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Objective: The objective of this research study was to obtain the varietal description of two varieties of manzano chili pepper in Las Montañas region, in central Veracruz, Mexico. Design/methodology/approach: The varietal characterization module was established under greenhouse conditions. The markers recorded were in accordance with the International Plant Genetic Resources Institute for Capsicum and the Graphic Handbook for Variety Description of manzano chili pepper. The plants were characterized from seedling in greenhouse to adult plant. The agronomic management of the crop was carried out in accordance with the manual for the production of manzano chili pepper in Las Montañas, state of Veracruz. Results: All qualitative markers were constant for the two varieties, MEXUVNE1-15-C2 and MEXUVCU1-16-C2, from seedling to fruit setting. In contrast, there were dissimilarities in plant height, and stem, leaf, flower, fruit and seed dimensions. Study limitations/implications: The pandemic caused by COVID-19 was the main limitation, resulting in some markers not being recorded in a timely manner as indicated in the Graphic Handbook. Findings/conclusions: Both varieties are very similar; however, the greatest distinction was in the quantitative markers, such as: plant height, fruit length, fruit diameter and number of seeds.

Bax proteins form pores in the mitochondrial outer membrane to initiate apoptosis. This might involve their embedding in the cytosolic leaflet of the lipid bilayer, thus generating tension to induce a lipid pore with radially arranged lipids forming the wall. Alternatively, Bax proteins might comprise part of the pore wall. However, there is no unambiguous structural evidence for either hypothesis. Using NMR, we determined a high‐resolution structure of the Bax core region, revealing a dimer with the nonpolar surface covering the lipid bilayer edge and the polar surface exposed to water. The dimer tilts from the bilayer normal, not only maximizing nonpolar interactions with lipid tails but also creating polar interactions between charged residues and lipid heads. Structure‐guided mutations demonstrate the importance of both types of protein–lipid interactions in Bax pore assembly and core dimer configuration. Therefore, the Bax core dimer forms part of the proteolipid pore wall to permeabilize mitochondria., NMR structures of membrane‐bound Bax core dimer reveal dual interactions with non‐polar tails and charged heads of bilayer lipids contributing directly to apoptotic mitochondrial permeabilization.

SummaryBax proteins form pores in the mitochondrial outer membrane to initiate apoptosis. They may embed in the cytosolic leaflet of the lipid bilayer generating tension to induce a lipid pore with radially arranged lipids forming the wall. Alternatively, they may comprise part of the pore wall. However, there is no unambiguous structural evidence for either hypothesis. Using NMR, we determine a high-resolution structure of the Bax core region that forms a dimer with the nonpolar surface covering the lipid bilayer edge and the polar surface exposed to water. The dimer tilts from the bilayer normal, not only maximizing nonpolar interactions with lipid tails but creating polar interactions between charged residues and lipid heads. Structure-guided mutations demonstrate the importance of both protein-lipid interactions in Bax pore assembly and core dimer configuration. Therefore, the Bax core dimer forms part of the proteolipid pore wall to permeabilize mitochondria.