Abstract
The conserved TREX complex, which contains UAP56, Aly, CIP29, and the multi-subunit THO complex, functions in mRNA export. Recently, several putative new components of the human TREX complex were identified by mass spectrometry. Here, we investigated the function of two of these, PDIP3 and ZC11A. Our data indicate that both of these proteins are components of a common TREX complex and function in mRNA export. Recently, we found that both CIP29 and Aly associate with the DEAD box helicase UAP56 and with the TREX complex in an ATP-dependent manner. We now show that this is also the case for PDIP3 and ZC11A. Thus, together with previous work, our data indicate that the TREX complex participates in multiple ATP-dependent interactions.
Highlights
During gene expression, pre-mRNAs are synthesized in the nucleus, undergo RNA processing, followed by export of the mature mRNA to the cytoplasm for translation
To further investigate PDIP3 and ZC11A, we RNase-treated HeLa nuclear extracts (Fig. 1C) and used them for IP/Westerns (Fig. 1D, E). This analysis revealed that PDIP3a and b efficiently co-IP with TREX components, including THOC2, UAP56 and Aly (Fig. 1D)
PDIP3 was reported to associate with the exon junction complex (EJC), which is recruited to exon junctions during splicing [8,9]
Summary
Pre-mRNAs are synthesized in the nucleus, undergo RNA processing, followed by export of the mature mRNA to the cytoplasm for translation. We show that both proteins are immunoprecipitated (IP’d) by antibodies to known TREX components in RNase-treated nuclear extracts, and PDIP3 and ZC11A reciprocally co-IP in these extracts. We found that both PDIP3 and ZC11A, like CIP29 and Aly, require ATP for association with UAP56 and the TREX complex.
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
