Salt-stress-responsive membrane proteins in Rhodobacter sphaeroides f. sp. denitrificans IL 106.
The salt-mediated-stress response in Rhodobacter sphaeroides f. sp. denitrificans IL 106 was investigated by culturing cells in the presence and in the absence of NaCl in growth media. Fractionation of cells followed by SDS-PAGE and 2D-PAGE revealed an increase in the levels of membrane proteins of 39 and 50 kDa and a decrease in the level of a membrane protein of 52 kDa with increasing levels of external NaCl. The proteins were isolated and sequenced. The polypeptide of 50 kDa in the inner membrane was assigned to an ATP synthase beta chain and that of 52 kDa in the outer membrane to a flagellar filament protein. As the N terminal of the 39 kDa protein in the outer membrane was blocked, partial proteolysis was carried out and four peptides were sequenced. Each sequence exhibited no significant homology with those available in databases, suggesting that the polypeptide of 39 kDa (named SspA) is a novel salt-stress-induced protein.
Xu
X
X
Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo, Tokyo 113-8657, Japan.
Abo
M
M
Okubo
A
A
Yamazaki
S
S