Gene Name | EIF4G2 |
HF Protein Name | Eukaryotic translation initiation factor 4 gamma 2 |
HF Function | Essential for viral DNA replication |
Uniprot ID | P78344 |
Protein Sequence | View Fasta Sequence |
NCBI Gene ID | 1982 |
Host Factor (HF) Name in Paper | eIF4GII |
Gene synonyms | DAP5 |
Ensemble Gene ID | ENSG00000110321 |
Ensemble Transcript | ENST00000640650 [P78344-1] |
KEGG ID | Go to KEGG Database |
Gene Ontology ID(s) | GO:0003723, GO:0003743, GO:0005829, GO:0005913, GO:0006446, GO:0007050, GO:0008135, GO:0008219, GO:0010507, GO:0016020, GO:0016281, GO:0030307, GO:0034645, GO:0045296, |
MINT ID | P78344 |
STRING | Click to see interaction map |
GWAS Analysis | Click to see gwas analysis |
OMIM ID | 602325 |
PANTHER ID | N.A. |
PDB ID(s) | 3D3M, 3L6A, 4IUL, |
pfam ID | PF02847, PF02854, PF02020, |
Drug Bank ID | N.A., |
ChEMBL ID | N.A. |
Organism | Homo sapiens (Human) |
Virus Name | Vaccinia Virus |
Virus Short Name | VACV |
Order | Unassigned |
Virus Family | Poxviridae |
Virus Subfamily | Chordopoxvirinae |
Genus | Orthopoxvirus |
Species | Vaccinia virus |
Host | Human, mammals |
Cell Tropism | Dendritic cells, monocytes/macrophages, b lymphocytes, activated t lymphocytes |
Associated Disease | N.A. |
Mode of Transmission | N.A. |
VIPR DB link | https://www.viprbrc.org/brc/home.spg?decorator=pox |
ICTV DB link | https://talk.ictvonline.org/ictv-reports/ictv_9th_report/dsdna-viruses-2011/w/dsdna_viruses/74/poxviridae |
Virus Host DB link | http://www.genome.jp/virushostdb/view/?virus_lineage=Poxviridae |
Paper Title | Translation of mRNAs from vesicular stomatitis virus and vaccinia virus is differentially blocked in cells with depletion of eIF4GI and/or eIF4GII |
Author's Name | Ewelina Welnowska, Alfredo Castello, Pablo Moral and Luis Carrasco |
Journal Name | Journal Of Molecular Biology |
Pubmed ID | 19769989 |
Abstract | Cytolytic viruses abrogate host protein synthesis to maximize the translation of their own mRNAs. In this study, we analyzed the eukaryotic initiation factor (eIF) 4G requirement for translation of vesicular stomatitis virus (VSV) and vaccinia virus (VV) mRNAs in HeLa cells using two different strategies: eIF4G depletion by small interfering RNAs or cleavage of eIF4G by expression of poliovirus 2A protease. Depletion of eIF4GI or eIF4GII moderately inhibits cellular protein synthesis, whereas silencing of both factors has only a slightly higher effect. Under these conditions, the extent of VSV protein synthesis is similar to that of nondepleted control cells, whereas VV expression is substantially reduced. Similar results were obtained when eIF4E was depleted. On the other hand, eIF4G cleavage by poliovirus 2A protease strongly inhibits translation of VV protein expression, whereas translation directed by VSV mRNAs is not abrogated, even though VSV mRNAs are capped. Therefore, the requirement for eIF4F activity is different for VV and VSV, suggesting that the molecular mechanism by which their mRNAs initiate their translation is also different. Consistent with these findings, eIF4GI does not colocalize with ribosomes in VSV-infected cells, while eIF2alpha locates at perinuclear sites coincident with ribosomes. |
Used Model | HeLa cells |
DOI | 10.1016/j.jmb.2009.09.036 |