Back to Search
Start Over
OsCML16 interacts with a novel CC-NBS-LRR protein OsPi304 in the Ca2+/Mg2+ dependent and independent manner in rice
- Source :
- Biochemical and Biophysical Research Communications. 504:346-351
- Publication Year :
- 2018
- Publisher :
- Elsevier BV, 2018.
-
Abstract
- In plants, many target proteins of calmodulins (CaMs) have been identified in cellular metabolism and responses. However, calmodulin-like proteins (CMLs) and their target proteins have not been discovered in stress responses in rice. In this study, a novel CC-NBS-LRR protein was obtained in screening a cold stress rice seedlings yeast cDNA library with OsCML16 as bait. Furthermore, yeast two-hybrid and BiFC assays demonstrated that the full length, CC region in the N-terminus and LRR in the C-terminus of Pi304 protein could interact with OsCML16. More interestingly, OsCML16 bound to the 1–10 motif rather than 1–14 motif in the Ca2+ or Mg2+ dependent manner in vitro. In addition, transcript levels of OsCML16 and OsPi304 were induced more markedly in Nipponbare than in 9311 under cold stress. Taken together, these data indicates that they are involved in the cold stress signaling and response in rice.
- Subjects :
- 0106 biological sciences
0301 basic medicine
Cellular metabolism
Dependent manner
cDNA library
Chemistry
Biophysics
food and beverages
Cell Biology
01 natural sciences
Biochemistry
Yeast
Cell biology
03 medical and health sciences
Bimolecular fluorescence complementation
030104 developmental biology
Molecular Biology
Cold stress
010606 plant biology & botany
CALMODULIN-LIKE PROTEIN
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 504
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi...........5f81b77791d6352a8f5ab7061a405d0b