Plasmid Control of 6-Aminohexanoic Acid Cyclic Dimer Degradation Enzymes of Flavobacterium sp. K172
Plasmid Control of 6-Aminohexanoic Acid Cyclic Dimer Degradation Enzymes of Flavobacterium sp. K172
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黄杆菌属 6-氨基己酸环状二聚体降解酶的质粒控制。
DOI：
10.1128/jb.143.1.238-245.1980
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发表时间：
1980
影响因子：
3.2
通讯作者：
H. Okada
中科院分区：
文献类型：
--
作者：
S. Negoro;H. Shinagawa;A. Nakata;S. Kinoshita;Tomoya Hatozaki;H. Okada
黄杆菌属K172能够在作为唯一碳源和氮源的6-氨基己酸环状二聚体上生长，并且研究了负责酶、6-氨基己酸环状二聚体水解酶和6-氨基己酸线性低聚物水解酶的质粒控制。 K172野生株含有三种质粒：pOAD1（26.2兆道尔顿）、pOAD2（28.8兆道尔顿）和pOAD3（37.2兆道尔顿）。丝裂霉素 C 很容易消除野生菌株 K172 在环状二聚体上生长的能力，并且环状二聚体水解酶无法通过催化活性或抗体沉淀来检测。没有检测到治愈菌株的回复。 pOAD2 并未在每个测试的治愈菌株中检测到，但在转化体中得到恢复。转化体恢复了两种酶活性，并且转化体的环状二聚体水解酶在免疫学上与野生株相同。所有测试的菌株，包括野生菌株、治愈菌株和转化菌株，无论代谢活性如何，都具有相同的 pOAD3。一些治愈菌株拥有与野生菌株相同的 pOAD1，但其他菌株则含有结构部分改变的质粒，这些质粒可能是通过删除、插入或替换等遗传重排从 pOAD1 衍生而来。这些结果表明这些酶的基因是在pOAD2上携带的。
Flavobacterium sp. K172, which is able to grow on 6-aminohexanoic acid cyclic dimer as the sole source of carbon and nitrogen, and plasmid control of the responsible enzymes, 6-aminohexanoic acid cyclic dimer hydrolase and 6-aminohexanoic acid linear oligomer hydrolase, were studied. The wild strain of K172 harbors three kinds of plasmid, pOAD1 (26.2 megadaltons), pOAD2 (28.8 megadaltons), and pOAD3 (37.2 megadaltons). The wild strain K172 was readily cured of its ability to grow on the cyclic dimer by mitomycin C, and the cyclic dimer hydrolase could not be detected either as catalytic activity or by antibody precipitation. No reversion of the cured strains was detected. pOAD2 was not detected in every cured strain tested but was restored in a transformant. The transformant recovered both of the enzyme activities, and the cyclic dimer hydrolase of the transformant was immunologically identical with that of the wild strain. All of the strains tested, including the wild, cured, and transformant ones, possessed identical pOAD3 irrespective of the metabolizing activity. Some of the cured strains possessed pOAD1 identical with the wild strain, but the others harbored plasmids with partially altered structures which were likely to be derived from pOAD1 by genetic rearrangements such as deletion, insertion, or substitution. These results suggested that the genes of the enzymes were borne on pOAD2.