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First published online March 12, 2004
doi: 10.1242/10.1242/jcs.00992

Journal of Cell Science 117, 1553-1566 (2004)
Published by The Company of Biologists 2004
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Research Article

CRM1 and Ran are present but a NES-CRM1-RanGTP complex is not required in Balbiani ring mRNP particles from the gene to the cytoplasm

Jian Zhao*, Shao-Bo Jin and Lars Wieslander{ddagger}

Department of Molecular Biology and Functional Genomics, Stockholm University, SE-106 91 Stockholm, Sweden

{ddagger} Author for correspondence (e-mail: lars.wieslander{at}molbio.su.se)

Accepted 17 November 2003

Messenger RNA is formed from precursors known as pre-mRNA. These precursors associate with proteins to form pre-mRNA-protein (pre-mRNP) complexes. Processing machines cap, splice and polyadenylate the pre-mRNP and in this way build the mRNP. These processing machines also affect the export of the mRNP complexes from the nucleus to the cytoplasm. Export to the cytoplasm takes place through a structure in the nuclear membrane called the nuclear pore complex (NPC). Export involves adapter proteins in the mRNP and receptor proteins that bind to the adapter proteins and to components of the NPC. We show that the export receptor chromosomal region maintenance protein 1 (CRM1), belonging to a family of proteins known as importin-ß-like proteins, binds to gene-specific Balbiani ring (BR) pre-mRNP while transcription takes place. We also show that the GTPase known as Ran binds to BR pre-mRNP, and that it binds mainly in the interchromatin. However, we also show using leptomycin B treatment that a NES-CRM1-RanGTP complex is not essential for export, even though both CRM1 and Ran accompany the BR mRNP through the NPC. Our results therefore suggest that several export receptors associate with BR mRNP and that these receptors have redundant functions in the nuclear export of BR mRNP.

Key words: Gene expression, mRNA export, Export receptors


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© The Company of Biologists Ltd 2004