Abstract
Arabidopsis COLD SHOCK DOMAIN PROTEIN 3 (AtCSP3) shares an RNA chaperone function with E. coli cold shock proteins and regulates freezing tolerance during cold acclimation. Here, we screened for AtCSP3-interacting proteins using a yeast two-hybrid system and 38 candidate interactors were identified. Sixteen of these were further confirmed in planta interaction between AtCSP3 by a bi-molecular fluorescence complementation assay. We found that AtCSP3 interacts with CONSTANS-LIKE protein 15 and nuclear poly(A)-binding proteins in nuclear speckles. Three 60S ribosomal proteins (RPL26A, RPL40A/UBQ2, and RPL36aB) and the Gar1 RNA-binding protein interacted with AtCSP3 in the nucleolus and nucleoplasm, suggesting that AtCSP3 functions in ribosome biogenesis. Interactions with LOS2/enolase and glycine-rich RNA-binding protein 7 that are cold inducible, and an mRNA decap** protein 5 (DCP5) were observed in the cytoplasm. These data suggest that AtCSP3 participates in multiple complexes that reside in nuclear and cytoplasmic compartments and possibly regulates RNA processing and functioning.
Abbreviations
- BiFC:
-
Bi-molecular fluorescence complementation
- COL:
-
CONSTANS-LIKE protein
- CBF:
-
C-repeat-binding factor
- CSD:
-
Cold shock domain
- CSPs:
-
Cold shock domain protein
- DCP:
-
Decap** protein
- Gar:
-
Glycine-arginine rich domain
- GFP:
-
Green fluorescent protein
- GRP:
-
Glycine-rich RNA-binding protein
- LOS:
-
Low expression of osmotically responsive gene
- PABN:
-
Nuclear type of poly(A)-binding protein
- RPL:
-
Ribosomal protein
- YFP:
-
Yellow fluorescent protein
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Acknowledgments
This research was supported in part by grants from the Japan Society for the Promotion of Science (KAKENHI Scientific Research B 19380063) and NARO project 112g0 (Wheat and Soybean Biotechnology) to R.I.
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An erratum to this article is available at http://dx.doi.org/10.1007/s12192-014-0567-7.
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Kim, MH., Sonoda, Y., Sasaki, K. et al. Interactome analysis reveals versatile functions of Arabidopsis COLD SHOCK DOMAIN PROTEIN 3 in RNA processing within the nucleus and cytoplasm. Cell Stress and Chaperones 18, 517–525 (2013). https://doi.org/10.1007/s12192-012-0398-3
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DOI: https://doi.org/10.1007/s12192-012-0398-3