Identification of the internal ribosome entry sites (IRES) of prion protein gene

• Published in: The international journal of biochemistry & cell biology Vol. 93; pp. 46 - 51
• Main Authors: Luo, Xiao-Nuan, Song, Qin-Qin, Yu, Jie, Song, Juan, Wang, Xin-Ling, Xia, Dong, Sun, Peng, Han, Jun
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier Ltd 01.12.2017
• Subjects: Animals; Cricetinae; Endoplasmic Reticulum Stress - drug effects; Endoplasmic Reticulum Stress - genetics; HEK293 Cells; Humans; Internal Ribosome Entry Sites - physiology; IRES; Peptide Chain Initiation, Translational - physiology; Prion protein gene; Prion Proteins - biosynthesis; Prion Proteins - genetics; RNA, Messenger - genetics; RNA, Messenger - metabolism; Translation mechanism; Tunicamycin - pharmacology; IRES; Translation mechanism; Prion protein gene
• ISSN: 1357-2725; 1878-5875
• DOI: 10.1016/j.biocel.2017.10.014

Many studies demonstrated that there are several type bands of prion protein in cells. However, the formation of different prion protein bands is elusive. After several low molecular weight bands of prion protein appeared in SMB-S15 cells infected with scrapie agent Chandler, we think that IRES-dependent translation mechanism induced by prion is involved in the formation of prion protein bands. Then we designed a series of pPrP-GFP fusing plasmids and bicistronic plasmids to identify the IRES sites of prion protein gene and found 3 IRES sites inside of PrP mRNA. We also demonstrated that cap-independent translation of PrP was associated with the ER stress through Tunicamycin treatment. We still found that only IRE1 and PERK pathway regulated the IRES-dependent translation of PrP in this study. Our results indicated, we found that PrP gene had an IRES-dependent translation initiation mechanism and we successfully identified the IRESs inside of the prion protein gene.