Among the numerous strategies plants have developed to fend off enemy attack, antimicrobial peptides (AMPs) stand out as one of the most prominent defensive barriers that grant direct and durable resistance against a wide range of pests and pathogens. These small proteins are characterized by a compact structure and an overall positive charge. AMPs have an ancient origin and widespread occurrence in the plant kingdom but show an unusually high degree of variation in their amino acid sequences. Interestingly, there is a strikingly conserved topology among the plant AMP families, suggesting that the defensive properties of these peptides are not determined by their primary sequences but rather by their tridimensional structure. To explore and expand this idea, we here discuss the role of AMPs for plant defense from a structural perspective. We show how specific structural properties, such as length, charge, hydrophobicity, polar angle and conformation, are essential for plant AMPs to act as a chemical shield that hinders enemy attack. Knowledge on the topology of these peptides is facilitating the isolation, classification and even structural redesign of AMPs, thus allowing scientists to develop new peptides with multiple agronomical and pharmacological potential.
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Cover Image
Cover Image
The cover image shows an artistic representation of the fluorescence-based assay of deadenylase activity used by Pavanello et al. in this issue, with fluorescence proportional to enzyme activity. Fluorescence (λem = 528 nm) was detected in a multi-mode reader using 96-well plates. Activity of different enzyme complexes (left to right) was measured at various time points (top to bottom). Controls (inactive enzyme preparations and no enzyme controls) were also included (bottom two rows). Pavanello et al. report that the central region of CNOT1 and CNOT9 stimulates deadenylation by the Ccr4–Not nuclease module (see pages 3437–3450).
A structural perspective of plant antimicrobial peptides
Marcelo Lattarulo Campos, Luciano Morais Lião, Eliane Santana Fernandes Alves, Ludovico Migliolo, Simoni Campos Dias, Octávio Luiz Franco; A structural perspective of plant antimicrobial peptides. Biochem J 15 November 2018; 475 (21): 3359–3375. doi: https://doi.org/10.1042/BCJ20180213
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