BULLETIN 1
Africa's First Gene-Edited Grapevine Promises Climate Resilience
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April 22, 2026
In a landmark achievement for African biotechnology, researchers from Stellenbosch University and the Agricultural Research Council have successfully produced the continent's first gene-edited grapevine. By using CRISPR-Cas9 technology to switch off a specific gene known as VvDMR6.1, the team has developed a woody crop variety with enhanced resistance to devastating diseases. This breakthrough, recently published in the journal Plant Stress, marks a significant milestone in using precision breeding to protect high-value horticultural crops in Africa.
The primary focus of the research was to combat downy mildew, a major fungal disease that poses a constant threat to global viticulture. By silencing the VvDMR6.1 gene—which typically makes the plant more susceptible to infection—the researchers significantly reduced the grapevine's vulnerability to the pathogen. Interestingly, the study revealed an unexpected dual role for the gene; once edited, the plants also demonstrated a superior ability to conserve water. This dual benefit suggests that a single targeted genetic change can simultaneously bolster a plant's defenses against both biological pests and environmental hardships.
Lead researcher Dr. Manuela Campa emphasized that this innovation arrives at a critical time as climate change intensifies both drought conditions and disease outbreaks. While gene editing has been widely used in annual crops, its application in perennial woody species like grapevines has historically been limited by long breeding cycles and complex regeneration systems. This success opens the door for more sustainable and resilient agricultural practices across Africa, potentially securing the future of the continent's wine and table grape industries against an increasingly volatile environment.
For more details, read this article.
See: https://www.isaaa.org/kc/cropbiotechupdate/article/default.asp?ID=21791
The primary focus of the research was to combat downy mildew, a major fungal disease that poses a constant threat to global viticulture. By silencing the VvDMR6.1 gene—which typically makes the plant more susceptible to infection—the researchers significantly reduced the grapevine's vulnerability to the pathogen. Interestingly, the study revealed an unexpected dual role for the gene; once edited, the plants also demonstrated a superior ability to conserve water. This dual benefit suggests that a single targeted genetic change can simultaneously bolster a plant's defenses against both biological pests and environmental hardships.
Lead researcher Dr. Manuela Campa emphasized that this innovation arrives at a critical time as climate change intensifies both drought conditions and disease outbreaks. While gene editing has been widely used in annual crops, its application in perennial woody species like grapevines has historically been limited by long breeding cycles and complex regeneration systems. This success opens the door for more sustainable and resilient agricultural practices across Africa, potentially securing the future of the continent's wine and table grape industries against an increasingly volatile environment.
For more details, read this article.
See: https://www.isaaa.org/kc/cropbiotechupdate/article/default.asp?ID=21791
BULLETIN 2
Exhibition Features Gene-edited Glowing Plants in China
Exhibition Features Gene-edited Glowing Plants in China
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Photo Source: Magicpen Bio
April 22, 2026
Gene-edited glowing plants were one of the highlights of the 2026 Garden Conference x Garden Collection Design Week held on April 17-19, 2026, at Suzhou International Expo Center in China. The glowing plants were showcased by Magicpen Bio, a China-based startup focused on research and development of gene-edited glowing plants.
The glowing plants were developed by introducing firefly and glowing fungi genes into plant cells, allowing them to emit a soft glow. The researchers have modified more than 20 species to glow in the dark, including orchids, sunflowers, and chrysanthemums.
Over the three-day event, Magicpen Bio's exhibition highlighted a growing industry demand for innovative "night garden" solutions that move beyond traditional artificial lighting. They placed the glowing plants in a fully enclosed, independent exhibition hall. The booth attracted approximately 840 groups of professional visitors, including house designers, landscape engineers, and cultural tourism operators.
The company's main goal is to position luminous plants as key tools for reimagining landscape design and nighttime environments across China.
Read more from Magicpen Bio and Euronews.
See https://www.isaaa.org/kc/cropbiotechupdate/article/default.asp?ID=21785
The glowing plants were developed by introducing firefly and glowing fungi genes into plant cells, allowing them to emit a soft glow. The researchers have modified more than 20 species to glow in the dark, including orchids, sunflowers, and chrysanthemums.
Over the three-day event, Magicpen Bio's exhibition highlighted a growing industry demand for innovative "night garden" solutions that move beyond traditional artificial lighting. They placed the glowing plants in a fully enclosed, independent exhibition hall. The booth attracted approximately 840 groups of professional visitors, including house designers, landscape engineers, and cultural tourism operators.
The company's main goal is to position luminous plants as key tools for reimagining landscape design and nighttime environments across China.
Read more from Magicpen Bio and Euronews.
See https://www.isaaa.org/kc/cropbiotechupdate/article/default.asp?ID=21785
SCIENTIFIC NEWS
Rubisco kinetic acclimation at the holoenzyme level
Bryce Askey, Maddie Ceminsky, Elena Scott, Yongsheng Wang, Zhen Guo Oh, Stavros Azinas, Arthur Laganowsky, and Laura Helen Gunn
PNAS; April 15 2026; 123 (16) e2519914123; https://doi.org/10.1073/pnas.2519914123
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Significance
Kinetic acclimation enables proteins to adjust their activity in response to environmental perturbations. For the CO2-fixing enzyme Rubisco, kinetic acclimation may be conferred by its small subunits. Plants express multiple small subunits and vary their expression with temperature. Here, we demonstrate that different small subunits can bind to the same Rubisco to form a heterogeneous holoenzyme. These small subunits had distinct kinetic effects which aligned with changes in holoenzyme structure and stability. Our findings indicate that small subunits enable Rubisco kinetic acclimation via manipulation of flexibility. By assembling a more rigid active site in higher temperatures and a more flexible one in lower temperatures, plants maximize the efficiency of their Rubisco, and thus photosynthesis, over a wide range of temperatures.
Kinetic acclimation enables proteins to adjust their activity in response to environmental perturbations. For the CO2-fixing enzyme Rubisco, kinetic acclimation may be conferred by its small subunits. Plants express multiple small subunits and vary their expression with temperature. Here, we demonstrate that different small subunits can bind to the same Rubisco to form a heterogeneous holoenzyme. These small subunits had distinct kinetic effects which aligned with changes in holoenzyme structure and stability. Our findings indicate that small subunits enable Rubisco kinetic acclimation via manipulation of flexibility. By assembling a more rigid active site in higher temperatures and a more flexible one in lower temperatures, plants maximize the efficiency of their Rubisco, and thus photosynthesis, over a wide range of temperatures.
Abstract
In plants, the CO2-fixing enzyme Rubisco is hexadecameric, with each mature holoenzyme containing eight small subunits (SSus). Many plants express multiple SSus and vary their expression in response to environmental cues. Previous work indicates that this may allow fine-tuning of Rubisco’s performance in a variable environment (i.e., kinetic acclimation). Despite SSu pools being heterogeneous and dynamic, nearly no evidence exists for holoenzyme-level heterogeneity. Here, we characterized the structural and kinetic plasticity of Rubisco. We first established that SSu-heterogeneous Rubisco exists in Arabidopsis thaliana and quantified the prevalence of heterogeneity. We found SSu-heterogeneous Rubisco to make up over half of the Rubisco pool when heterologously expressed. This Rubisco contained at least four unique SSu ratios, indicating a variety of holoenzyme arrangements are possible. We then tested the kinetic effect of different SSus and found heterogeneity to have an antagonistic effect on substrate and inhibitor affinity. Kinetic differences between the SSus correlated with changes in local flexibility, and cryo-EM analysis illustrated a structural mechanism through which SSus may influence catalysis. Our kinetic and structural findings align with the hypothesized role of SSus in kinetic acclimation, as we observed the warm temperature-expressed SSu of A. thaliana to confer a stabilizing effect to the active site relative to the cool temperature-expressed SSu. This increase in stability manifested as a reduction in flexibility and increase in substrate affinity, indicating that fine-tuning of local stability may underlie Rubisco kinetic acclimation.
See: https://www.pnas.org/doi/10.1073/pnas.2519914123
In plants, the CO2-fixing enzyme Rubisco is hexadecameric, with each mature holoenzyme containing eight small subunits (SSus). Many plants express multiple SSus and vary their expression in response to environmental cues. Previous work indicates that this may allow fine-tuning of Rubisco’s performance in a variable environment (i.e., kinetic acclimation). Despite SSu pools being heterogeneous and dynamic, nearly no evidence exists for holoenzyme-level heterogeneity. Here, we characterized the structural and kinetic plasticity of Rubisco. We first established that SSu-heterogeneous Rubisco exists in Arabidopsis thaliana and quantified the prevalence of heterogeneity. We found SSu-heterogeneous Rubisco to make up over half of the Rubisco pool when heterologously expressed. This Rubisco contained at least four unique SSu ratios, indicating a variety of holoenzyme arrangements are possible. We then tested the kinetic effect of different SSus and found heterogeneity to have an antagonistic effect on substrate and inhibitor affinity. Kinetic differences between the SSus correlated with changes in local flexibility, and cryo-EM analysis illustrated a structural mechanism through which SSus may influence catalysis. Our kinetic and structural findings align with the hypothesized role of SSus in kinetic acclimation, as we observed the warm temperature-expressed SSu of A. thaliana to confer a stabilizing effect to the active site relative to the cool temperature-expressed SSu. This increase in stability manifested as a reduction in flexibility and increase in substrate affinity, indicating that fine-tuning of local stability may underlie Rubisco kinetic acclimation.
See: https://www.pnas.org/doi/10.1073/pnas.2519914123
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Figure:
SSu-heterogeneous Rubisco can be purified from A. thaliana plants. (A) Dual-SSu construct design used to generate transformed plant lines. (B) 3-wk-old T2 plants. (Scale bar, 2 cm.) (C) Native and SDS PAGE of total soluble and affinity purified protein from T3 plants. Rubisco bands in H > S lanes appear more intense than those in H lanes because H > S fractions were concentrated prior to loading. Sol: total soluble; H: HisTrap purified; H > S: HisTrap and StrepTrap purified; RFP: red fluorescent protein.
SSu-heterogeneous Rubisco can be purified from A. thaliana plants. (A) Dual-SSu construct design used to generate transformed plant lines. (B) 3-wk-old T2 plants. (Scale bar, 2 cm.) (C) Native and SDS PAGE of total soluble and affinity purified protein from T3 plants. Rubisco bands in H > S lanes appear more intense than those in H lanes because H > S fractions were concentrated prior to loading. Sol: total soluble; H: HisTrap purified; H > S: HisTrap and StrepTrap purified; RFP: red fluorescent protein.











