Setlow B, Setlow P
Department of Biochemistry, University of Connecticut Health Center, Farmington 06030, USA.
J Bacteriol. 1995 Jul;177(14):4149-51. doi: 10.1128/jb.177.14.4149-4151.1995.
Binding of alpha/beta-type, small, acid-soluble proteins from Bacillus subtilis and Clostridium bifermentans to DNA protected these proteins against cleavage by their specific protease (GPR) as well as by trypsin and chymotrypsin. These data suggest that alpha/beta-type, small, acid-soluble protein binding to DNA (i) may result in a structural change in these proteins, giving a more compact protein structure, and (ii) may be important in slowing the degradation of these proteins by GPR, in particular during sporulation.
来自枯草芽孢杆菌和双发酵梭菌的α/β型小酸溶性蛋白质与DNA的结合保护了这些蛋白质,使其免受其特异性蛋白酶(GPR)以及胰蛋白酶和胰凝乳蛋白酶的切割。这些数据表明,α/β型小酸溶性蛋白质与DNA的结合(i)可能导致这些蛋白质发生结构变化,形成更紧凑的蛋白质结构,并且(ii)可能在减缓这些蛋白质被GPR降解方面很重要,特别是在孢子形成过程中。