Characterization of the interaction of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum with bacterial membranes.
Characterization of the interaction of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum with bacterial membranes.
复制标题
红色红螺菌二硝基酶还原酶激活糖水解酶与细菌膜相互作用的表征。
DOI：
10.1007/s002030050739
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发表时间：
1999
影响因子：
2.8
通讯作者：
Ludden,PW
中科院分区：
文献类型：
--
作者：
Halbleib,CM;Ludden,PW
表征了二硝基酶还原酶激活糖水解酶 (DRAG) 与细菌膜的相互作用以及 DRAG 对核苷酸的溶解作用。来自红色红螺菌的纯化 DRAG 可逆地结合来自 Rsp 的细菌沉淀部分。 rubrum 和其他固氮细菌。 DRAG 饱和了 Rsp 的膜部分。 rubrumat 的浓度为 0.2 mol DRAG/mol 细菌叶绿素，表明 DRAG 结合物质在膜中普遍存在。 DRAG 与磷脂囊泡的结合较差，表明 DRAG 与膜相互作用需要蛋白质。鸟苷和尿苷三核苷酸和二核苷酸特异性地将DRAG从Rsp的沉淀级分中解离。 rubrum和Azotobacter vinelandii，而腺苷核苷酸没有解离作用。鸟苷 5'-三磷酸从膜上解离 DRAG，其浓度导致 50% 解离 (EC50) 为 5.0 ± 0.5 mM；二磷酸鸟苷的 EC50 为 15.0 ± 2.0 mM。我们认为 GTP 是 DRAG 调节的潜在参与者，可能控制 DRAG 与膜的关联程度。
The interaction of dinitrogenase reductase-activating glycohydrolase (DRAG) with bacterial membranes and the solubilization of DRAG in response to nucleotides were characterized. Purified DRAG fromRhodospirillum rubrumreversibly bound bacterial pellet fractions fromRsp. rubrumand other nitrogen-fixing bacteria. DRAG saturated the membrane fraction ofRsp. rubrumat a concentration of 0.2 mol DRAG/mol bacteriochlorophyll, suggesting that the DRAG-binding species is prevalent in the membrane. DRAG bound poorly to phospholipid vesicles, suggesting a protein requirement for DRAG interaction with the membrane. Guanosine and uridine tri- and di-nucleotides specifically dissociated DRAG from the pellet fractions ofRsp. rubrumandAzotobacter vinelandii, while adenosine nucleotides had no dissociative effect. Guanosine 5′-triphosphate dissociated DRAG from the membrane at a concentration causing 50% dissociation (EC50) of 5.0 ± 0.5 mM; guanosine disphosphate had an EC50of 15.0 ± 2.0 mM. We propose that GTP is a potential participant in the regulation of DRAG, possibly controlling the extent of DRAG association with the membrane.