Jagodzik P, Jackowski G
Department of Plant Physiology, Institute of Experimental Biology, Adam Mickiewicz University, ul. Uniwersytetu Poznańskiego 6, 61-614 Poznań, Poland.
Photosynthetica. 2022 Feb 15;60(2):212-218. doi: 10.32615/ps.2022.004. eCollection 2022.
Little data on the role played by chloroplast protein AtDeg2 as a chaperone is available. Therefore, we sought for chloroplast proteins protected from high irradiance-induced interprotein aggregation disulphide bridges by AtDeg2 acting as a holdase. To reach this goal, we performed analyses which involved comparative diagonal electrophoreses of lysates of chloroplasts isolated from wild type (WT) plants and transgenic plants which expressed AtDeg2 lacking its chaperone activity but retaining the protease activity. The results of the analyses indicate that AtDeg2 acting as a holdase prevents a single chloroplast protein, ., the γ subunit of ATP synthase from long-term high irradiance-induced homodimerization mediated by disuplhide bridges and this allows us to better understand a complexity of physiological significance of AtDeg2 - the chloroplast protein of dual protease/chaperone activity.
关于叶绿体蛋白AtDeg2作为伴侣蛋白所起作用的数据很少。因此，我们寻找了受AtDeg2作为保持酶保护而免受高辐照度诱导的蛋白质间聚集二硫键影响的叶绿体蛋白。为了实现这一目标，我们进行了分析，其中包括对从野生型（WT）植物和表达缺乏伴侣活性但保留蛋白酶活性的AtDeg2的转基因植物中分离出的叶绿体裂解物进行比较对角线电泳。分析结果表明，AtDeg2作为保持酶可防止单一叶绿体蛋白，即ATP合酶的γ亚基通过二硫键介导的长期高辐照度诱导的同型二聚化，这使我们能够更好地理解AtDeg2（具有双重蛋白酶/伴侣活性的叶绿体蛋白）生理意义的复杂性。
