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Expansins are non-hydrolytic cell wall-loosening proteins that are involved in the cell wall modifications that underlie many plant developmental processes. Root hair growth requires the accumulation of cell wall materials and dynamic cell wall modification at the tip region. Although several lines of indirect evidence support the idea that expansin-mediated wall modification occurs during root hair growth, the involvement of these proteins remains to be demonstrated in vivo. In this study, we used RNA interference (RNAi) to examine the biological function of Arabidopsis thaliana EXPANSIN A7 (AtEXPA7), which is expressed specifically in the root hair cell. The root hairspecific AtEXPA7 promoter was used to drive RNAi expression, which targeted two independent regions in the AtEXPA7 transcript. Quantitative reverse transcriptase-PCR analyses were used to examine AtEXPA7 transcript levels. In four independent RNAi transformant lines, RNAi expression reduced AtEXPA7 transcript levels by 25-58% compared to controls. Accordingly, the root hairs of RNAi transformant lines were 25-48% shorter than control plants and exhibited a broader range of lengths than the controls. Our results provide in vivo evidence that expansins are required for root hair tip growth.

The formation of leaves and other lateral organs in plants depends on the proper specification of adaxial-abaxial (upper-lower) polarity. KANADI1 (KAN1), a member of the GARP family of transcription factors, is a key regulator of abaxial identity, leaf growth, and meristem formation in Arabidopsis thaliana. Here, we demonstrate that the Myb-like domain in KAN1 binds the 6-bp motif GNATA(A/T) and that this motif alone is sufficient to squelch transcription of a linked reporter in vivo. In addition, we report that KAN1 acts as a transcriptional repressor. Among its targets are genes involved in auxin biosynthesis, auxin transport, and auxin response. Furthermore, we find that the adaxializing HD-ZIPIII transcription factor REVOLUTA has opposing effects on multiple components of the auxin pathway. We hypothesize that HD-ZIPIII and KANADI transcription factors pattern auxin accumulation and responsiveness in the embryo. Specifically, we propose the opposing actions of KANADI and HD-ZIPIII factors on cotyledon formation (KANADI represses and HD-ZIPIII promotes cotyledon formation) occur through their opposing actions on genes acting at multiple steps in the auxin pathway.

The ATP-dependent Lon protease is a highly conserved enzyme that is present in archeae, eubacteria, and eukaryotes, and plays an important role in intracellular protein degradation. We have isolated a Lon protease gene, OsLon1, from Oryza sativa. The cDNA contained a 2,655 bp ORF. Comparative analysis showed that OsLon1 shared significant similarity with the previously reported Lon proteases from maize, Arabidopsis, human, and bacteria. Tissue expression pattern analysis revealed that OsLon1 was highly expressed in young leaves, mature leaves, and leaf sheaths but only weakly in young roots, mature roots, and young panicles. The OsLon1 gene was successfully expressed in E. coli and the detected protein size, about 120 kDa, matched the expected molecular mass of the His-tagged OsLon1 protein.

Plants damaged by insects can synthesize and release volatile chemicals that attract natural enemies of the herbivore. The maize (Zea mays subsp. mays) terpene synthase gene stc1 is part of that indirect defense response, being induced in seedling blades in response to herbivory by beet army worm. Many genes in maize are duplicated because of a past whole-genome duplication event, and several of these orthologs display different expression patterns. We report here the isolation and characterization of tps26 and confirm by homology and synteny criteria that it is the ortholog of stc1. Prior genetic analysis revealed that the stc1 function is not duplicated, raising the interesting question of how the two orthologs have become differentiated in their expression. tps26 encodes a 633-amino acid protein that is highly conserved with STC1. Like stc1, tps26 is induced by wounding, but in the roots and leaf sheath, instead of the blade, and not in response to beet army worm feeding. tps26 maps near a quantitative trait locus for Southwestern corn borer resistance, making it a plausible candidate gene for that quantitative trait locus. However, while possessing highly polymorphic tps26 alleles, the resistant and susceptible parents of the mapping population do not differ in levels of tps26 expression. Moreover, tps26 is not induced specifically by Southwestern corn borer feeding. Therefore, although they share a wounding response, the stc1 and tps26 maize orthologs differ in their tissue specificity and their induction by insect herbivores. The N termini of STC1 and TPS26 are predicted to encode plastid transit peptides; fusion proteins of green fluorescent protein to either N terminus localized to the plastid, confirming that prediction. The mature proteins, but not the respective complete proteins, were active and synthesized a blend of monoterpenes, indicating that they are monoterpene synthases. A gene closely related to stc1/tps26 is found in the sorghum (Sorghum spp.) genome at a location that is not orthologous with stc1. The possible origin of stc1-like genes is discussed.

Plants damaged by insects can synthesize and release volatile chemicals that attract natural enemies of the herbivore. The maize (Zea mays subsp. mays) terpene synthase gene stc1 is part of that indirect defense response, being induced in seedling blades in response to herbivory by beet army worm. Many genes in maize are duplicated because of a past whole-genome duplication event, and several of these orthologs display different expression patterns. We report here the isolation and characterization of tps26 and confirm by homology and synteny criteria that it is the ortholog of stc1. Prior genetic analysis revealed that the stc1 function is not duplicated, raising the interesting question of how the two orthologs have become differentiated in their expression. tps26 encodes a 633-amino acid protein that is highly conserved with STC1. Like stc1, tps26 is induced by wounding, but in the roots and leaf sheath, instead of the blade, and not in response to beet army worm feeding. tps26 maps near a quantitative trait locus for Southwestern corn borer resistance, making it a plausible candidate gene for that quantitative trait locus. However, while possessing highly polymorphic tps26 alleles, the resistant and susceptible parents of the mapping population do not differ in levels of tps26 expression. Moreover, tps26 is not induced specifically by Southwestern corn borer feeding. Therefore, although they share a wounding response, the stc1 and tps26 maize orthologs differ in their tissue specificity and their induction by insect herbivores. The N termini of STC1 and TPS26 are predicted to encode plastid transit peptides; fusion proteins of green fluorescent protein to either N terminus localized to the plastid, confirming that prediction. The mature proteins, but not the respective complete proteins, were active and synthesized a blend of monoterpenes, indicating that they are monoterpene synthases. A gene closely related to stc1/tps26 is found in the sorghum (Sorghum spp.) genome at a location that is not orthologous with stc1. The possible origin of stc1-like genes is discussed.

Using Rapid Amplification of cDNA ends (RACE) technique, the full-length cDNA encoding a NaCl-induced fructose-1, 6-diphosphate aldolase (DsALDP) was obtained. It was shown that the DsALDP had a relatively high homology (66%-73%) to chloroplast fructose-1, 6-diphosphate aldolase (AldP) in many plants according to their amino acid sequences. The phylogenetic analysis further confirmed that AldP in alga is the nearest to DsALDP. As to its expression pattern,DsALDP was denovo synthesized by NaCl induction. Its expression level was significantly changed with inducing time. After the selectedDsALDP cDNA subcloned into a binary vector pBI121, the new construct was introduced into tobacco byAgrobacterium tumefaciens. The results of Southern blot and RT-PCR analysis of four transgenic T1 plants indicated thatDsALDP was integrated into genome of these transgenic plants and effectively expressed. Aldolase activities have been detected in T1-1, T1-2 and T1-3 plants by bioassay under 100-200 mmol/L NaCl. It was also observed that proline contents in them were differentially increased.[PUBLICATION ABSTRACT]

Butyrate supplementation has gained considerable attention for its potential benefits in livestock, particularly concerning intestinal health and growth performance. This review synthesizes recent research on the diverse roles of butyrate, across various livestock species. As a short-chain fatty acid, butyrate is known for enhancing intestinal development, improving immune function, and modulating microbial diversity. Studies indicate that butyrate supports gut barrier integrity, reduces inflammation, and optimizes feed efficiency, especially during the critical weaning and post-weaning periods in calves, piglets, and lambs. Supplementation with butyrate in livestock has been shown to increase average daily gain (ADG), improve gut microbiota balance, promote growth, enhance gut health, boost antioxidant capacity, and reduce diarrhea. Additionally, butyrate plays a role in the epigenetic regulation of gene expression through histone acetylation, influencing tissue development and immune modulation. Its anti-inflammatory and antioxidant effects have been demonstrated across various species, positioning butyrate as a potential therapeutic agent in animal nutrition. This review suggests that optimizing butyrate supplementation strategies to meet the specific needs of each species may yield additional benefits, establishing butyrate as an important dietary additive for enhancing growth performance and health in livestock.

Background Lysine acetylation in proteins is a ubiquitous and conserved post-translational modification, playing a critical regulatory role in almost every aspect of living cells. Although known for many years, its function remains elusive in Fusarium graminearum , one of the most important necrotrophic plant pathogens with huge economic impact. Results By the combination of affinity enrichment and high-resolution LC-MS/MS analysis, large-scale lysine acetylome analysis was performed. In total, 577 lysine acetylation sites matched to 364 different proteins were identified. Bioinformatics analysis of the acetylome showed that the acetylated proteins are involved in a wide range of cellular functions and exhibit diverse subcellular localizations. Remarkably, 10 proteins involved in the virulence or DON (deoxynivalenol) biosynthesis were found to be acetylated, including 4 transcription factors, 4 protein kinases and 2 phosphatases. Protein-protein interaction network analysis revealed that acetylated protein complexes are involved in diversified interactions. Conclusions This work provides the first comprehensive survey of a possible lysine acetylome in F. graminearum and reveals previously unappreciated roles of lysine acetylation in the regulation of diverse biological processes. This work provides a resource for functional analysis of acetylated proteins in filamentous fungi.

Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causes a respiratory disease called coronavirus disease 2019 (COVID-19), the spread of which has led to a pandemic. An effective preventive vaccine against this virus is urgently needed. As an essential step during infection, SARS-CoV-2 uses the receptor-binding domain (RBD) of the spike protein to engage with the receptor angiotensin-converting enzyme 2 (ACE2) on host cells 1 , 2 . Here we show that a recombinant vaccine that comprises residues 319–545 of the RBD of the spike protein induces a potent functional antibody response in immunized mice, rabbits and non-human primates ( Macaca mulatta ) as early as 7 or 14 days after the injection of a single vaccine dose. The sera from the immunized animals blocked the binding of the RBD to ACE2, which is expressed on the cell surface, and neutralized infection with a SARS-CoV-2 pseudovirus and live SARS-CoV-2 in vitro. Notably, vaccination also provided protection in non-human primates to an in vivo challenge with SARS-CoV-2. We found increased levels of RBD-specific antibodies in the sera of patients with COVID-19. We show that several immune pathways and CD4 T lymphocytes are involved in the induction of the vaccine antibody response. Our findings highlight the importance of the RBD domain in the design of SARS-CoV-2 vaccines and provide a rationale for the development of a protective vaccine through the induction of antibodies against the RBD domain. A recombinant vaccine that targets the receptor-binding domain of the spike protein of SARS-CoV-2 induces a potent antibody response in immunized mice, rabbits and non-human primates, and protects primates from infection with the virus.