Chitinases produced by Paenibacillus illinoisensis and Bacillus thuringiensis subsp. pakistani degrade Nod factor from Bradyrhizobium japonicum.
Chitinases produced by Paenibacillus illinoisensis and Bacillus thuringiensis subsp. pakistani degrade Nod factor from Bradyrhizobium japonicum.
复制标题
伊利诺伊州类芽孢杆菌和苏云金芽孢杆菌亚种产生的几丁质酶。
DOI：
10.1016/j.micres.2006.06.013
复制
发表时间：
2008
影响因子：
6.7
通讯作者：
Donald L. Smith
中科院分区：
文献类型：
--
作者：
W. Jung;F. Mabood;A. Souleimanov;R. Park;Donald L. Smith
几丁质酶是水解几丁质内部 β-1,4-N-乙酰基-d-葡萄糖胺键的酶。由于Nod因子的骨架是几丁质低聚物，我们研究了土壤细菌伊利诺类芽孢杆菌KJA-424和苏云金芽孢杆菌亚种是否产生几丁质酶。巴基斯坦 HD 395 能够降解日本慢生根瘤菌 (Bradyrhizobium japonicum) 产生的 Nod 因子，当存在几丁质酶时，这种现象可能会破坏日本慢生根瘤菌 (Bradyrhizobium japonicum)-大豆信号传导和根瘤建立。纯化的 Nod 因子 [LCO Nod Bj-V (C18:1, MeFuc)] 从日本慢生根瘤菌 (Bradyrhizobium japonicum) 中分离出来，并与从 KJA-424 和 HD395 中分离的粗几丁质酶一起孵育，有或没有醋酸盐缓冲液。孵育15小时后，通过HPLC对所得溶液中的Nod因子进行定量。在醋酸盐缓冲液中用 KJA-424 (91.9%) 和 HD395 (86.5%) 几丁质酶处理后降解最大。包含醋酸盐缓冲液的处理比不含醋酸盐缓冲液的处理具有更高的降解水平。对于所有处理，降解率均大于 77%。
Chitinases are enzymes that hydrolyze internal β-1,4-N-acetyl-d-glucosamine linkages of chitin. Since the backbone of Nod factors is a chitin oligomer, we investigated whether chitinases produced by soil bacteria Paenibacillus illinoisensis KJA-424 and Bacillus thuringiensis subsp. Pakistani HD 395 are able to degrade Nod factor produced by Bradyrhizobium japonicum, a phenomenon that could disrupt B. japonicum-soybean signaling and nodule establishment when chitinases are present. Purified Nod factor [LCO Nod Bj-V (C18:1, MeFuc)] was isolated from Bradyrhizobium japonicum and incubated with crude chitinases isolated from KJA-424 and HD395, with or without acetate buffer. After 15h of incubation, Nod factor in the resulting solution was quantified by HPLC. Degradation was greatest following treatment with KJA-424 (91.9%) and HD395 (86.5%) chitinases in acetate buffer. Treatments that included acetate buffer had higher levels of degradation than those without. For all treatments degradation was greater than 77%.