RESUMEN
Plant pollen tubes and root hairs typical polarized tip growth. It is well established that calcium ions (Ca2+) play essential roles in maintaining cell polarity and guiding cell growth orientation. Ca2+ signals are encoded by Ca2+ channels and transporters and are decoded by a variety of Ca2+-binding proteins often called Ca2+ sensors, in which calcineurin B-like protein (CBL) proteins function by interacting with and activating a group of kinases, activate CBL-interacting protein kinases (CIPKs). Some CBL-CIPK complexes, such as CBL2/3-CIPK12/19, act as crucial regulators of pollen tube growth. Whether these calcium decoding components regulate the growth of root hairs, another type of plant cell featuring Ca2+-regulated polarized growth, remains unknown. In this study, we identified CIPK13 and CIPK18 as genes specifically expressed in Arabidopsis (Arabidopsis thaliana) root hairs. The cipk13 cipk18 double mutants showed reduced root hair length and lower growth rates. The calcium oscillations at the root hair tip were attenuated in the cipk13 cipk18 mutants as compared to the wild-type plants. Through yeast two-hybrid screens, CBL2 and CBL3 were identified as interacting with CIPK13 and CIPK18. cbl2 cbl3 displayed a shortened root hair phenotype similar to cipk13 cipk18. This genetic analysis, together with biochemical assays showing activation of CIPK13/18 by CBL2/3, supported the conclusion that CBL2/3 and CIPK13/18 may work as Ca2+-decoding modules in controlling root hair growth. Thus, the findings that CIPK12/19 and CIPK13/18 function in pollen tube and root hair growth, respectively, illustrate a molecular mechanism in which the same CBLs recruit distinct CIPKs in regulating polarized tip growth in different types of plant cells.
RESUMEN
In this study, eight types of materials including nanoparticles (Cu and CaCO3), metallic ions (Ca2+ and Cu2+), and amino acid substances (serine, tyrosine, sericin amino acid, and fibroin amino acid) were used as additives in silkworm diets to obtain in-situ modified silk fiber composites. The results indicate that tyrosine and fibroin amino acids significantly increase potassium content in silk fibers and induce the transformation of α-helices and random coils to ß-sheet structures, resulting in higher crystallinities and better mechanical properties. However, the other additives-modified silk fibers show a decrease in ß-sheet contents and a slight increase or even decrease in tensile strengths. This finding provides a green and effective approach to produce mechanically enhanced silk fibers with high crystallinity on a large scale. Moreover, the modification mechanisms of these additives were discussed in this study, which could offer new insights into the design and regulation of modified fibers or composites with desirable properties and functions.