Carlson H C, Lu S, Kroos L, Haldenwang W G
Department of Microbiology, University of Texas Health Science Center, San Antonio 78284, USA.
J Bacteriol. 1996 Jan;178(2):546-9. doi: 10.1128/jb.178.2.546-549.1996.
sigma E and sigma K are sporulation-specific sigma factors of Bacillus subtilis that are synthesized as inactive proproteins. Pro-sigma E and pro-sigma K are activated by the removal of 27 and 20 amino acids, respectively, from their amino termini. To explore the properties of the precursor-specific sequences, we exchanged the coding elements for these domains in the sigma E and sigma K structural genes and determined the properties of the resulting chimeric proteins in B. subtilis. The pro-sigma E-sigma K chimera accumulated and was cleaved into active sigma K, while the pro-sigma K-sigma E fusion protein failed to accumulate and is likely unstable in B. subtilis. A fusion of the sigE "pro" sequence to an unrelated protein (bovine rhodanese) also formed a protein that was cleaved by the pro-sigma E processing apparatus. The data suggest that the sigma E pro sequence contains sufficient information for pro-sigma E processing as well as a unique quality needed for sigma E accumulation.
σE和σK是枯草芽孢杆菌的芽孢形成特异性σ因子,它们以无活性的前体蛋白形式合成。前体σE和前体σK分别通过从其氨基末端去除27个和20个氨基酸而被激活。为了探究前体特异性序列的特性,我们在σE和σK结构基因中交换了这些结构域的编码元件,并测定了所得嵌合蛋白在枯草芽孢杆菌中的特性。前体σE-σK嵌合体积累并被切割成活性σK,而前体σK-σE融合蛋白未能积累,并且在枯草芽孢杆菌中可能不稳定。sigE“前体”序列与一种不相关的蛋白(牛硫氰酸酶)的融合也形成了一种被前体σE加工装置切割的蛋白。数据表明,σE前体序列包含前体σE加工所需的足够信息以及σE积累所需的独特性质。