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Essential role of urease in germination of nitrogen-limited Arabidopsis thaliana seeds

Author:
Zonia, L.E., Stebbins, N.E., Polacco, J.C.
Source:
Plant physiology 1995 v.107 no.4 pp. 1097-1103
ISSN:
0032-0889
Subject:
Arabidopsis thaliana, seed germination, urease, enzyme activity, nitrogen, nutrient deficiencies, biogeochemical cycles, seedlings, developmental stages, phenyl phosphorodiamidate, urea, nutrient transport, genes, chromosome mapping, gene expression, plant morphology, chemical constituents of plants, transcription (genetics), binding sites
Abstract:
In Arabidopsis thaliana, urease transcript levels increased sharply between 2 and 4 d after germination (DAG) and were maintained at maximal levels until at least 8 DAG. Seed urease specific activity declined upon germination but began to increase in seedlings 2 DAG, reaching approximately 75% of seed activity by 8 DAG. Urea levels showed a small transient increase 1 DAG and then approximately paralleled urease activity, reaching maximal levels at approximately 9 DAG. Urease inhibition with phenylphosphorodiamidate resulted in a 2- to 4-fold increase in urea levels throughout seedling development. Arginine pools (0-8 DAG) changed approximately in parallel with the urea pool. Consistent with arginine being a major source of urea, arginase activity increased 10-fold in the interval 0 to 6 DAG. Allopurinol, a xanthine dehydrogenase inhibitor, had no effect on urea levels up to 3 DAG but reduced the urea pool by 30 to 40% during the interval 5 to 8 DAG, suggesting that purine degradation contributed to the urea pool well after germination, if at all. In aged Arabidopsis seeds, there was a correlation between phenylphosphorodiamidate inactivation of urease and germination inhibition, the latter overcome by NH4NO3 or amino acids. Since urease activity, urea precursor, and urea increase in young seedlings, and since urease inactivation results in a nitrogen-reversible inhibition of germination, we propose that urease recycles urea-nitrogen in the seedling.
Agid:
664763