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Root xylem transport of amino acids in the root hemiparasitic shrub Olax phyllanthi (Labill) R.Br. (Olacaceaea) and its multiple hosts
Author(s) -
PATE J. S.,
WOODALL G.,
JESCHKE W. D.,
STEWART G. R.
Publication year - 1994
Publication title -
plant, cell and environment
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.646
H-Index - 200
eISSN - 1365-3040
pISSN - 0140-7791
DOI - 10.1111/j.1365-3040.1994.tb00528.x
Subject(s) - xylem , haustorium , biology , botany , amino acid , asparagine , host (biology) , biochemistry , ecology
The amino acid compositions of the root xylem saps of Olax phyllanthi and a range of its common hosts were examined in native coastal heath in Western Australia and in pot cultures of Olax reliant on single hosts. When hosts specializing in the xylem transport of one major solute (asparagine, glutamine, histidine, arginine or proline) were exploited, the endophytic tissue of haustoria and the xylem sap of Olax showed much lower proportions of this than of other solutes, suggesting pronounced metabolic transformation prior to xylem loading by the parasite. However, the xylem sap of Olax did partly reflect the compositions of its hosts; for example, djenkolic acid and pipecolic acid were present when Olax was parasitic on species of Acacia , and levels of citrulline and aspartic acid were higher than normal when it exploited hosts transporting large amounts of these compounds. Back‐flow of S‐ethenyl cysteine, a novel amino acid specific to Olax , was observed to another root hemiparasite ( Exocarpos sparteus ) in native habitat and to certain non‐parasitic hosts in water‐stressed pot cultures. Haustoria exhibited high levels of glutamine synthetase but showed appreciable in vivo nitrate reductase activity only when on hosts with high xylem levels of nitrate.