| Literature DB >> 34956301 |
Chunhong Li1,2, Shifeng Cao3, Kaituo Wang1,2, Changyi Lei1, Nana Ji2, Feng Xu4, Yongbo Jiang1, Linglan Qiu1, Yonghua Zheng2.
Abstract
[This corrects the article DOI: 10.3389/fpls.2021.646147.].Entities:
Keywords: Botrytis cinerea; NPR1; grape berries; heat shock protein; priming resistance; β-aminobutyric acid
Year: 2021 PMID: 34956301 PMCID: PMC8698354 DOI: 10.3389/fpls.2021.812672
Source DB: PubMed Journal: Front Plant Sci ISSN: 1664-462X Impact factor: 5.753
Figure 5VvHSP24 interacts with VvNPR1 in vivo and in vitro. (A) Yeast two-hybrid analysis of the physical interaction between VvHSP24 and VvNPR1. SD-T-L-H, SD/-Trp-Leu-His agar medium; SD-T-L-H-A, SD/-Trp-Leu-His-Ade agar medium. The right-angled triangles on the top of the gridded Petri dishes represent the absorbance of yeasts at 600 nm in a 10-fold dilution series, from 1 to 10−2 abs. (B) The GST-fused VvNPR1 protein (1 mL) was incubated with 1 mL of preimmobilized His-VvHSP24 protein in a total volume of 25 mL at 4°C for more than 8 h. The pulled down proteins (6 μL) were analyzed by western blotting with anti-His or anti-GST antibodies.