Molecular and Cellular Biology, May 2001, p. 3462-3471, Vol. 21, No. 10
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.10.3462-3471.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


Department of Biological Sciences, Stanford University, Stanford, California 943051; Protein Chemistry Department, Genentech, Inc., South San Francisco, California 940802; and Section of Molecular Cell and Developmental Biology, Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, Texas 787123
Received 4 January 2001/Returned for modification 12 February 2001/Accepted 27 February 2001
The early stages of Drosophila melanogaster development rely extensively on posttranscriptional forms of gene regulation. Deployment of the anterior body patterning morphogen, the Bicoid protein, requires both localization and translational regulation of the maternal bicoid mRNA. Here we provide evidence that the bicoid mRNA is also selectively stabilized during oogenesis. We identify and isolate a protein, BSF, that binds specifically to IV/V RNA, a minimal form of the bicoid mRNA 3' untranslated region that supports a normal program of mRNA localization during oogenesis. Mutations that disrupt the BSF binding site in IV/V RNA or substantially reduce the level of BSF protein lead to reduction in IV/V RNA levels, indicating a role for BSF in RNA stabilization. The BSF protein is novel and lacks all of the characterized RNA binding motifs. However, BSF does include multiple copies of the PPR motif, whose function is unknown but appears in other proteins with roles in RNA metabolism.
Present address: Gorilla Genomics, Alameda, CA 94501.
Present address: Rigel Inc., South San Francisco, CA 94080.
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