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Published online 21 March 2005. doi:10.1083/jcb.200407173
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 168, Number 7, 1013-1025
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Article

Hrp59, an hnRNP M protein in Chironomus and Drosophila, binds to exonic splicing enhancers and is required for expression of a subset of mRNAs



Eva Kiesler1, Manuela E. Hase1, David Brodin2, and Neus Visa1

1 Department of Molecular Biology and Functional Genomics, Stockholm University, SE-10691 Stockholm, Sweden
2 Department of Biosciences at Novum, Karolinska Institute, SE-14157 Huddinge, Sweden

Correspondence to Neus Visa: neus.visa{at}molbio.su.se

Here, we study an insect hnRNP M protein, referred to as Hrp59. Hrp59 is relatively abundant, has a modular domain organization containing three RNA-binding domains, is dynamically recruited to transcribed genes, and binds to premRNA cotranscriptionally. Using the Balbiani ring system of Chironomus, we show that Hrp59 accompanies the mRNA from the gene to the nuclear envelope, and is released from the mRNA at the nuclear pore. The association of Hrp59 with transcribed genes is not proportional to the amount of synthesized RNA, and in vivo Hrp59 binds preferentially to a subset of mRNAs, including its own mRNA. By coimmunoprecipitation of Hrp59–RNA complexes and microarray hybridization against Drosophila whole-genome arrays, we identify the preferred mRNA targets of Hrp59 in vivo and show that Hrp59 is required for the expression of these target mRNAs. We also show that Hrp59 binds preferentially to exonic splicing enhancers and our results provide new insights into the role of hnRNP M in splicing regulation.

E. Kiesler and M. Hase have contributed equally to this work.

Abbreviations used in this paper: BR, Balbiani ring; BrUTP, bromo-UTP; CAT, chloramphenicol acetyltransferase; CF, connecting fiber; DSP, dithiobis-succinimidyl propionate; ESE, exonic splicing enhancer; IP, immunoprecipitation; NPC, nuclear pore complex; premRNP, premessenger RNP complex; RRM, RNA-recognition motif.


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