-bound form by eIF2B (Fig. 1) [1]. However, this which then was successfully crystallized [3]. X-ray nucleotide exchange activity of eIF2B is inhibited by the diffraction data of the eIF2B crystals were collected phosphorylation of eIF2. The phosphorylation of eIF2 at SPring-8 BL32XU and BL41XU and at Photon is known to be rapidly induced by eIF2 kinases under Factory beamlines. The initial phases were determined various stress conditions such as viral infection and from the selenomethionine-derivative data set by the amino acid deprivation, and the phosphorylated eIF2 single-wavelength anomalous dispersion method [4]. forms a tight inactive complex with eIF2B. As a result The crystal structure of eIF2B was finally refined to a of this inhibition, the cellular level of the active GTP- resolution of 3.0 Å, revealing its decameric architecture.
[Show full text]
Prokaryote Translation (Protein Synthesis) Steps Initiation
Prokaryote Translation (Protein Synthesis) Steps Initiation There are three initiation factors that along with GTP assist the mRNA in attaching to the small 30S ribosomal subunit, and the initiator tRNA-formylMethionine complex to bind to the mRNA. The Shine-Dalgarno sequence on the 5' end of the mRNA matches up to the anti-Shine-Dalgarno sequence on the 3' end of the 16S rRNA of the small subunit. Once the anticodon of the initiator tRNA-formylMet complex binds the AUG start codon, the large 50S ribosomal subunit binds to the ribosomal binding site on the mRNA and to a domain on the tRNA in the P (peptidyl) site. The A (aminoacyl) site is empty as is the E (exit) site. Elongation The EF-Tu (elongation factor Tu) binds GTP and then the appropriate tRNA-AA at the TΨCG loop and attaches it to the A site on the large ribosomal subunit. If the tRNA-AA anticodon matches the codon, the GTPase domain on EF-Tu catalyzes GTP to GDP and releases from the tRNA-AA. Now the amine group of this tRNA-AA complex can form a peptide bond with the formyl-methionine amino acid in the P site. The peptidyl transferase activity is controlled by the 23S rRNA and L2 and L3 proteins. At this point the initiator tRNA is separated from its formyl-methionine amino acid. Another complex EF-G with GTP binds where the EF-Tu-GDP complex dissociated from the tRNA-AA in the A site and with the catalysis of GTP to GDP moves the ribosome three nucleotides down the mRNA.
[Show full text]
Anti-Eif2 Alpha Antibody (ARG57723)
Product datasheet [email protected] ARG57723 Package: 100 μl anti-eIF2 alpha antibody Store at: -20°C Summary Product Description Mouse Monoclonal antibody recognizes eIF2 alpha Tested Reactivity Hu, Ms, Rat Tested Application ICC/IF, WB Specificity This antibody detects endogenous levels of eIF2 alpha and does not cross-react with related proteins. Host Mouse Clonality Monoclonal Isotype IgG2b Target Name eIF2 alpha Antigen Species Human Immunogen Purified recombinant Human eIF2 alpha protein fragments expressed in E. coli. Conjugation Un-conjugated Alternate Names eIF-2alpha; EIF-2A; Eukaryotic translation initiation factor 2 subunit 1; EIF2; EIF-2alpha; EIF2A; eIF-2-alpha; Eukaryotic translation initiation factor 2 subunit alpha; eIF-2A; EIF-2 Application Instructions Application table Application Dilution ICC/IF 1:200 WB 1:1000 Application Note * The dilutions indicate recommended starting dilutions and the optimal dilutions or concentrations should be determined by the scientist. Calculated Mw 36 kDa Properties Form Liquid Purification Affinity purified. Buffer PBS (pH 7.4), 0.03% Proclin300 and 50% Glycerol. Preservative 0.03% Proclin300 Stabilizer 50% Glycerol Concentration 4 mg/ml Storage instruction For continuous use, store undiluted antibody at 2-8°C for up to a week. For long-term storage, aliquot and store at -20°C. Storage in frost free freezers is not recommended. Avoid repeated freeze/thaw cycles. Suggest spin the vial prior to opening. The antibody solution should be gently mixed before use. www.arigobio.com 1/2 Note For laboratory research only, not for drug, diagnostic or other use. Bioinformation Gene Symbol EIF2S1 Gene Full Name eukaryotic translation initiation factor 2, subunit 1 alpha, 35kDa Background The translation initiation factor EIF2 catalyzes the first regulated step of protein synthesis initiation, promoting the binding of the initiator tRNA to 40S ribosomal subunits.
[Show full text]
Protein Synthesis
40632_CH08_151_188.qxp 12/14/06 12:12 PM Page 151 8 Protein Synthesis CHAPTER OUTLINE 8.1 Introduction • The rRNA of the 30S bacterial ribosomal subunit has a com- plementary sequence that base pairs with the Shine– 8.2 Protein Synthesis Occurs by Initiation, Elongation, Dalgarno sequence during initiation. and Termination 8.8 Small Subunits Scan for Initiation Sites on Eukaryotic • The ribosome has three tRNA-binding sites. mRNA • An aminoacyl-tRNA enters the A site. • Eukaryotic 40S ribosomal subunits bind to the 5′ end of • Peptidyl-tRNA is bound in the P site. mRNA and scan the mRNA until they reach an initiation site. • Deacylated tRNA exits via the E site. • A eukaryotic initiation site consists of a ten-nucleotide • An amino acid is added to the polypeptide chain by trans- sequence that includes an AUG codon. ferring the polypeptide from peptidyl-tRNA in the P site to • 60S ribosomal subunits join the complex at the initiation aminoacyl-tRNA in the A site. site. 8.3 Special Mechanisms Control the Accuracy of Protein 8.9 Eukaryotes Use a Complex of Many Initiation Factors Synthesis • Initiation factors are required for all stages of initiation, • The accuracy of protein synthesis is controlled by specific including binding the initiator tRNA, 40S subunit attach- mechanisms at each stage. ment to mRNA, movement along the mRNA, and joining of 8.4 Initiation in Bacteria Needs 30S Subunits and Accessory the 60S subunit. Factors • Eukaryotic initiator tRNA is a Met-tRNA that is different from the Met-tRNA used in elongation, but the methionine • Initiation of protein synthesis requires separate 30S and is not formulated.
[Show full text]