Journal
CELL STRESS & CHAPERONES
Volume 18, Issue 4, Pages 517-525Publisher
SPRINGER
DOI: 10.1007/s12192-012-0398-3
Keywords
Cold shock protein; RNA chaperone; Nucleus; Cytoplasm; Arabidopsis thaliana; mRNA processing
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Funding
- Japan Society for the Promotion of Science [19380063]
- NARO [112g0]
- Grants-in-Aid for Scientific Research [22380063, 19380063] Funding Source: KAKEN
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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 decapping 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.
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