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Identification of Drosophila Bicoid-interacting proteins using a custom two-hybrid selection

  • SUNY Albany
  • Wadsworth Center for Laboratories and Research

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

Abstract

Bicoid directs pattern formation in the developing Drosophila embryo, and does so by performing two seemingly unrelated tasks; it activates transcription and represses translation. To understand how Bicoid carries out this dual role, we sought to identify Bicoid-ancillary proteins that might mediate Bicoid's function in transcription or translation. We used a customized version of the two-hybrid method and found two Bicoid-interacting proteins, Bin1 and Bin3, both of which interact with Bicoid in vitro. Bin1 is similar to a human protein (SAP18) involved in transcription regulation, and Bin3, described in this paper, is similar to a family of protein methyltransferases that modify RNA-binding proteins. Given that Bicoid's role as a translation regulator requires RNA binding, we suggest that the Bicoid- interacting methyltransferase might be important for that role. The custom two-hybrid method we used, in which Bicoid is bound to DNA via its own DNA binding domain, rather than via a fusion-protein tether, should be generally applicable to other DNA binding proteins. (C) 2000 Published by Elsevier Science B.V.

Original languageEnglish
Pages (from-to)329-339
Number of pages11
JournalGene
Volume245
Issue number2
DOIs
StatePublished - Mar 21 2000

Keywords

  • Homeodomain
  • One-hybrid
  • Protein methyltransferase
  • dSAP18

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