Development-specific protein S of Myxococcus xanthus: purification and characterization.
Development-specific protein S of Myxococcus xanthus: purification and characterization.
复制标题
黄色粘球菌发育特异性蛋白 S：纯化和表征。
DOI：
10.1128/jb.148.2.678-683.1981
复制
发表时间：
1981
影响因子：
3.2
通讯作者：
Inouye,M
中科院分区：
文献类型：
--
作者：
Inouye,S;Harada,W;Zusman,D;Inouye,M
S蛋白是从黄色粘球菌发育后期的细胞中提纯并结晶得到的一种发育特异性蛋白。圆二色谱表明，无论有无钙离子，S蛋白都具有较高的β结构，这是S蛋白在粘孢子表面自组装所必需的。其氨基酸和羧基末端序列分别为丙氨酸-天冬氨酸-acid-isoleucine-glycine-valine-alanine-methionine-asparagine-asparagine-aspartic酸-苏氨酸-丝氨酸-丝氨酸和异亮氨酸-精氨酸(异亮氨酸、丝氨酸)。用胰酶消化相对分子质量为23,000的S蛋白，得到一个10,000个相对分子质量的抗胰酶核心蛋白。对该核心肽进行了纯化，并与蛋白质S进行了氨基酸组成比较。该核心肽能在钙离子存在下自组装到孢子表面，并与蛋白质S竞争结合到孢子表面。S蛋白与核心肽对孢子表面的亲和力之比为1.55。
Protein S, a development-specific protein of Myxococcus xanthus, was purified from the cells of a late stage of development and crystallized. Its circular dichroism spectra indicated that protein S had a high content of beta-structure in both the presence and absence of calcium ion, which is required for self-assembly of protein S on the myxospore surface. Its amino and carboxyl terminal sequences were determined to be alanine-aspartic acid-isoleucine-glycine-valine-alanine-methionine-asparagine-asparagine-aspartic acid-threonine-serine-serine and isoleucine-arginine (isoleucine, serine), respectively. When protein S (molecular weight, 23,000) was digested with trypsin, a trypsin-resistant core of 10,000 molecular weight was obtained. The core peptide was purified, and its amino acid composition was compared with that of protein S. The core peptide was capable of self-assembly on the spore surface in the presence of calcium ion and competed with protein S for binding on the spore surface. The ratio of affinity to the spore surface for protein S to that for the core peptide was 1.55.
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