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In rice, leucine-rich repeat nucleotide-binding site (NLR) proteins are pivotal immune receptors in combating -triggered rice blast. However, the precise molecular mechanism underlying how NLR proteins regulate downstream signalling remains elusive due to the lack of knowledge regarding their direct downstream targets. The NLR protein Pigm-1 was cloned from Shuangkang 77009 in our laboratory. This study shows that the nucleotide-binding site (NBS) domain of Pigm-1 facilitates its binding to and activation of OsRac1 while the coiled-coil (CC) domain enables its binding to and activation of RAI1, ultimately inducing cell death. At the same time, after knocking out in the background of Shuangkang 77009 containing , two knockout lines showed susceptibility to rice blast. This study reveals OsRac1, a GTPase, as a signalling molecule involved in Pigm-1-mediated blast resistance, suggesting its potential as a common downstream effector of rice NLR proteins. Additionally, a transcriptional activator, RAI1, acts as an essential Pigm-1 interactor for blast resistance. Furthermore, a novel material 9311() was prepared by using two-line restorer line 9311 as receptor and Shuangkang 77009 as donor with molecular marker-assisted technology, which improved blast resistance and yield. This research demonstrates that molecular marker-assisted selection technology enhances both resistance and yield in the crucial two-line restorer 9311(). This study offers crucial insights into how Pigm-1 protein activates downstream molecules and serves as a valuable reference for the molecular breeding of rice blast resistance genes, particularly .
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http://dx.doi.org/10.3390/plants14020217 | DOI Listing |
Carbohydr Res
September 2025
Laboratory for Biochemistry & Glycobiology, Ghent University, Department of Biotechnology, Ghent, Belgium. Electronic address:
Lectins are carbohydrate-binding proteins which play key roles in various biological processes, including cell signaling, pathogen recognition and development. Previous research conducted on ricin-B lectin domains and carbohydrate-binding modules of family 13 (CBM13) illustrated the striking resemblances between these two groups of protein domains. In this study, we report on the discovery, identification and putative biochemical characteristics of a ricin-B-like domain that is unique for GH27 enzymes from land plants, identified in the OsAPSE enzyme from Japanese rice (Oryza sativa L.
View Article and Find Full Text PDFFront Plant Sci
August 2025
Faculty of Modern Agricultural Engineering, Kunming University of Science and Technology, Kunming, China.
Introduction: Rice is an important food crop but is susceptible to diseases. However, currently available spot segmentation models have high computational overhead and are difficult to deploy in field environments.
Methods: To address these limitations, a lightweight rice leaf spot segmentation model (MV3L-MSDE-PGFF-CA-DeepLabv3+, MMPC-DeepLabv3+) was developed for three common rice leaf diseases: rice blast, brown spot and bacterial leaf blight.
3 Biotech
October 2025
ICAR-National Rice Research Institute, Cuttack, Odisha 753006 India.
Just as Gregor Mendel's laws of inheritance laid the foundation for modern genetics, the emergence of Clustered Regularly Interspaced Short Palindromic Repeats (CRISPR)/Cas systems has catalyzed a new era in precision genome engineering. CRISPR/Cas has revolutionized rice ( L.) breeding by enabling precise, transgene-free edits to improve yield, nutrition, and stress tolerance.
View Article and Find Full Text PDFPlant Cell Environ
September 2025
State Key Laboratory for Conservation and Utilization of Bio-Resources in Yunnan, College of Plant Protection, Yunnan Agricultural University, Kunming, China.
Light and darkness are critical environmental factors that regulate plant immune responses. OsPIL1, a phytochrome-interacting factor-like protein, has been implicated in rice immunity against Magnaporthe oryzae, although its underlying mechanism remains unclear. This study aimed to dissect how OsPIL1 integrates light or darkness to modulate rice immunity.
View Article and Find Full Text PDFPlant Cell Environ
October 2025
College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou, China.