Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3)

Proceedings of the National Academy of Sciences of the United States of America

Volumn 108, Issue 51, 2011, Pages 20473-20478

  Sun, Chaomin ^a   Todorovic, Aleksandar ^a   Querol Audí, Jordi ^a   Bai, Yun ^b   Villa, Nancy ^c   Snyder, Monica ^b   Ashchyan, John ^b   Lewis, Christopher S ^b   Hartland, Abbey ^a   Gradia, Scott ^a   Fraser, Christopher S ^c   Doudna, Jennifer A ^b,d   Nogales, Eva ^b,d   Cate, Jamie H D ^b,d  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d LAWRENCE BERKELEY NATIONAL LABORATORY   (United States)

Author keywords

Electron microscopy; Protein synthesis; Supramolecular complex assembly; Translation regulation

Indexed keywords

COP9 SIGNALOSOME; INITIATION FACTOR 3; MESSENGER RNA; PROTEASOME; RECOMBINANT PROTEIN;

ARTICLE; COMPLEX FORMATION; CONTROLLED STUDY; ESCHERICHIA COLI; HEPATITIS C VIRUS; HUMAN; INTERNAL RIBOSOME ENTRY SITE; MOLECULAR WEIGHT; NONHUMAN; ORTHOLOGY; PARTICLE SIZE; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN LIPID INTERACTION; PROTEIN MODIFICATION; PROTEIN RECONSTITUTION; PROTEIN STRUCTURE; PROTEIN SUBUNIT; RIBOSOME SUBUNIT; TRANSLATION INITIATION;

DNA, COMPLEMENTARY; ESCHERICHIA COLI; EUKARYOTIC INITIATION FACTOR-3; HELA CELLS; HEPACIVIRUS; HUMANS; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; MOLECULAR CONFORMATION; MULTIPROTEIN COMPLEXES; PEPTIDE HYDROLASES; PROTEIN BINDING; PROTEIN BIOSYNTHESIS; PROTEIN STRUCTURE, TERTIARY; RIBOSOMES; RNA, MESSENGER;

ESCHERICHIA COLI; EUKARYOTA; HEPATITIS C VIRUS;

EID: 84855492118     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1116821108     Document Type: Article

References (57)

1. Pick E, Hofmann K, Glickman MH (2009) PCI complexes: Beyond the proteasome, CSN, and eIF3 Troika. Mol Cell 35:260-264.
2. Sharon M, Taverner T, Ambroggio XI, Deshaies RJ, Robinson CV (2006) Structural organization of the 19S proteasome lid: Insights from MS of intact complexes. PLoS Biol 4:e267.
3. Zhou M, et al. (2008) Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3. Proc Natl Acad Sci USA 105:18139-18144.
4. Sharon M, et al. (2009) Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality. Structure 17:31-40.
5. Enchev RI, Schreiber A, Beuron F, Morris EP (2010) Structural insights into the COP9 signalosome and its common architecture with the 26S proteasome lid and eIF3. Structure 18:518-527.
6. Gallastegui N, GrollM(2010) The 26S proteasome: Assembly and function of a destructive machine. Trends Biochem Sci 35:634-642.
7. Moretti J, et al. (2010) The translation initiation factor 3f (eIF3f) exhibits a deubiquitinase activity regulating notch activation. PLoS Biol 8:e1000545.
8. Jackson RJ, Hellen CU, Pestova TV (2010) The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 11:113-127.
9. Damoc E, et al. (2007) Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometry. Mol Cell Proteomics 6:1135-1146. (Pubitemid 47099225)
10. Silvera D, Formenti SC, Schneider RJ (2010) Translational control in cancer. Nat Rev Cancer 10:254-266.
11. Honda M, et al. (1996) Structural requirements for initiation of translation by internal ribosome entry within genome-length hepatitis C virus RNA. Virology 222:31-42. (Pubitemid 26281356)
12. Kamoshita N, Tsukiyama-Kohara K, Kohara M, Nomoto A (1997) Genetic analysis of internal ribosomal entry site on hepatitis C virus RNA: Implication for involvement of the highly ordered structure and cell type-specific transacting factors. Virology 233:9-18. (Pubitemid 27348764)
13. Sizova DV, Kolupaeva VG, Pestova TV, Shatsky IN, Hellen CU (1998) Specific interaction of eukaryotic translation initiation factor 3 with the 5′ nontranslated regions of hepatitis C virus and classical swine fever virus RNAs. J Virol 72:4775-4782. (Pubitemid 28215653)
14. Kieft JS, et al. (1999) The hepatitis C virus internal ribosome entry site adopts an ion-dependent tertiary fold. J Mol Biol 292:513-529. (Pubitemid 29457315)
15. Fraser CS, Doudna JA (2007) Structural and mechanistic insights into hepatitis C viral translation initiation. Nat Rev Microbiol 5:29-38. (Pubitemid 44942301)
16. Pestova TV, Shatsky IN, Fletcher SP, Jackson RJ, Hellen CU (1998) A prokaryotic-like mode of cytoplasmic eukaryotic ribosome binding to the initiation codon during internal translation initiation of hepatitis C and classical swine fever virus RNAs. Genes Dev 12:67-83. (Pubitemid 28083659)
17. Fraser CS, Hershey JW, Doudna JA (2009) The pathway of hepatitis C virus mRNA recruitment to the human ribosome. Nat Struct Mol Biol 16:397-404.
18. Terenin IM, Dmitriev SE, Andreev DE, Shatsky IN (2008) Eukaryotic translation initiation machinery can operate in a bacterial-like mode without eIF2. Nat Struct Mol Biol 15:836-841.
19. Pestova TV, Hellen CU, Shatsky IN (1996) Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry. Mol Cell Biol 16:6859-6869. (Pubitemid 26389745)
20. Unbehaun A, Borukhov SI, Hellen CU, Pestova TV (2004) Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP. Genes Dev 18:3078-3093. (Pubitemid 39658176)
21. Fraser CS, et al. (2004) The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40S ribosomal subunits in vitro. J Biol Chem 279:8946-8956. (Pubitemid 38295956)
22. Masutani M, Sonenberg N, Yokoyama S, Imataka H (2007) Reconstitution reveals the functional core of mammalian eIF3. EMBO J 26:3373-3383. (Pubitemid 47123530)
23. Alkalaeva EZ, Pisarev AV, Frolova LY, Kisselev LL, Pestova TV (2006) In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell 125:1125-1136. (Pubitemid 43866201)
24. Siridechadilok B, Fraser CS, Hall RJ, Doudna JA, Nogales E (2005) Structural roles for human translation factor eIF3 in initiation of protein synthesis. Science 310:1513-1515. (Pubitemid 41746350)
25. Cai Q, et al. (2010) Distinct regions of human eIF3 are sufficient for binding to the HCV IRES and the 40S ribosomal subunit. J Mol Biol 403:185-196.
26. Verlhac MH, Chen RH, Hanachi P, Hershey JW, Derynck R (1997) Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation. EMBO J 16:6812-6822. (Pubitemid 27503493)
27. Asano K, Phan L, Anderson J, Hinnebusch AG (1998) Complex formation by all five homologues of mammalian translation initiation factor 3 subunits from yeast Saccharomyces cerevisiae. J Biol Chem 273:18573-18585. (Pubitemid 28334788)
28. Phan L, Schoenfeld LW, Valasek L, Nielsen KH, Hinnebusch AG (2001) A subcomplex of three eIF3 subunits binds eIF1 and eIF5 and stimulates ribosome binding of mRNA and tRNA(i)-Met. EMBO J 20:2954-2965. (Pubitemid 32938578)
29. Kolupaeva VG, Unbehaun A, Lomakin IB, Hellen CU, Pestova TV (2005) Binding of eukaryotic initiation factor 3 to ribosomal 40S subunits and its role in ribosomal dissociation and anti-association. RNA 11:470-486. (Pubitemid 40397180)
30. Fletcher CM, Pestova TV, Hellen CU, Wagner G (1999) Structure and interactions of the translation initiation factor eIF1. EMBO J 18:2631-2637. (Pubitemid 29213292)
31. Olsen DS, et al. (2003) Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo. EMBO J 22:193-204. (Pubitemid 36119425)
32. Majumdar R, Bandyopadhyay A, Maitra U (2003) Mammalian translation initiation factor eIF1 functions with eIF1A and eIF3 in the formation of a stable 40 S preinitiation complex. J Biol Chem 278:6580-6587. (Pubitemid 36800921)
33. Korneeva NL, Lamphear BJ, Hennigan FL, Rhoads RE (2000) Mutually cooperative binding of eukaryotic translation initiation factor (eIF) 3 and eIF4A to human eIF4G-1. J Biol Chem 275:41369-41376. (Pubitemid 32054972)
34. LeFebvre AK, et al. (2006) Translation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit. J Biol Chem 281:22917-22932.
35. Otto GA, Puglisi JD (2004) The pathway of HCV IRES-mediated translation initiation. Cell 119:369-380. (Pubitemid 39423839)
36. Mayeur GL, Fraser CS, Peiretti F, Block KL, Hershey JW (2003) Characterization of eIF3k: A newly discovered subunit of mammalian translation initiation factor elF3. Eur J Biochem 270:4133-4139. (Pubitemid 37281631)
37. Valasek L, et al. (2003) The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo. Genes Dev 17:786-799. (Pubitemid 36359196)
38. Chiu WL, et al. (2010) The C-terminal region of eukaryotic translation initiation factor 3a (eIF3a) promotes mRNA recruitment, scanning, and, together with eIF3j and the eIF3b RNA recognition motif, selection of AUG start codons. Mol Cell Biol 30:4415-4434.
39. Fraser CS, Berry KE, Hershey JW, Doudna JA (2007) eIF3j is located in the decoding center of the human 40S ribosomal subunit. Mol Cell 26:811-819. (Pubitemid 46921006)
40. Pisarev AV, Hellen CU, Pestova TV (2007) Recycling of eukaryotic posttermination ribosomal complexes. Cell 131:286-299. (Pubitemid 47576139)
41. Hinnebusch AG (2006) eIF3: A versatile scaffold for translation initiation complexes. Trends Biochem Sci 31:553-562.
42. Lomakin IB, Kolupaeva VG, Marintchev A, Wagner G, Pestova TV (2003) Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing. Genes Dev 17:2786-2797. (Pubitemid 37463288)
43. Yu Y, et al. (2009) Position of eukaryotic translation initiation factor eIF1A on the 40S ribosomal subunit mapped by directed hydroxyl radical probing. Nucleic Acids Res 37:5167-5182.
44. Rabl J, Leibundgut M, Ataide SF, Haag A, Ban N (2011) Crystal structure of the eukaryotic 40S ribosomal subunit in complex with initiation factor 1. Science 331:730-736.
45. Kato JY, Yoneda-Kato N (2009) Mammalian COP9 signalosome. Genes Cells 14:1209-1225.
46. Stadtmueller BM, Hill CP (2011) Proteasome activators. Mol Cell 41:8-19.
47. Kieft JS, Zhou K, Jubin R, Doudna JA (2001) Mechanism of ribosome recruitment by hepatitis C IRES RNA. RNA 7:194-206. (Pubitemid 33590503)
48. Aslanidis C, de Jong PJ (1990) Ligation-independent cloning of PCR products (LIC-PCR). Nucleic Acids Res 18:6069-6074.
49. Stols L, et al. (2002) A new vector for high-throughput, ligation-independent cloning encoding a tobacco etch virus protease cleavage site. Protein Expression Purif 25:8-15. (Pubitemid 36034995)
50. Lander GC, et al. (2009) Appion: An integrated, database-driven pipeline to facilitate EM image processing. J Struct Biol 166:95-102.
51. Mindell JA, Grigorieff N (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142:334-347. (Pubitemid 36638267)
52. Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for highresolution single-particle reconstructions. J Struct Biol 128:82-97. (Pubitemid 30013436)
53. Tang G, et al. (2007) EMAN2: An extensible image processing suite for electron microscopy. J Struct Biol 157:38-46. (Pubitemid 44880785)
54. Kozak M (1990) Evaluation of the fidelity of initiation of translation in reticulocyte lysates from commercial sources. Nucleic Acids Res 18:2828.
55. Berry KE, Waghray S, Doudna JA (2010) The HCV IRES pseudoknot positions the initiation codon on the 40S ribosomal subunit. RNA 16:1559-1569.
56. Sun C, Pager CT, Luo G, Sarnow P, Cate JHD (2010) Hepatitis C virus core-derived peptides inhibit genotype 1b viral genome replication via interaction with DDX3X. PLoS One 5:e12826.
57. Ikeda K, Arao Y, Otsuka H, Kikuchi A, Kayama F (2004) Estrogen and phytoestrogen regulate the mRNA expression of adrenomedullin and adrenomedullin receptor components in the rat uterus. Mol Cell Endocrinol 223:27-34. (Pubitemid 38992907)