Translational repression by a complex between the iron-responsive element of ferritin mRNA and its specific cytoplasmic binding protein is position-dependent in vivo.
AUTOR(ES)
Goossen, B
RESUMO
The interaction of ferritin mRNA is regulated by iron via the interaction of a cytoplasmic binding protein (IRE-BP) with a specific stem-loop structure in the 5' untranslated region (UTR), referred to as the iron-responsive element (IRE). A high affinity RNA-protein complex between the IRE and the IRE-BP functions as a repressor of translation in vivo. Translational repression appears to depend upon the position of the IRE in the 5' UTR of the mRNA. IREs located in the 5' untranslated region 67 nucleotides or more downstream of the 5' terminus of the mRNA fail to mediate iron-dependent translational regulation and give rise to constitutively derepressed transcripts. A model is proposed in which translational regulation of protein biosynthesis involves a position-dependent interference of the IRE/IRE-BP complex with one of the initial steps in translation initiation.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=552186Documentos Relacionados
- Regulation of interaction of the iron-responsive element binding protein with iron-responsive RNA elements.
- A Mutation, in the Iron-Responsive Element of H Ferritin mRNA, Causing Autosomal Dominant Iron Overload
- The interaction between the iron-responsive element binding protein and its cognate RNA is highly dependent upon both RNA sequence and structure.
- Role of RNA secondary structure of the iron-responsive element in translational regulation of ferritin synthesis.
- Structural requirements of iron-responsive elements for binding of the protein involved in both transferrin receptor and ferritin mRNA post-transcriptional regulation.