The Pumilio RNA-Binding Domain Is Also a Translational Regulator

• Published in: Molecular cell Vol. 1; no. 6; pp. 863 - 872
• Main Authors: Wharton, Robin P, Sonoda, Junichiro, Lee, Tammy, Patterson, Michelle, Murata, Yoshihiko
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.05.1998
• Subjects: Amino Acid Sequence; Animals; Base Sequence; Drosophila - genetics; Drosophila Proteins; Eye - growth & development; Gene Expression Regulation, Developmental - physiology; Genes, Insect - physiology; Insect Proteins - chemistry; Insect Proteins - genetics; Molecular Sequence Data; Mutagenesis - physiology; Peptide Chain Initiation, Translational; Protein Binding - genetics; Protein Biosynthesis - physiology; Protein Structure, Tertiary; Ribosomes - physiology; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - genetics
• ISSN: 1097-2765; 1097-4164
• DOI: 10.1016/S1097-2765(00)80085-4

Posterior patterning in the Drosophila embryo requires the action of Nanos (Nos) and Pumilio (Pum), which collaborate to regulate the translation of maternal hunchback( hb) mRNA. Previous work demonstrated that Pum recognizes sites in the 3′ UTR of hb mRNA. In this report, we first define the RNA-binding domain of Pum and then show that residues essential for translational repression are embedded within this domain. We also show that Nos and Pum can repress cap-independent translation from an internal ribosome entry site (IRES) in vivo, suggesting that they act downstream of the initial steps of normal, cap-dependent translation.