Nanos and pumilio establish embryonic polarity in Drosophila by promoting posterior deadenylation of hunchback mRNA

Christopher Wreden, Arturo C. Verrotti, Jennifer A. Schisa, Marshal E. Lieberfarb, Sidney Strickland

Research output: Contribution to journalArticlepeer-review

181 Scopus citations

Abstract

Nanos protein promotes abdominal structures in Drosophila embryos by repressing the translation of maternal hunchback mRNA in the posterior. To study the mechanism of nanos-mediated translational repression, we first examined the mechanism by which maternal hunchback mRNA is translationally activated. In the absence of nanos activity, the poly(A) tail of hunchback mRNA is elongated concomitant with its translation, suggesting that cytoplasmic polyadenylation directs activation. However, in the presence of nanos the length of the hunchback mRNA poly(A) tail is reduced. To determine if nanos activity represses translation by altering the polyadenylation state of hunchback mRNA, we injected various in vitro transcribed RNAs into Drosophila embryos and determined changes in polyadenylation. Nanos activity reduced the polyadenylation status of injected hunchback RNAs by accelerating their deadenylation. Pumilio activity, which is necessary to repress the translation of hunchback, is also needed to alter polyadenylation. An examination of translation indicates a strong correlation between poly(A) shortening and suppression of translation. These data indicate that nanos and pumilio determine posterior morphology by promoting the deadenylation of maternal hunchback mRNA, thereby repressing its translation.

Original languageEnglish
Pages (from-to)3015-3023
Number of pages9
JournalDevelopment
Volume124
Issue number15
StatePublished - 1997
Externally publishedYes

Keywords

  • Drosophila
  • Hunchback
  • Maternal mRNA
  • Nanos
  • Polyadenylation
  • Pumilio
  • Translational repression

Fingerprint

Dive into the research topics of 'Nanos and pumilio establish embryonic polarity in Drosophila by promoting posterior deadenylation of hunchback mRNA'. Together they form a unique fingerprint.

Cite this