Characterization of BspA, a major boiling-stable, water-stress-responsive protein in aspen (Populus tremula).

We identified a novel 66 kDa boiling-stable protein (BspA) in cultured shoots of aspen (Populus tremula L.) which was highly expressed in response to gradual water stress. The BspA protein, which was highly expressed as early as 1 h after initiation of a drought treatment, accumulated during progressive water stress, decreased on rehydration, and was expressed in response to abscisic acid (ABA) application, as detected by SDS-PAGE protein analysis and Western blotting. Anti-BspA antibodies also cross-reacted with a 119 kDa protein. The 119 kDa protein was also induced by water stress, but it was detected only in the total protein fraction and not in the heat-stable fraction. The BspA protein cross-reacted with antibodies raised against a water-stress-responsive protein isolated from the African resurrection plant Craterostigma plantagineum Hochst. The N-terminal amino acid sequence of BspA was determined and exhibited high homology with the wheat germins GF-2.8 and GF-3.8. The BspA protein was the only major, water-stress-responsive boiling-stable protein detected in aspen.