Abstract:
:Human T-cell leukemia virus type 1 (HTLV-1) is the etiological agent of adult T-cell leukemia (ATL). The HTLV-1 basic leucine zipper protein (HBZ) is expressed in all cases of ATL and is directly associated with virus pathogenicity. The two isoforms of the HBZ protein are synthesized from antisense messenger RNAs (mRNAs) that are either spliced (sHBZ) or unspliced (usHBZ) versions of the HBZ transcript. The sHBZ and usHBZ mRNAs have entirely different 5'untranslated regions (5'UTR) and are differentially expressed in cells, with the sHBZ protein being more abundant. Here, we show that differential expression of the HBZ isoforms is regulated at the translational level. Translation initiation of the usHBZ mRNA relies on a cap-dependent mechanism, while the sHBZ mRNA uses internal initiation. Based on the structural data for the sHBZ 5'UTR generated by SHAPE in combination with 5' and 3' deletion mutants, the minimal region harboring IRES activity was mapped to the 5'end of the sHBZ mRNA. In addition, the sHBZ IRES recruited the 40S ribosomal subunit upstream of the initiation codon, and IRES activity was found to be dependent on the ribosomal protein eS25 and eIF5A.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Cáceres CJ,Angulo J,Lowy F,Contreras N,Walters B,Olivares E,Allouche D,Merviel A,Pino K,Sargueil B,Thompson SR,López-Lastra Mdoi
10.1093/nar/gky802subject
Has Abstractpub_date
2018-11-16 00:00:00pages
11030-11047issue
20eissn
0305-1048issn
1362-4962pii
5095458journal_volume
46pub_type
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