Study on ion-coupled subunit interaction of Na-HransbcatingV-ATPase

Na-HransbcateV-ATP酶离子耦合亚基相互作用的研究

• 批准号: 17570117
• 负责人: KAKINUMA Yoshimi
• 金额: $ 2.3万
• 依托单位: Ehime University
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 2005
• 资助国家: 日本
• 起止时间: 2005 至 2006
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-17570117/
• 关键词: V-ATPase; Sodium; Ion; Enterococcus hirae

(i) The membrane rotor ring from the vacuolar-type (V-type) sodium ion-pumping adenosine triphosphatase (Na+-ATPase) from Enterococcus hirae consists of 10 NtpK subunits, which are homologs of the 16-kilodalton and 8-kilodalton proteolipids found in other V-ATPases and in FIFo-or F-ATPases, respectively. Each NtpK subunit has four transmembrane alpha helices, with a sodium ion bound between helices 2 and 4 at a site buried deeply in the membrane that includes the essential residue glutamate-139. This site is probably connected to the membrane surface by two half-channels in subunit NtpI, against which the ring rotates. Symmetry mismatch between the rotor and catalytic domains appears to be an intrinsic feature of both V-and F-ATPases.(ii) By biochemical analysis of V-ATPase complex formation with the ntp gene-deleted mutant strains, we found that the VI portion is composed of subunit A, B, C, D, E, F, G and V0 portion of subunit I and K. Subunit B is not necessary to form the ACDIK complex, and subunit A plays a key role for V0V1 complex formation. All these results are important for understanding the molecular interaction of V-ATPase subunits during ion translocation.

(i)来自肠球菌的液泡型（V型）钠离子泵三磷酸腺苷酶（Na+-ATP酶）的膜转子环由10个NtpK亚基组成，它们分别是在其他V-ATP酶和FIFo-或F-ATP酶中发现的16千道尔顿和8千道尔顿蛋白脂的同系物。每个NtpK亚基有四个跨膜α螺旋，在螺旋2和4之间的一个位点上有一个钠离子，该位点深埋在膜中，包括必需残基谷氨酸-139。这个网站可能是连接到膜表面的两个半通道亚基NtpI，对环旋转。转子和催化结构域之间的对称性错配似乎是V-ATP酶和F-ATP酶的内在特征。(ii)通过对ntp基因缺失突变株V-ATPase复合物形成的生化分析，发现V1部分由A、B、C、D、E、F、G亚基和I、K亚基的V0部分组成。亚基B不是形成ACDIK复合物所必需的，而亚基A在V0 V1复合物的形成中起关键作用。这些结果对于理解V-ATP酶亚基在离子转运过程中的分子相互作用具有重要意义。

项目成果

Deletion analysis of the subunit gene of V-type Na^+-ATPase from Enterococcus hirae

海拉肠球菌V型Na^-ATP酶亚基基因的缺失分析

• 发表时间: 2006
• 期刊: J. Biochem (Tokyo) 139
• 作者: T.Hosaka;K.Takase;T.Murata;Y.Kakinuma;I.Yamato
• 通讯作者: I.Yamato

Structure of the rotor ring of the V-type Na+-ATPaseJ a model for ion translocation of a rotary motor revealed from the X-ray structure

V型Na-ATP酶转子环结构J从X射线结构揭示旋转电机离子易位模型

• 发表时间: 2006
• 期刊: Seibutsu butsuri 46(6)
• 作者: Murata;T.;Yamato;I.;Kakinuma;Y.
• 通讯作者: Y.

Structure of the rotor of Enterococcus hirae V-ATPase and medicinal science

希拉肠球菌V-ATP酶转子的结构与医学科学

• 发表时间: 2006
• 期刊: Bioscience and industry 64(2)
• 作者: Kakinuma;Y
• 通讯作者: Y

Structure and mechanism of vacuolar Na+-translocating ATPase from Enterococcus hirae

• DOI: 10.1007/s10863-005-9481-0
• 发表时间: 2005-12-01
• 期刊: JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
• 影响因子: 3
• 作者: Murata, T;Yamato, I;Kakinuma, Y
• 通讯作者: Kakinuma, Y

Structure of the rotor of the V-type Na+-ATPase from Enterococcus hirae

• DOI: 10.1126/science.1110064
• 发表时间: 2005-04-29
• 期刊: SCIENCE
• 影响因子: 56.9
• 作者: Murata, T;Yamato, I;Walker, JE
• 通讯作者: Walker, JE