Significance Lignin is a defining polymer of vascular plants and of great physiological, ecological, and economical importance. Yet, its polymerization in the cell wall is still not understood. Lignin polymerizing enzymes, laccases and peroxidases, exist in vast numbers in plant genomes. By focusing on a specific lignin structure, the ring-like Casparian strips (CSs), we reduced candidate numbers and abolished essentially all laccases with detectable endodermal expression. Yet, not even slight defects in CS formation were detected. By contrast, a quintuple peroxidase mutant displayed a complete absence of CS. Our findings suggest that cells lignify differently depending on whether lignin is localized or ubiquitous and whether cells stay alive during and after lignification, as well as the composition of the cell wall.