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// Workers AI · dad joke modeWhat did EIF3J say to its friend? "You translate to a good time

From Wikipedia, the free encyclopedia

EIF3J
Identifiers
AliasesEIF3J, EIF3S1, eIF3-alpha, eIF3-p35, eukaryotic translation initiation factor 3 subunit J
External IDsOMIM: 603910; MGI: 3704486; GeneCards: EIF3J
Available structures
PDBOrtholog search: PDBe RCSB
Orthologs
DatabasesNCBI: entry; OMA: entry
SpeciesHumanMouse
Entrez

8669

100042807

Ensembl

ENSG00000104131

ENSMUSG00000043424

UniProt

O75822

Q66JS6

RefSeq (mRNA)

NM_003758
NM_001284335
NM_001284336

NM_001256055

RefSeq (protein)

NP_001271264
NP_001271265
NP_003749

NP_001242984

Location (UCSC)Chr 15: 44.54 – 44.56 MbChr 18: 43.61 – 43.61 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Eukaryotic translation initiation factor 3 subunit J (eIF3j) is a protein that in humans is encoded by the EIF3J gene.[5][6] It is implicated in translation initiation and recycling.[7][8]

Structure

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The crystal structure of the C-terminal part of human eIF3j was determined in the scope of the Structural Genomics Consortium and showed that it consists of a 6-helix bundle.[9] eIF3j has subsequently been visualized as part of ribosomal translation initiation complexes, both for human[10][11][12] and yeast eIF3j.[12][13] The general binding location is similar for both species, located at the A-site between eIF1A and helix 16 of the ribosomal small subunit. However, differences are apparent in the arrangement of the C-terminal helix bundle and its rotation. The N-terminal part of eIF3j was visualized only in the context of a yeast pre-initiation complex, showing that it binds the entry of the mRNA tunnel.[13]

Function

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Eukaryotic translation initiation factor 3 subunit J is reported to play an important role in the assembly of the 43S pre-initiation complex. It specifically binds to the 40S subunit in vitro[14][15] and increases the affinity of eIF3 to the small subunit.[14] The binding of eIF3j to the small subunit occurs in an anticooperative fashion with eIF1, eIF1A, and the ternary complex of eIF2, tRNA, and GTP. However, eIF3 reduces the negative cooperativity strongly.[16]

eIF3j's N-terminal part binds the mRNA channel[17][13] and has been shown to reduce the mRNA's affinity to the ribosomal small subunit,[17][18]thus preventing translation initiation to progress. The ternary complex is essential to reduce eIF3j's affinity for the 43S pre-initiation complex and therefore to allow binding of mRNA. However, despite the presence of eIF3j, mRNA may still be able to bind in a pre-accommodated state in presence of eIF4A,[18] meaning that the mRNA partially occupies the mRNA channel but is not in its final position.

Start codon selection is reported to be effected by eIF3j, as knock-out of eIF3j leads to less stringent selection of start codons[19]

The activity of eIF3j may be regulated by phosphorylation by CK2[20] and through cleavage by caspase-3.[14]

See also

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References

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  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000104131 – Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000043424 – Ensembl, May 2017
  3. ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ↑ Block KL, Vornlocher HP, Hershey JW (December 1998). "Characterization of cDNAs encoding the p44 and p35 subunits of human translation initiation factor eIF3". The Journal of Biological Chemistry. 273 (48): 31901–31908. doi:10.1074/jbc.273.48.31901. PMID 9822659.
  6. ↑ "Entrez Gene: EIF3S1 eukaryotic translation initiation factor 3, subunit 1 alpha, 35kDa".
  7. ↑ Merrick WC, Pavitt GD (December 2018). "Protein Synthesis Initiation in Eukaryotic Cells". Cold Spring Harbor Perspectives in Biology. 10 (12) a033092. doi:10.1101/cshperspect.a033092. PMC 6280705. PMID 29735639.
  8. ↑ Hellen CU (October 2018). "Translation Termination and Ribosome Recycling in Eukaryotes". Cold Spring Harbor Perspectives in Biology. 10 (10) a032656. doi:10.1101/cshperspect.a032656. PMC 6169810. PMID 29735640.
  9. ↑ Tempel W, Nedyalkova L, Hong B, MacKenzie F, Arrowsmith CH, Edwards AM, et al. (2008). Crystal structure of human translation initiation factor 3, subunit 1 alpha (Report). The Protein Databank. doi:10.2210/pdb3bpj/pdb.
  10. ↑ Aylett CH, Boehringer D, Erzberger JP, Schaefer T, Ban N (March 2015). "Structure of a yeast 40S-eIF1-eIF1A-eIF3-eIF3j initiation complex". Nature Structural & Molecular Biology. 22 (3): 269–271. doi:10.1038/nsmb.2963. PMID 25664723.
  11. ↑ Brito Querido J, Sokabe M, Kraatz S, Gordiyenko Y, Skehel JM, Fraser CS, et al. (September 2020). "Structure of a human 48S translational initiation complex". Science. 369 (6508). New York, N.Y.: 1220–1227. doi:10.1126/science.aba4904. PMC 7116333. PMID 32883864.
  12. 1 2 Kratzat H, MacKens-Kiani T, Ameismeier M, Potocnjak M, Cheng J, Dacheux E, et al. (January 2021). "A structural inventory of native ribosomal ABCE1-43S pre-initiation complexes". The EMBO Journal. 40 (1) EMBJ2020105179. doi:10.15252/embj.2020105179. PMC 7780240. PMID 33289941.
  13. 1 2 3 Ikeuchi K, Ivic N, Buschauer R, Cheng J, Fröhlich T, Matsuo Y, et al. (May 2023). "Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2". Nature Communications. 14 (1) 2730. doi:10.1038/s41467-023-38161-w. PMC 10175282. PMID 37169754.
  14. 1 2 3 Fraser CS, Lee JY, Mayeur GL, Bushell M, Doudna JA, Hershey JW (March 2004). "The j-subunit of human translation initiation factor eIF3 is required for the stable binding of eIF3 and its subcomplexes to 40 S ribosomal subunits in vitro". The Journal of Biological Chemistry. 279 (10): 8946–8956. doi:10.1074/jbc.M312745200. PMID 14688252.
  15. ↑ Elantak L, Tzakos AG, Locker N, Lukavsky PJ (2007). "Structure of eIF3b RNA Recognition Motif and Its Interaction with eIF3j". Journal of Biological Chemistry. 282 (11): 8165–8174. doi:10.1074/jbc.M610860200. PMID 17190833.
  16. ↑ Sokabe M, Fraser CS (November 2014). "Human eukaryotic initiation factor 2 (eIF2)-GTP-Met-tRNAi ternary complex and eIF3 stabilize the 43 S preinitiation complex". The Journal of Biological Chemistry. 289 (46): 31827–31836. doi:10.1074/jbc.M114.602870. PMC 4231660. PMID 25246524.
  17. 1 2 Fraser CS, Berry KE, Hershey JW, Doudna JA (June 2007). "eIF3j is located in the decoding center of the human 40S ribosomal subunit". Molecular Cell. 26 (6): 811–819. doi:10.1016/j.molcel.2007.05.019. PMID 17588516.
  18. 1 2 Sokabe M, Fraser CS (June 2017). "A helicase-independent activity of eIF4A in promoting mRNA recruitment to the human ribosome". Proceedings of the National Academy of Sciences of the United States of America. 114 (24): 6304–6309. doi:10.1073/pnas.1620426114. PMC 5474785. PMID 28559306.
  19. ↑ Elantak L, Wagner S, Herrmannová A, Karásková M, Rutkai E, Lukavsky PJ, et al. (March 2010). "The indispensable N-terminal half of eIF3j/HCR1 cooperates with its structurally conserved binding partner eIF3b/PRT1-RRM and with eIF1A in stringent AUG selection". Journal of Molecular Biology. 396 (4): 1097–1116. doi:10.1016/j.jmb.2009.12.047. PMC 2824034. PMID 20060839.
  20. ↑ Borgo C, Franchin C, Salizzato V, Cesaro L, Arrigoni G, Matricardi L, et al. (July 2015). "Protein kinase CK2 potentiates translation efficiency by phosphorylating eIF3j at Ser127". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1853 (7): 1693–1701. doi:10.1016/j.bbamcr.2015.04.004. PMID 25887626.

Further reading

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[edit]
  • Overview of all the structural information available in the PDB for UniProt: O75822 (Human Eukaryotic translation initiation factor 3 subunit J (EIF3J)) at the PDBe-KB.
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