25 years ago, a researcher at the Howard Hughes Medical Institute at Duke University discovered “Xinyan DongAn important plant protein, and because she was a radio fan, she decided to name it “NPR1” after the non-profit American Broadcasting Corporation.
In the years since that discovery, Dong has done a lot of research on this protein, discovering that it has a key role in regulating plants’ defense genes against a wide range of diseases. The protein has been shown to give plants resistance to disease when overexpressed in a large number of crops such as rice and wheat.
However, despite its pivotal role in plant immunity, the lack of information about the protein’s structure – or shape – has hampered the understanding of its regulatory mechanisms, posing a dilemma for those interested in plant sciences.
But after many years, Dong and her colleagues put the jewel at the top of the crown; I discovered the form of the protein in its active form and inactive appearance, and “I was finally able to see it after many years of effort,” Dong told Al-Alam.
It turns out that NPR1 consists of double-winged arms resembling a single-winged bird gliding through the air, and that this protein interacts with transcription factors – in its active form – on both wings to stimulate immunity and protect plants.
and according the study Published in the journal Nature, NPR1 is known as a “key regulator controlling more than 2,000 genes involved in plant immunity.” Despite its huge role in plant defense, its form has remained elusive; Without detailed structural data, scientists have struggled to understand how the protein controls plant protection.
Scientists say figuring out what this protein looks like could change the way we grow plants. “Resolving the NPR1 protein structure will provide key information for engineering the protein and its related compound to improve their activities,” Dong told Science.
NPR1 is a good target for large-scale disease resistance engineering in different crop backgrounds in vitro and in limited field experiments, thus revealing the structural information will facilitate its application in large-scale agriculture; By better understanding how plants naturally confer widespread disease resistance, scientists will be able to engineer better crops with enhanced protection against known and emerging diseases, while at the same time reducing the use of chemical pesticides that are significant pollutants.
In conjunction with planting operations, the farmer must have the ability to fight many pests and pathogens that hinder plant growth; Water rot, for example, is one of the worst diseases, resulting in the Irish Potato Famine (1845-1852) that killed one million people, and today, pathogens still infect bananas, avocados and other popular crops.
But addressing the problem with traditional approaches can be problematic. Chemical pesticides, for example, often pollute the environment, which is one reason why plant breeders are now looking for genetic solutions, such as engineering plant cells to produce high levels of NPR1, and this approach has proven successful in the lab and in limited field trials, but with one problem; As immunity increases, growth declines.
According to a plant biologist at Sainsbury’s Laboratory in the United Kingdom, “Jonathan Jones” – who was not involved in that study – the new knowledge of NPR1 structure and behavior can help researchers avoid this problem and engineer better crops, and “Jones” says in statements transmitted by a press release received “for science.” Transcript of it: “Understanding how a protein works and interacts with other molecules has great potential to be very powerful in promoting disease resistance in plants.”
The researchers used X-ray crystallography and cryo-electron microscopy, which were developed by German Joachim Frank and for which he won the Nobel Prize, to reveal the structure of this important protein.
Over the past years, many researchers have failed to image this protein due to the difficulty of purifying it, but Dong’s team succeeded in purifying the protein and using deep freezing technology to produce high-resolution images that reveal its main functional areas.
Dong says: “These experiments took 4 full years, and now we can close a door that has been open for many years; Seeing the protein’s structure with our own eyes shuts the door to all speculation.
However, a closed door, as usual, opens new doors. Now Dong would like to know how the protein folds, adding, “The folding process will reveal why some plants fail to resist pests or succeed, and there are many questions waiting. Uncovering the protein’s structure opens up other doors and entirely new research directions.”
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