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An Erythroid-Enriched Endoribonuclease (ErEN) Involved in α -Globin mRNA Turnover

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Messenger RNA (mRNA) decay utilizes both exoribonucleolytic and endoribonucleolytic enzymes where the latter are generally more prone to be transcript-specific. An erythroid-enriched endoribonuclease, ErEN, can destabilize the α -globin mRNA through directing a site-specific cleavage within the 3' untranslated region (3' UTR) both in vitro and in vivo. ErEN activity is sequence- and/or local structure-specific as the minimal recognition/cleavage sequence can be conferred onto a heterologous RNA and mutations at the cleavage site immunize the mRNA from ErEN hydrolysis. Interestingly, the ErEN cleavage activity is regulated by an mRNA stability complex (α -complex). An interaction between the α -complex and the poly(A)-binding protein (PABP) accentuates α -complex binding to a region overlapping the ErEN cleavage site and further prevents premature ErEN-mediated decay. At present the identity of ErEN remains elusive, yet its identification will provide mechanistic and functional insights into the general processes of endoribonuclease-mediated mRNA turnover and erythropoiesis.





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Keywords: ErEN; endoribonuclease; erythropoiesis; mRNA decay; α-globin

Document Type: Research Article

Affiliations: Department of Cell Biology and Neuroscience, Rutgers University, Piscataway, New Jersey 08854-082 , USA.

Publication date: 2007-02-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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