eukaryotic initiation factor 1

Summary

Summary: A eukaryotic initiation factor that binds to 40S ribosomal subunits. Although initially considered a "non-essential" factor for eukaryotic transcription initiation, eukaryotic initiation factor-1 is now thought to play an important role in localizing RIBOSOMES at the initiation codon of MRNA.

Top Publications

  1. Pisarev A, Kolupaeva V, Pisareva V, Merrick W, Hellen C, Pestova T. Specific functional interactions of nucleotides at key -3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex. Genes Dev. 2006;20:624-36 pubmed
  2. Singh C, He H, Ii M, Yamamoto Y, Asano K. Efficient incorporation of eukaryotic initiation factor 1 into the multifactor complex is critical for formation of functional ribosomal preinitiation complexes in vivo. J Biol Chem. 2004;279:31910-20 pubmed
    b>Eukaryotic initiation factor 1 (eIF1) is a low molecular weight factor critical for stringent AUG selection in eukaryotic translation...
  3. Moazed D, Samaha R, Gualerzi C, Noller H. Specific protection of 16 S rRNA by translational initiation factors. J Mol Biol. 1995;248:207-10 pubmed
    ..We were unable to detect any effect of IF-2 on the reactivity pattern of 16 S rRNA, suggesting that this factor may interact primarily through protein-protein interactions. ..
  4. Acker M, Shin B, Dever T, Lorsch J. Interaction between eukaryotic initiation factors 1A and 5B is required for efficient ribosomal subunit joining. J Biol Chem. 2006;281:8469-75 pubmed
  5. Carter A, Clemons W, Brodersen D, Morgan Warren R, Hartsch T, Wimberly B, et al. Crystal structure of an initiation factor bound to the 30S ribosomal subunit. Science. 2001;291:498-501 pubmed
    ..The structure explains how localized changes at the ribosomal A site lead to global alterations in the conformation of the 30S subunit. ..
  6. Passmore L, Schmeing T, Maag D, Applefield D, Acker M, Algire M, et al. The eukaryotic translation initiation factors eIF1 and eIF1A induce an open conformation of the 40S ribosome. Mol Cell. 2007;26:41-50 pubmed
    ..Our results suggest that eIF1 and eIF1A promote an open, scanning-competent preinitiation complex that closes upon start codon recognition and eIF1 release to stabilize ternary complex binding and clamp down on mRNA. ..
  7. Battiste J, Pestova T, Hellen C, Wagner G. The eIF1A solution structure reveals a large RNA-binding surface important for scanning function. Mol Cell. 2000;5:109-19 pubmed
    ..Site-directed mutations at multiple positions along the RNA-binding surface were defective in the ability to properly assemble preinitiation complexes at the AUG codon in vitro. ..
  8. Lomakin I, Kolupaeva V, Marintchev A, Wagner G, Pestova T. Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing. Genes Dev. 2003;17:2786-97 pubmed
  9. Pestova T, Borukhov S, Hellen C. Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons. Nature. 1998;394:854-9 pubmed
    ..These proteins act synergistically to mediate assembly of ribosomal initiation complexes at the initiation codon and dissociate aberrant complexes from the mRNA. ..

More Information

Publications90

  1. Fekete C, Applefield D, Blakely S, Shirokikh N, Pestova T, Lorsch J, et al. The eIF1A C-terminal domain promotes initiation complex assembly, scanning and AUG selection in vivo. EMBO J. 2005;24:3588-601 pubmed
    ..Thus, the OB-fold is crucial for ribosome-binding and the C-terminal domain of eIF1A has eukaryotic-specific functions in TC recruitment and scanning. ..
  2. Algire M, Maag D, Lorsch J. Pi release from eIF2, not GTP hydrolysis, is the step controlled by start-site selection during eukaryotic translation initiation. Mol Cell. 2005;20:251-62 pubmed
    ..Release of P(i), which makes GTP hydrolysis irreversible, appears to be controlled by the AUG-dependent dissociation of eIF1 from the preinitiation complex. ..
  3. Sette M, van Tilborg P, Spurio R, Kaptein R, Paci M, Gualerzi C, et al. The structure of the translational initiation factor IF1 from E.coli contains an oligomer-binding motif. EMBO J. 1997;16:1436-43 pubmed
    ..Specific changes of NMR signals of IF1 upon titration with 30S ribosomal subunit identifies several residues that are involved in the interaction with ribosomes. ..
  4. Maag D, Algire M, Lorsch J. Communication between eukaryotic translation initiation factors 5 and 1A within the ribosomal pre-initiation complex plays a role in start site selection. J Mol Biol. 2006;356:724-37 pubmed
    ..These data suggest strongly that the interaction between eIF1A and eIF5 is involved in maintaining the fidelity of start codon recognition in vivo. ..
  5. Olsen D, Savner E, Mathew A, Zhang F, Krishnamoorthy T, Phan L, et al. Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo. EMBO J. 2003;22:193-204 pubmed
    ..We propose a modular organization for eIF1A wherein a core ribosome-binding domain is flanked by flexible segments that mediate interactions with other factors involved in recruitment of TC and release of eIF1A at subunit joining. ..
  6. Marintchev A, Kolupaeva V, Pestova T, Wagner G. Mapping the binding interface between human eukaryotic initiation factors 1A and 5B: a new interaction between old partners. Proc Natl Acad Sci U S A. 2003;100:1535-40 pubmed
    ..The binding between the C termini of eIF1A and eIF5B has implications for eukaryote-specific mechanisms of recruitment and release of translation IFs from the ribosome. ..
  7. Fekete C, Mitchell S, Cherkasova V, Applefield D, Algire M, Maag D, et al. N- and C-terminal residues of eIF1A have opposing effects on the fidelity of start codon selection. EMBO J. 2007;26:1602-14 pubmed
    ..We conclude that tight binding of eIF1A to the PIC is an important determinant of AUG selection and is modulated in opposite directions by residues in the NTT and CTT of eIF1A. ..
  8. Lomakin I, Shirokikh N, Yusupov M, Hellen C, Pestova T. The fidelity of translation initiation: reciprocal activities of eIF1, IF3 and YciH. EMBO J. 2006;25:196-210 pubmed
  9. Maag D, Fekete C, Gryczynski Z, Lorsch J. A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon. Mol Cell. 2005;17:265-75 pubmed
    ..These rearrangements probably play a role in triggering GTP hydrolysis and committing the complex to downstream events. ..
  10. Asano K, Clayton J, Shalev A, Hinnebusch A. A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNA(Met) is an important translation initiation intermediate in vivo. Genes Dev. 2000;14:2534-46 pubmed
    ..We propose that the multifactor complex is an important intermediate in translation initiation in vivo. ..
  11. Koivula T, Hemilä H. Nucleotide sequence of a Lactococcus lactis gene cluster encoding adenylate kinase, initiation factor 1 and ribosomal proteins. J Gen Microbiol. 1991;137:2595-600 pubmed
    ..subtilis. The putative promoter is located between adk and infA. ..
  12. Ozturk S, Kinzy T. Guanine nucleotide exchange factor independence of the G-protein eEF1A through novel mutant forms and biochemical properties. J Biol Chem. 2008;283:23244-53 pubmed publisher
    ..The biochemical properties of these eEF1A mutants provide insight into the mechanism behind GEF-independent G-protein function. ..
  13. Phan L, Zhang X, Asano K, Anderson J, Vornlocher H, Greenberg J, et al. Identification of a translation initiation factor 3 (eIF3) core complex, conserved in yeast and mammals, that interacts with eIF5. Mol Cell Biol. 1998;18:4935-46 pubmed
    ..Thus, eIF5 and Sui1p may be recruited to the 40S ribosomes through physical interactions with the Nip1p subunit of eIF3. ..
  14. Conte M, Kelly G, Babon J, Sanfelice D, Youell J, Smerdon S, et al. Structure of the eukaryotic initiation factor (eIF) 5 reveals a fold common to several translation factors. Biochemistry. 2006;45:4550-8 pubmed
    ..These results reveal a novel protein fold common to several factors involved in related steps of translation initiation. The implications of these observations are discussed in terms of the mechanism of translation initiation. ..
  15. De Sousa P, Watson A, Schultz R. Transient expression of a translation initiation factor is conservatively associated with embryonic gene activation in murine and bovine embryos. Biol Reprod. 1998;59:969-77 pubmed
    ..Our results suggest that transient expression of eIF-1A in the mouse and cow is a conserved pattern of gene expression associated with EGA in mammals. ..
  16. Pineda Lucena A, Yi G, Chang X, Cort J, Kennedy M, Edwards A, et al. Solution structure of the hypothetical protein MTH0637 from Methanobacterium thermoautotrophicum. J Biomol NMR. 2002;22:291-4 pubmed
  17. Yamamoto Y, Singh C, Marintchev A, Hall N, Hannig E, Wagner G, et al. The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4G. Proc Natl Acad Sci U S A. 2005;102:16164-9 pubmed
    ..These results indicate that the eIF5 HEAT domain is a critical nucleation core for preinitiation complex assembly and function. ..
  18. Fields C, Adams M. Expressed sequence tags identify a human isolog of the suil translation initiation factor. Biochem Biophys Res Commun. 1994;198:288-91 pubmed
    ..The identification of suilisol illustrates the utility of assemblies of independent ESTs for deriving full-length cDNA sequences for new human genes. ..
  19. Majumdar R, Maitra U. Regulation of GTP hydrolysis prior to ribosomal AUG selection during eukaryotic translation initiation. EMBO J. 2005;24:3737-46 pubmed
    ..These results, taken together, demonstrate the biochemical requirements for regulation of GTP hydrolysis and its coupling to the AUG selection process during translation initiation. ..
  20. Kleiman S, Yogev L, Hauser R, Botchan A, Maymon B, Paz G, et al. Expression profile of AZF genes in testicular biopsies of azoospermic men. Hum Reprod. 2007;22:151-8 pubmed
    ..The findings contribute to the search and selection of the most valuable gene markers potentially useful as additional tools for predicting complete spermatogenesis by multiplex expression analysis. ..
  21. Brock S, Szkaradkiewicz K, Sprinzl M. Initiation factors of protein biosynthesis in bacteria and their structural relationship to elongation and termination factors. Mol Microbiol. 1998;29:409-17 pubmed
    ..We present data that extend the mimicry hypothesis to initiation factors 1 and 2, originally postulated for the aminoacyl-tRNA x elongation factor Tu x GTP ternary complex, elongation factor G and release factors. ..
  22. Johnson K, Cruickshank R, Adams R, Smith V, Page R, Clayton D. Dramatically elevated rate of mitochondrial substitution in lice (Insecta: Phthiraptera). Mol Phylogenet Evol. 2003;26:231-42 pubmed
    ..Relative rate estimates also increase with model complexity, indicating that methods accounting for more multiple substitution estimate higher relative rates. ..
  23. Myrick K, Dearolf C. Hyperactivation of the Drosophila Hop jak kinase causes the preferential overexpression of eIF1A transcripts in larval blood cells. Gene. 2000;244:119-25 pubmed
    ..Our results support the model that D-eIF1A is one of the target genes through which the Drosophila Jak kinase pathway regulates hemocyte development. ..
  24. Yu Y, Marintchev A, Kolupaeva V, Unbehaun A, Veryasova T, Lai S, et al. Position of eukaryotic translation initiation factor eIF1A on the 40S ribosomal subunit mapped by directed hydroxyl radical probing. Nucleic Acids Res. 2009;37:5167-82 pubmed publisher
    ..In contrast, eIF1A-CTT appears to interfere with the P-site tRNA-head interaction in the 'closed' complex and is likely ejected from the P-site upon start codon recognition...
  25. Low P, Talián G, Sass M. Up- and downregulated genes in muscles that undergo developmentally programmed cell death in the insect Manduca sexta. FEBS Lett. 2005;579:4943-8 pubmed
    ..Expression of these genes had not been previously reported to be altered in dying ISMs. An ecdysteroid agonist, RH-5849, that prevented PCD in ISMs also blocked these changes. ..
  26. Mateyak M, Kinzy T. eEF1A: thinking outside the ribosome. J Biol Chem. 2010;285:21209-13 pubmed publisher
    ..A mechanistic understanding of these non-canonical functions of eEF1A will shed light on many important biological questions, including viral-host interaction, subcellular organization, and the integration of key cellular pathways. ..
  27. Celano B, Pawlik R, Gualerzi C. Interaction of Escherichia coli translation-initiation factor IF-1 with ribosomes. Eur J Biochem. 1988;178:351-5 pubmed
  28. Weber M, Beckering C, Marahiel M. Complementation of cold shock proteins by translation initiation factor IF1 in vivo. J Bacteriol. 2001;183:7381-6 pubmed
    ..Two of the possible explanation models are discussed. ..
  29. Nanda J, Cheung Y, Takacs J, Martin Marcos P, Saini A, Hinnebusch A, et al. eIF1 controls multiple steps in start codon recognition during eukaryotic translation initiation. J Mol Biol. 2009;394:268-85 pubmed publisher
    ..Our data indicate that eIF1 plays multiple roles in start codon recognition and suggest that prior to AUG recognition it prevents eIF5 from binding to a key site in the PIC required for triggering downstream events. ..
  30. Nagashima K, Kasai M, Nagata S, Kaziro Y. Structure of the two genes coding for polypeptide chain elongation factor 1 alpha (EF-1 alpha) from Saccharomyces cerevisiae. Gene. 1986;45:265-73 pubmed
    ..The sequence which commonly exists in the 5'-flanking regions of ribosomal protein genes of S. cerevisiae was also present in the two EF1 alpha genes. ..
  31. Chaudhuri J, Chowdhury D, Maitra U. Distinct functions of eukaryotic translation initiation factors eIF1A and eIF3 in the formation of the 40 S ribosomal preinitiation complex. J Biol Chem. 1999;274:17975-80 pubmed
    ..eIF2.GTP to 40 S subunits, and eIF3 stabilizing the resulting complex and preventing its disruption by 60 S ribosomal subunits. ..
  32. Ganoza M, Aoki H, Burkhardt N, Murphy B. The ribosome as affinity matrix': efficient purification scheme for translation factors. Biochimie. 1996;78:51-61 pubmed
    ..The procedure markedly simplifies the isolation, in homogeneous form, of all the non-ribosomal proteins required to reconstruct translation. ..
  33. Kapralou S, Fabbretti A, Garulli C, Gualerzi C, Pon C, Spurio R. Characterization of Bacillus stearothermophilus infA and of its product IF1. Gene. 2009;428:31-5 pubmed publisher
    ..stearothermophilus IF1 now allows us to analyze the translation initiation pathway using efficient in vitro tests based entirely on purified components derived from this thermophilic Gram-positive bacterium. ..
  34. Majumdar R, Bandyopadhyay A, Maitra U. Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40 S preinitiation complex. J Biol Chem. 2003;278:6580-7 pubmed
    ..These studies suggest that it is possible for eIF1 and eIF1A to bind the 40 S preinitiation complex prior to mRNA binding. ..
  35. Cummings H, Sands J, Foreman P, Fraser J, Hershey J. Structure and expression of the infA operon encoding translational initiation factor IF1. Transcriptional control by growth rate. J Biol Chem. 1991;266:16491-8 pubmed
    ..Therefore, metabolic control of infA expression occurs exclusively at the level of transcription by the P2 promoter. ..
  36. Kageyama S, Nagata M, Aoki F. Isolation of nascent messenger RNA from mouse preimplantation embryos. Biol Reprod. 2004;71:1948-55 pubmed
    ..The amount of each transcript in the nascent mRNA fraction and in the total mRNA pool changed differently over time, demonstrating that this method can be used to obtain profiles of genes transcribed during development. ..
  37. Cao L, Lin Q, Li X. [Proteomic study of paclitaxel on human cervical carcinoma HCE1]. Zhong Nan Da Xue Xue Bao Yi Xue Ban. 2008;33:512-7 pubmed
    ..These proteins may be involved in the proliferation inhibition of human cervical carcinoma cells by paclitaxel. ..
  38. Spurio R, Paci M, Pawlik R, La Teana A, DiGiacco B, Pon C, et al. Site-directed mutagenesis and NMR spectroscopic approaches to the elucidation of the structure-function relationships in translation initiation factors IF1 and IF3. Biochimie. 1991;73:1001-6 pubmed
  39. Magnani L, Cabot R. Manipulation of SMARCA2 and SMARCA4 transcript levels in porcine embryos differentially alters development and expression of SMARCA1, SOX2, NANOG, and EIF1. Reproduction. 2009;137:23-33 pubmed publisher
    ..Our data strongly support the hypothesis that SMARCA2 and SMARCA4 play different but fundamental roles controlling gene expression during early mammalian embryogenesis. ..
  40. Yamamoto H, Nakashima N, Ikeda Y, Uchiumi T. Binding mode of the first aminoacyl-tRNA in translation initiation mediated by Plautia stali intestine virus internal ribosome entry site. J Biol Chem. 2007;282:7770-6 pubmed
    ..This conformational change caused by the PSIV-IRES may be responsible for the activation of eEF2 action and stimulation of the first tRNA binding to the P site without initiation factors. ..
  41. Terenin I, Dmitriev S, Andreev D, Royall E, Belsham G, Roberts L, et al. A cross-kingdom internal ribosome entry site reveals a simplified mode of internal ribosome entry. Mol Cell Biol. 2005;25:7879-88 pubmed
    ..We suggest that the single-stranded nature of the RhPV IRES accounts for its strong but less selective potential to bind key mRNA recruiting components of the translation initiation apparatus from diverse origins. ..
  42. Yamaji Y, Kobayashi T, Hamada K, Sakurai K, Yoshii A, Suzuki M, et al. In vivo interaction between Tobacco mosaic virus RNA-dependent RNA polymerase and host translation elongation factor 1A. Virology. 2006;347:100-8 pubmed
    ..The methyltransferase domain of TMV RdRp was indicated to be responsible for the interaction with eEF1A in vitro and in yeast. These results suggest that eEF1A is a component of the virus replication complex of TMV. ..
  43. Bulygin K, Repkova M, Ven yaminova A, Graifer D, Karpova G, Frolova L, et al. Positioning of the mRNA stop signal with respect to polypeptide chain release factors and ribosomal proteins in 80S ribosomes. FEBS Lett. 2002;514:96-101 pubmed
  44. Gilbert R, Gordiyenko Y, von der Haar T, Sonnen A, Hofmann G, Nardelli M, et al. Reconfiguration of yeast 40S ribosomal subunit domains by the translation initiation multifactor complex. Proc Natl Acad Sci U S A. 2007;104:5788-93 pubmed
    ..This is expected to increase the accessibility of the mRNA channel, thus enabling the 40S subunit to convert to a recruitment-competent state. ..
  45. Sørensen H, Hedegaard J, Sperling Petersen H, Mortensen K. Remarkable conservation of translation initiation factors: IF1/eIF1A and IF2/eIF5B are universally distributed phylogenetic markers. IUBMB Life. 2001;51:321-7 pubmed
    ..Because of these two application levels, IF1/eIF1A-IF2/eIF5B is a phylogenetic "dual level" marker. ..
  46. Wang Q, Chung Y, deVries W, Struwe M, Latham K. Role of protein synthesis in the development of a transcriptionally permissive state in one-cell stage mouse embryos. Biol Reprod. 2001;65:748-54 pubmed
  47. Kjaer S, Wind T, Ravn P, Østergaard M, Clark B, Nissim A. Generation and epitope mapping of high-affinity scFv to eukaryotic elongation factor 1A by dual application of phage display. Eur J Biochem. 2001;268:3407-15 pubmed
    ..In both cases a perinuclear localization of hEF1A was observed. No evidence for the reported nuclear localization of hEF1A was obtained. ..
  48. Rosmond R, Chagnon Y, Holm G, Chagnon M, Perusse L, Lindell K, et al. A glucocorticoid receptor gene marker is associated with abdominal obesity, leptin, and dysregulation of the hypothalamic-pituitary-adrenal axis. Obes Res. 2000;8:211-8 pubmed
    ..An abnormal control of HPA axis function due to genetic alterations may contribute to the pathogenesis of abdominal obesity. ..
  49. Tachibana H. Green tea polyphenol EGCG signaling pathway through the 67-kDa laminin receptor. Nihon Yakurigaku Zasshi. 2008;132:145-9 pubmed publisher
  50. Sijben Müller G, Hallick R, Alt J, Westhoff P, Herrmann R. Spinach plastid genes coding for initiation factor IF-1, ribosomal protein S11 and RNA polymerase alpha-subunit. Nucleic Acids Res. 1986;14:1029-44 pubmed
    ..The genes are transcribed in vivo and appear to encode functional proteins. These findings imply that plastid chromosomes code for components of the organelle transcription apparatus. ..
  51. Fraser C, Berry K, Hershey J, Doudna J. eIF3j is located in the decoding center of the human 40S ribosomal subunit. Mol Cell. 2007;26:811-9 pubmed
    ..These results suggest that eIF3j functions in part by regulating access of the mRNA-binding cleft in response to initiation factor binding. ..
  52. Reibarkh M, Yamamoto Y, Singh C, del Rio F, Fahmy A, Lee B, et al. Eukaryotic initiation factor (eIF) 1 carries two distinct eIF5-binding faces important for multifactor assembly and AUG selection. J Biol Chem. 2008;283:1094-103 pubmed
    ..Thus, eIF5 is an excellent candidate for the direct partner of eIF1-KH that mediates the critical link. The direct interaction at eIF1-KH also places eIF5 near the decoding site of the 40 S subunit. ..
  53. Nagel K, Voigt J. An inhibitor of elongation factor G (EF-G) GTPase present in the ribosome wash of Escherichia coli: a complex of initiation factors IF1 and IF3?. Biochim Biophys Acta. 1992;1129:145-8 pubmed
    ..Therefore, IF1 as well as the EF-G GTPase inhibitor do not influence the ribosome-dependent EF-G GTPase by affecting the association of ribosomal subunits. ..
  54. Langdon J, Vonakis B, MacDonald S. Identification of the interaction between the human recombinant histamine releasing factor/translationally controlled tumor protein and elongation factor-1 delta (also known as eElongation factor-1B beta). Biochim Biophys Acta. 2004;1688:232-6 pubmed
    ..Our findings of an interaction between HrHRF and EF-1delta taken with some of the recently published information concerning the TCTP (HrHRF) mentioned above suggest a possible intracellular role for TCTP/HrHRF. ..
  55. Metz A, Timmer R, Allen M, Browning K. Sequence of a cDNA encoding the alpha-subunit of wheat translation elongation factor 1. Gene. 1992;120:315-6 pubmed
    ..The deduced amino acid sequence is compared to EF-1 alpha from other species and to elongation factor Tu (EF-Tu) from Escherichia coli. Putative GTP-binding sites are identified. ..
  56. Pestova T, Lomakin I, Lee J, Choi S, Dever T, Hellen C. The joining of ribosomal subunits in eukaryotes requires eIF5B. Nature. 2000;403:332-5 pubmed
    ..It is a homologue of the prokaryotic initiation factor IF2 (re and, like it, mediates joining of subunits and has a ribosome-dependent GTPase activity that is essential for its function. ..
  57. Rausell A, Kanhonou R, Yenush L, Serrano R, Ros R. The translation initiation factor eIF1A is an important determinant in the tolerance to NaCl stress in yeast and plants. Plant J. 2003;34:257-67 pubmed
    ..Finally, transgenic Arabidopsis plants expressing BveIF1A exhibited increased tolerance to NaCl. These results suggest that the translation initiation factor eIF1A is an important determinant of sodium tolerance in yeast and plants. ..
  58. Naranda T, MacMillan S, Donahue T, Hershey J. SUI1/p16 is required for the activity of eukaryotic translation initiation factor 3 in Saccharomyces cerevisiae. Mol Cell Biol. 1996;16:2307-13 pubmed
  59. Mingot J, Kostka S, Kraft R, Hartmann E, Gorlich D. Importin 13: a novel mediator of nuclear import and export. EMBO J. 2001;20:3685-94 pubmed
  60. Davis W, De Sousa P, Schultz R. Transient expression of translation initiation factor eIF-4C during the 2-cell stage of the preimplantation mouse embryo: identification by mRNA differential display and the role of DNA replication in zygotic gene activation. Dev Biol. 1996;174:190-201 pubmed
    ..Results of these experiments suggest that the first round of DNA replication is permissive with respect to ZGA and that the second round is repressive. ..
  61. Sheikh M, Fernandez Salas E, Yu M, Hussain A, Dinman J, Peltz S, et al. Cloning and characterization of a human genotoxic and endoplasmic reticulum stress-inducible cDNA that encodes translation initiation factor 1(eIF1(A121/SUI1)). J Biol Chem. 1999;274:16487-93 pubmed
  62. Mitchell S, Lorsch J. Should I stay or should I go? Eukaryotic translation initiation factors 1 and 1A control start codon recognition. J Biol Chem. 2008;283:27345-9 pubmed publisher
    ..Both factors perform their tasks through a variety of interactions with other components of the initiation machinery, in many cases mediated by the unstructured regions of the two proteins. ..
  63. Phan L, Schoenfeld L, VALASEK L, Nielsen K, Hinnebusch A. A subcomplex of three eIF3 subunits binds eIF1 and eIF5 and stimulates ribosome binding of mRNA and tRNA(i)Met. EMBO J. 2001;20:2954-65 pubmed
    ..Thus, several key functions of eIF3 can be carried out by the PRT1-TIF32-NIP1 subcomplex. ..
  64. Metz A, Browning K. Assignment of the beta-subunit of wheat eIF2 by protein and DNA sequence analysis and immunoanalysis. Arch Biochem Biophys. 1997;342:187-9 pubmed
    ..Only the p38 subunit of purified wheat germ eIF2 reacted with the antisera. The p38 subunit of wheat eIF2 is therefore the equivalent of mammalian eIF2beta. ..
  65. Kwon S, Lee I, Kim N, Choi D, Oh Y, Bae S. Translation initiation factor eIF1A possesses RNA annealing activity in its oligonucleotide-binding fold. Biochem Biophys Res Commun. 2007;361:681-6 pubmed
    ..Our results indicate that eIF1A may function as an RNA chaperone, inducing conformational changes in rRNA in the 43S preinitiation complex. ..
  66. Hu S, Li Y, Liu G, Song Q, Wang L, Han Y, et al. A protein chip approach for high-throughput antigen identification and characterization. Proteomics. 2007;7:2151-61 pubmed
    ..Among them, we discovered that eIF1A expressed only in normal liver tissues, not in hepatocellular carcinoma in humans. ..
  67. Cummings H, Hershey J. Translation initiation factor IF1 is essential for cell viability in Escherichia coli. J Bacteriol. 1994;176:198-205 pubmed
    ..Cells depleted of IF1 exhibit few polysomes, suggesting that IF1 functions in the initiation phase of protein synthesis. ..
  68. Soudet J, Gelugne J, Belhabich Baumas K, Caizergues Ferrer M, Mougin A. Immature small ribosomal subunits can engage in translation initiation in Saccharomyces cerevisiae. EMBO J. 2010;29:80-92 pubmed publisher
  69. Schneider H, Dabauvalle M, Wilken N, Scheer U. Visualizing protein interactions involved in the formation of the 42S RNP storage particle of Xenopus oocytes. Biol Cell. 2010;102:469-78 pubmed publisher
  70. Ivanov I, Loughran G, Sachs M, Atkins J. Initiation context modulates autoregulation of eukaryotic translation initiation factor 1 (eIF1). Proc Natl Acad Sci U S A. 2010;107:18056-60 pubmed publisher
    ..Elaborate cellular machinery exists to ensure the fidelity of start codon selection. Eukaryotic initiation factor 1 (eIF1) plays a central role in this process...
  71. Moody C, Scott R, Amirghahari N, Nathan C, Young L, Dawson C, et al. Modulation of the cell growth regulator mTOR by Epstein-Barr virus-encoded LMP2A. J Virol. 2005;79:5499-506 pubmed
    ..Intervention by this DNA tumor virus in cellular translational controls is likely to be an integral component of EBV tumorigenesis. ..
  72. Cort J, Koonin E, Bash P, Kennedy M. A phylogenetic approach to target selection for structural genomics: solution structure of YciH. Nucleic Acids Res. 1999;27:4018-27 pubmed
    ..Thus, the phylogenetic approach to target selection described here was used successfully to identify a new homologous superfamily within this topology. ..
  73. Cheung Y, Maag D, Mitchell S, Fekete C, Algire M, Takacs J, et al. Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo. Genes Dev. 2007;21:1217-30 pubmed
  74. Kainuma M, Hershey J. Depletion and deletion analyses of eucaryotic translation initiation factor 1A in Saccharomyces cerevisiae. Biochimie. 2001;83:505-14 pubmed
    ..Therefore the charged terminal regions contribute to, but are not absolutely essential for, eIF1A function. ..
  75. Maag D, Lorsch J. Communication between eukaryotic translation initiation factors 1 and 1A on the yeast small ribosomal subunit. J Mol Biol. 2003;330:917-24 pubmed
    ..The data presented here provide a foundation on which to build a quantitative understanding of the network of interactions between these essential factors and the rest of the initiation machinery. ..
  76. Pittman Y, Valente L, Jeppesen M, Andersen G, Patel S, Kinzy T. Mg2+ and a key lysine modulate exchange activity of eukaryotic translation elongation factor 1B alpha. J Biol Chem. 2006;281:19457-68 pubmed
    ..These results indicate the significant role of Mg2+ in the nucleotide exchange reaction by eEF1B alpha and establish the catalytic function of Lys-205 in displacing Mg2+ from its binding site. ..
  77. Acker M, Kolitz S, Mitchell S, Nanda J, Lorsch J. Reconstitution of yeast translation initiation. Methods Enzymol. 2007;430:111-45 pubmed
    ..1998; Trachsel et al., 1977). The following describes methods for synthesizing and purifying the components of the yeast initiation system and assays useful for its characterization. ..
  78. Kolitz S, Takacs J, Lorsch J. Kinetic and thermodynamic analysis of the role of start codon/anticodon base pairing during eukaryotic translation initiation. RNA. 2009;15:138-52 pubmed publisher
    ..This induced-fit mechanism supports the proposal that initiation codon recognition by the 43S complex induces a conformational change from an open state to a closed one that arrests movement along the mRNA. ..
  79. Oropeza A, Wrenzycki C, Herrmann D, Hadeler K, Niemann H. Improvement of the developmental capacity of oocytes from prepubertal cattle by intraovarian insulin-like growth factor-I application. Biol Reprod. 2004;70:1634-43 pubmed
  80. VALASEK L, Nielsen K, Zhang F, Fekete C, Hinnebusch A. Interactions of eukaryotic translation initiation factor 3 (eIF3) subunit NIP1/c with eIF1 and eIF5 promote preinitiation complex assembly and regulate start codon selection. Mol Cell Biol. 2004;24:9437-55 pubmed
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