Iron Deficiency Decreases Suberization in Bean Roots through a Decrease in Suberin-Specific Peroxidase Activity.

Abstract

The suberin content of young root parts of iron-deficient and iron-sufficient Phaseolus vulgaris L. cv Prélude was determined. The aliphatic components that could be released from suberin-enriched fractions by LiAID(4) depolymerization were identified by gas chromatography-mass spectrometry. In the normal roots, the major aliphatic components were omega-hydroxy acids and dicarboxylic acids in which saturated C(16) and monounsaturated C(18) were the dominant homologues. Iron-deficient bean roots contained only 11% of the aliphatic components of suberin found in control roots although the relative composition of the constituents was not significantly affected by iron deficiency. Analysis of the aromatic components of the suberin polymer that could be released by alkaline nitrobenzene oxidation of bean root samples showed a 95% decrease in p-hydroxybenzaldehyde, vanillin, and syringaldehyde under iron-deficient conditions. The inhibition of suberin synthesis in bean roots was not due to a decrease in Fe-dependent omega-hydroxylase activity since normal omega-hydroxylation could be demonstrated, both in vitro with microsomal preparations and in situ by labeling of omega-hydroxy and dicarboxylic acids with [(14)C]acetate. The level of the isozyme of peroxidase that is specifically associated with suberization was suppressed by iron deficiency to 25% of that found in control roots. None of the other extracted isozymes of peroxidase was affected by the iron nutritional status. The activity of the suberin-associated peroxidase was restored within 3 to 4 days after application of iron to the growth medium. The results suggest that, in bean roots, iron deficiency causes inhibition of suberization by causing a decrease in the level of isoperoxidase activity which is required for polymerization of the aromatic domains of suberin, while the ability to synthesize the aliphatic components of the suberin polymer is not impaired.