Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/22668
Title: Initiation of Apaf-1 translation by internal ribosome entry.
Authors: Coldwell, MJ
Mitchell, SA
Stoneley, M
MacFarlane, M
Willis, AE
First Published: 17-Feb-2000
Citation: ONCOGENE, 2000, 19 (7), pp. 899-905
Abstract: The apoptotic protease activating factor (Apaf-1) plays a central role in apoptosis: interaction of this protein with procaspase-9 leads to cleavage and activation of this initiator caspase. In common with other mRNAs whose protein products have a major regulatory function, the 5' untranslated region (UTR) of Apaf-1 is long, G-C rich and has the potential to form secondary structure. We have shown that the 5' UTR of Apaf-1 contains an internal ribosome entry segment, located in a 233 nucleotide region towards the 3' end of the leader, and that the translation initiation of this mRNA occurs only by internal ribosome entry. The Apaf-1 IRES is active in almost all human cell types tested, including Human cervical carcinoma (HeLa), Human liver carcinoma (HepG2), Human breast carcinoma (MCF7), Human embryonic kidney (HK293), African Green Monkey kidney (COS7) and Human lung (MRC5). The Apaf-1 IRES initiates translation as efficiently as the HRV IRES, but is less active than the c-myc IRES. We propose that the Apaf-1 IRES ensures that a constant cellular level of Apaf-1 protein is maintained even under conditions where cap-dependent translation is compromised. Oncogene (2000) 19, 899 - 905.
DOI Link: 10.1038/sj.onc.1203407
ISSN: 0950-9232
Links: http://hdl.handle.net/2381/22668
Type: Journal Article
Appears in Collections:Published Articles, Dept. of Biochemistry

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