The regulation of glutamine synthetase (GS) from Agaricus bisporus was stud
ied at the posttranscriptional level using a specific antibody fraction dir
ected against purified GS. The cross-reactivity of the antiserum against va
rious Agaricus species and other fungi was tested and low reactivity with t
he Ascomycetes was found. GS protein and activity levels were measured in c
ell-free extracts of mycelium grown on different N sources. In mycelium gro
wn on glutamine or ammonium as N source, the biosynthetic GS activity is hi
gher than the transferase activity. Moreover, the results show a correlatio
n between GS biosynthetic activity, GS protein, and previously reported mRN
A levels. Also, after addition of ammonium or glutamine to glutamate-utiliz
ing cultures, transferase activity decreased more rapidly than biosynthetic
activity and GS protein level. This suggests a conformational modification
which only affects transferase activity. (C) 1999 Academic Press.