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PMID: 9660969 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The Pumilio RNA-binding domain is also a translational regulator.

Molecular cell ·Vol. 1 ·No. 6 ·1998-05-00 ·Pages 863-72

Wharton RP, Sonoda J, Lee T, Patterson M, Murata Y

Abstract

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.

MeSH Terms
Amino Acid Sequence Animals Base Sequence Drosophila/genetics Drosophila Proteins Eye/growth & development Gene Expression Regulation, Developmental/physiology Genes, Insect/physiology Insect Proteins/chemistry,genetics Molecular Sequence Data Mutagenesis/physiology Peptide Chain Initiation, Translational Protein Binding/genetics Protein Biosynthesis/physiology Protein Structure, Tertiary RNA-Binding Proteins/chemistry,genetics Ribosomes/physiology
Chemicals
Drosophila Proteins Insect Proteins RNA-Binding Proteins pum protein, Drosophila
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Wharton R P
Howard Hughes Medical Institute, Department of Genetics, Duke University Medical Center, Durham, North Carolina 27710, USA.
Sonoda J
Lee T
Patterson M
Murata Y
Article Info
Journal
Molecular cell
Abbr.
Mol Cell
ISSN
1097-2765
Published
1998-05-00
Pages
863-72
Language
English
Region
United States
NLM ID
9802571
Subset
IM
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