Parker W, Wells T A, Meza-Keuthen S, Kim I S, Song P S
Department of Chemistry, University of Nebraska, Lincoln 68588-0304, USA.
J Protein Chem. 1995 Feb;14(2):53-7. doi: 10.1007/BF01888362.
Recently, Mummert et al. [Nature 363, 644-648 (1993)] isolated a proposed TCP1-related chaperone. Here we report several findings concerning the protein which they sequenced. Two similar N-terminal sequences were obtained from this abundant 60-kDa protein. Internal sequences were also acquired by protease digestion. Initially it was believed the protein was able to completely inhibit citrate synthase aggregation, but later purifications demonstrated that the 60-kDa polypeptide lacked both chaperone activity and the previously reported kinase activity [Grimm et al., Planta 178, 199-206 (1989)]. It is now our belief that this protein is neither a chaperone nor a kinase.
最近,穆默特等人[《自然》363, 644 - 648 (1993)]分离出一种推测与TCP1相关的伴侣蛋白。在此我们报告一些关于他们测序的这种蛋白质的发现。从这种丰富的60 kDa蛋白质中获得了两个相似的N端序列。通过蛋白酶消化也获得了内部序列。最初认为该蛋白质能够完全抑制柠檬酸合酶的聚集,但后来的纯化表明,这种60 kDa的多肽既缺乏伴侣活性,也缺乏先前报道的激酶活性[格林姆等人,《植物》178, 199 - 206 (1989)]。我们现在认为这种蛋白质既不是伴侣蛋白也不是激酶。