Isolated ε subunit of thermophilic F1-ATPase binds ATP
Isolated ε subunit of thermophilic F1-ATPase binds ATP
复制标题
DOI：
10.1074/jbc.m306140200
复制
发表时间：
2003-09-19
影响因子：
4.8
通讯作者：
Yoshida, M
中科院分区：
文献类型：
--
作者：
Kato-Yamada, Y;Yoshida, M
F-1-ATP酶是F-0 F1-ATP合酶的可溶性部分，具有α（3）β（3）γ δ亚基结构，其中核苷酸结合位点位于α和β亚基中，并且据信不位于其它亚基中。然而，我们在这里报告，分离的F-1-ATP酶的ATP酶亚基从嗜热芽孢杆菌菌株PS 3可以结合ATP。通过凝胶过滤层析分离ATP亚基-ATP复合物直接证明结合。该结合不依赖于Mg 2+，但对ATP具有高度特异性;然而，ADP、GTP、UTP和CTP不能结合。缺少C-末端螺旋发夹的α-亚基不能结合ATP。尽管在相同条件下尚未检测到ATP与来自其他生物体的分离的ATP酶亚基的结合，但出现了一种可能性，即ATP酶亚基充当F0 F1-ATP合酶的细胞内ATP水平传感器。
F-1-ATPase, a soluble part of the F0F1-ATP synthase, has subunit structure alpha(3)beta(3)gammadeltaepsilon in which nucleotide-binding sites are located in the alpha and beta subunits and, as believed, in none of the other subunits. However, we report here that the isolated epsilon subunit of F-1-ATPase from thermophilic Bacillus strain PS3 can bind ATP. The binding was directly demonstrated by isolating the epsilon subunit-ATP complex with gel filtration chromatography. The binding was not dependent on Mg2+ but was highly specific for ATP; however, ADP, GTP, UTP, and CTP failed to bind. The epsilon subunit lacking the C-terminal helical hairpin was unable to bind ATP. Although ATP binding to the isolated epsilon subunits from other organisms has not been detected under the same conditions, a possibility emerges that the epsilon subunit acts as a built in cellular ATP level sensor of F0F1-ATP synthase.