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Updated: Jul 20, 2026
10:06
Engineering Artificial Factors to Specifically Manipulate Alternative Splicing in Human Cells
Published on: April 26, 2017
XE7: a novel splicing factor that interacts with ASF/SF2 and ZNF265
A Helena Mangs1, Helen J L Speirs, Christine Goy
1Basic & Clinical Genomics Laboratory, School of Medical Sciences and Bosch Institute, The University of Sydney, NSW 2006, Australia.
Nucleic Acids Research
|September 20, 2006
Summary
The uncharacterized protein XE7 is a novel alternative splicing regulator. It interacts with SR proteins and influences splice site selection, revealing a new role in mRNA processing.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Pre-messenger RNA (mRNA) splicing is a critical process for gene expression, carried out by the spliceosome.
- SR proteins are essential components of the spliceosome, regulating both constitutive and alternative splicing.
- The uncharacterized human protein XE7 was identified through a yeast two-hybrid screen and proteomic analysis of the spliceosome.
Purpose of the Study:
- To investigate the function of the uncharacterized human protein XE7.
- To determine if XE7 plays a role in mRNA processing and alternative splicing regulation.
- To characterize the interactions and cellular localization of XE7.
Main Methods:
- Yeast two-hybrid screening using SR-related protein ZNF265 as bait.
- Proteomic analysis of the human spliceosome.
- Analysis of XE7 isoforms and its arginine/serine (RS)-rich region.
- Co-immunoprecipitation assays to study protein interactions.
- Cellular localization studies using immunofluorescence microscopy.
- Functional assays using minigenes (CD44, Tra2-beta1, SRp20) to assess splice site selection.
Main Results:
- XE7 was identified as a novel protein interacting with ZNF265 and the SR protein ASF/SF2.
- The arginine/serine (RS)-rich region of XE7 is crucial for its interactions with ZNF265 and ASF/SF2.
- XE7 localizes to nuclear speckles, colocalizing with other SR proteins, including ZNF265 and ASF/SF2.
- XE7 influences alternative splice site selection in CD44, Tra2-beta1, and SRp20 minigenes.
- XE7 exists in two isoforms, with the larger isoform containing an RS-rich region suggesting a role in mRNA processing.
Conclusions:
- XE7 is an alternative splicing regulator that functions similarly to SR proteins.
- XE7's interactions and localization within the spliceosome suggest its involvement in mRNA processing.
- The study reveals XE7 as a novel component influencing alternative splicing decisions.
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