Adaptor Aly and co‐adaptor Thoc5 function in the Tap‐p15‐mediated nuclear export of HSP70 mRNA |
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| Authors: | Jun Katahira Hitomi Inoue Ed Hurt Yoshihiro Yoneda |
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| Affiliation: | 1. Biomolecular Networks Laboratories, Biomolecular Dynamics Laboratory, Graduate School of Frontier Biosciences, Osaka University, Yamadaoka, Suita, Osaka, Japan;2. Department of Biochemistry, Graduate School of Medicine, Osaka University, Yamadaoka, Suita, Osaka, Japan;3. Biochemie‐Zentrum der Universit?t Heidelberg (BZH), Im Neuenheimer Feld, Heidelberg, Germany |
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| Abstract: | In metazoans, nuclear export of bulk mRNA is mediated by Tap‐p15, a conserved heterodimeric export receptor that cooperates with adaptor RNA‐binding proteins. In this article, we show that Thoc5, a subunit of the mammalian TREX complex, binds to a distinct surface on the middle (Ntf2‐like) domain of Tap. Notably, adaptor protein Aly and Thoc5 can simultaneously bind to non‐overlapping binding sites on Tap‐p15. In vivo, Thoc5 was not required for bulk mRNA export. However, nuclear export of HSP70 mRNA depends on both Thoc5 and Aly. Consistent with a function as a specific export adaptor, Thoc5 exhibits in vitro RNA‐binding activity and is associated with HSP70 mRNPs in vivo as a component of the stable THO complex. Thus, through the combinatorial use of an adaptor (e.g., Aly) and co‐adapter (e.g., Thoc5), Tap‐p15 could function as an export receptor for different classes of mRNAs. |
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| Keywords: | heat shock mRNA nucleo‐cytoplasmic transport TREX complex |
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