Struglics A, Fredlund K M, Møller I M, Allen J F
Plant Cell Biology, Lund University, Sweden.
Biochem Biophys Res Commun. 1998 Feb 24;243(3):664-8. doi: 10.1006/bbrc.1998.8151.
Inside-out submitochondrial particles from potato tuber mitochondria were incubated with [gamma-32P]ATP. More than 16 phosphorylated polypeptides were detected by autoradiography on an SDS-gel. Two phosphoproteins, migrating at 22 and 28 kDa, were excised from the SDS-gel, electroeluted, and purified further by anion chromatography. The phosphoproteins were N-terminally sequenced. Over the regions sequenced, the 22 and 28 kDa phosphoproteins had 100% sequence identity with potato proteins identified as the delta'-subunit of the F1-ATPase and the b-subunit of the F0-ATPase, respectively. We suggest that phosphorylation of these proteins may control the interaction between F1 and F0 and regulate energy coupling in oxidative phosphorylation.
将来自马铃薯块茎线粒体的内翻式亚线粒体颗粒与[γ-32P]ATP一起温育。通过SDS凝胶上的放射自显影检测到超过16种磷酸化多肽。从SDS凝胶上切下两条迁移率分别为22 kDa和28 kDa的磷蛋白，进行电洗脱，并通过阴离子色谱进一步纯化。对磷蛋白进行N端测序。在所测序的区域中，22 kDa和28 kDa的磷蛋白分别与被鉴定为F1-ATP酶的δ'-亚基和F0-ATP酶的b-亚基的马铃薯蛋白具有100%的序列同一性。我们认为这些蛋白质的磷酸化可能控制F1和F0之间的相互作用，并调节氧化磷酸化中的能量偶联。
