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The receptor-like kinase OsCR4 plays an important role in vegetative and reproductive growth in rice; it controls embryo morphogenesis, leaf development, and interlocking of the palea and lemma. To identify proteins capable of interacting with the OsCR4 extracellular domain (OsCR4E), we performed a yeast two-hybrid assay and obtained two candidate proteins, OsCIP1 and OsCIP2. Both proteins are cysteine-rich and harbor an N-terminal signal peptide. Localization studies showed OsCIP1-GFP accumulation at the cell surface and OsCIP2-GFP accumulation in cytoplasmic vesicles. Immunoblotting revealed the presence of full-length and truncated OsCIP1-GFP fusion proteins in tobacco leaves and rice roots, and Q62 was identified as the key site for protein cleavage. OsCIP1 was mainly expressed in vascular bundles and the interlocking tissues of the palea and lemma, while OsCIP2 was mainly expressed in mature seeds. Compared to wild type, oscip1 mutant plants exhibited a short seminal root. A phylogenetic tree analysis showed that the homologs of OsCIP1 we identified all belong to the family Gramineae. Our results suggest that OsCIP1 interacts with the extracellular domain of OsCR4.
Keywords
OsCR4, extracellular domain, yeast two-hybrid, OsCIP1, OsCIP2, rice
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This is a preprint, a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Research Article
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
History
CURRENT STATUS: Posted
Version 1
Posted 16 Mar, 2021
No community comments so far
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
The receptor-like kinase OsCR4 plays an important role in vegetative and reproductive growth in rice; it controls embryo morphogenesis, leaf development, and interlocking of the palea and lemma. To identify proteins capable of interacting with the OsCR4 extracellular domain (OsCR4E), we performed a yeast two-hybrid assay and obtained two candidate proteins, OsCIP1 and OsCIP2. Both proteins are cysteine-rich and harbor an N-terminal signal peptide. Localization studies showed OsCIP1-GFP accumulation at the cell surface and OsCIP2-GFP accumulation in cytoplasmic vesicles. Immunoblotting revealed the presence of full-length and truncated OsCIP1-GFP fusion proteins in tobacco leaves and rice roots, and Q62 was identified as the key site for protein cleavage. OsCIP1 was mainly expressed in vascular bundles and the interlocking tissues of the palea and lemma, while OsCIP2 was mainly expressed in mature seeds. Compared to wild type, oscip1 mutant plants exhibited a short seminal root. A phylogenetic tree analysis showed that the homologs of OsCIP1 we identified all belong to the family Gramineae. Our results suggest that OsCIP1 interacts with the extracellular domain of OsCR4.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
Figure 6
This is a list of supplementary files associated with this preprint. Click to download.
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