Nitrogen forms in bark, wood and foliage of nitrogen-fertilized Pinus sylvestris

• Published in: Tree Physiology
• Main Authors: Nordin, Annika, Uggla, Claes, Näsholm, Torgny
• Format: Text
• Language: English
• Published: Oxford University Press 2001
• Subjects: Original Articles; Northern Sweden
• Online Access: http://treephys.oxfordjournals.org/cgi/content/short/21/1/59; https://doi.org/10.1093/treephys/21.1.59

Cycling of soluble non-protein N compounds is thought to be indicative of the N-nutritional status of trees. We determined the major N forms in bark, wood and foliage and estimated the dependence of prevalent N forms on N availability in Pinus sylvestris L. trees from northern Sweden. Trees subjected to severe N limitation and trees that had been fertilized with an average 64 kg N ha−1 year−1 for 25 years were analyzed. Bark and wood samples were collected by tangentially cryo-sectioning the trunk into 30-μm thick sections, from the bark to the functional xylem. Soluble amino compounds were extracted from the sections for analysis. Sap samples from twigs were obtained by centrifugation, and bark samples from twigs were obtained by tissue extraction. In both needles and bark, arginine dominated the amino-N pool. Because arginine concentrations in needles increased with N fertilization, arginine dominance of the amino-N pool in needles was higher in N-fertilized trees than in control trees. In bark, N fertilization resulted in a large increase in glutamine concentration, so that glutamine accounted for a larger proportion of the amino-N pool in bark in N-fertilized trees than in control trees. Glutamine dominated the amino-N pool in wood of control trees. Nitrogen fertilization resulted in an increased proportion of arginine in the wood amino-N pool. We conclude that the composition of the amino-N pools in bark, wood and foliage is highly sensitive to N supply. The composition of the amino-N pools can contribute to the regulation of tree N-nutritional status, which is mediated by shoot to root signalling by long-distance transport of amino compounds.