Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0001486 (Adenovirus)
 3,125 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The transcriptional control elements of the Adenovirus (Ad) type 5 EIIA-late (L) promoter were analyzed in the context of the viral chromosome. Promoter mutants constructed in vitro [deletion and linker-scanning (LS)] were re-introduced into the non-essential EIII region of an Ad5 variant which lacked the EIA gene. They were then analyzed in human 293 cells for EIA-dependent and in HeLa cells for EIA-independent transcription. These studies revealed that a minimum of approximately 157 bp upstream from the Cap site are sufficient for the efficient transcription of this promoter in the presence or absence of the EIA gene products. Within the 157-bp sequence, multiple control elements can be identified. These are (i) a sequence block between -55 and -21 which contained a sequence resembling the TATA box and an Sp1 recognition site 5'-TGGGCGTGGT-3', (ii) a sequence block between -84 and -67 which contained a second Sp1 recognition sequence, 5'-CGGGCGGGAT-3' and a 5'-CCAAT-3' box in the non-coding strand and (iii) a 56-bp sequence block between -157 and -101 which contained a 5'-CCAAT-3' sequence in the non-coding strand. The transcriptional pattern of the LS mutants in 293 cells was very similar to that of HeLa cells suggesting that neither of the EIA gene products interact with EIIA-L promoter directly to modulate transcription. A purified Sp1 protein protected DNA sequences from -56 to -33 which includes the Sp1 recognition sequence closer to the cap site whereas the distal Sp1 recognition sequence showed a very weak affinity for the Sp1 factor.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:In vivo identification of multiple promoter domains of adenovirus EIIA-late promoter. 282 Jul 17

Earlier, targeting of DDX3 by few viral proteins has defined its role in mRNA transport and induction of interferon production. This study was conducted to investigate the function of bovine adenovirus (BAdV)-3 pVIII during virus infection. Here, we provided evidence regarding involvement of DDX3 in cap dependent cellular mRNA translation and demonstrated that targeting of DDX3 by adenovirus protein VIII interfered with cap-dependent mRNA translation function of DDX3 in virus infected cells. Adenovirus late protein pVIII interacted with DDX3 in transfected and BAdV-3 infected cells. pVIII inhibited capped mRNA translation in vitro and in vivo by limiting the amount of DDX3 and eIF3. Diminished amount of DDX3 and eIFs including eIF3, eIF4E, eIF4G, and PABP were present in cap binding complex in BAdV-3 infected or pVIII transfected cells with no trace of pVIII in cap binding complex. The total amount of eIFs appeared similar in uninfected or infected cells as BAdV-3 did not appear to degrade eIFs. The co-immunoprecipitation experiments indicated the absence of direct interaction between pVIII and eIF3, eIF4E, or PABP. These data indicate that interaction of pVIII with DDX3 interferes with the binding of eIF3, eIF4E and PABP to the 5' Cap. We conclude that DDX3 promotes cap-dependent cellular mRNA translation and BAdV-3 pVIII inhibits translation of capped cellular mRNA possibly by interfering with the recruitment of eIFs to the capped cellular mRNA.
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PMID:Bovine Adenovirus-3 pVIII Suppresses Cap-Dependent mRNA Translation Possibly by Interfering with the Recruitment of DDX3 and Translation Initiation Factors to the mRNA Cap. 2808 72