High impact information on ATGSR1

• GLN1;4 was another high affinity-type GS1 expressed in nitrogen-starved plants but was 10-fold less abundant than GLN1;1 [1].
• By contrast, the high affinity isoenzyme, GLN1;1 (Km for ammonium < 10 microm; Km for glutamate = 1.1 +/- 0.4 mm) was abundantly accumulated in the surface layers of roots during nitrogen limitation and was down-regulated by ammonium excess [1].
• Phosphorylation assays revealed that AtGLN1;1 could be specifically phosphorylated by AtCRK3 in vitro [2].
• In addition, both AtGLN1;1 and AtCRK3 could be induced by natural or artificially induced leaf senescence, implying that such interaction may be involved in the regulation of nitrogen remobilization during leaf senescence [2].
• Further analyses indicated that AtGLN1;1 could interact specifically with AtCRK3 and the kinase domain of AtCRK3 and the catalytic domain of AtGLN1;1 were responsible for such interaction, respectively [2].

Other interactions of ATGSR1

• Four distinct GS cDNA clones, lambda Atgsl1, lambda Atgsr1, lambda Atgsr2 and lambda Atkb6 were isolated and characterized [3].

References