Sagstetter M, Zimmermann R
Institut für Physiologische Chemie der Universität München, Federal Republic of Germany.
Biochem Biophys Res Commun. 1988 Jun 16;153(2):498-501. doi: 10.1016/s0006-291x(88)81122-7.
Processing of M13 procoat protein to transmembrane coat protein by dog pancreas microsomes is stimulated by a component of rabbit reticulocyte lysate and ATP. We asked whether this ATP-dependent reaction, involved in membrane assembly of procoat protein in the eukaryotic system, is related to the membrane potential dependent reaction observed for the membrane assembly of procoat protein in E. coli. Specifically, we asked if a mutant procoat protein which had been previously shown to be independent of the membrane potential with respect to its assembly in E. coli (M13am8H1R1 procoat protein) shows a stimulation by reticulocyte lysate and ATP in its assembly into microsomes. Since the mutant procoat protein behaved exactly as the wild type procoat protein in the eukaryotic in vitro system, we propose that the ATP-dependent reaction observed for the eukaryotic system does not substitute for the membrane potential dependent reaction in the prokaryotic system.
犬胰腺微粒体将M13前衣壳蛋白加工成跨膜衣壳蛋白的过程受到兔网织红细胞裂解物的一个组分和ATP的刺激。我们探究了这个参与真核系统中前衣壳蛋白膜组装的ATP依赖性反应,是否与在大肠杆菌中观察到的前衣壳蛋白膜组装的膜电位依赖性反应相关。具体而言,我们询问了一种先前已证明在大肠杆菌中组装时不依赖膜电位的突变前衣壳蛋白(M13am8H1R1前衣壳蛋白)在组装到微粒体中时是否受到网织红细胞裂解物和ATP的刺激。由于该突变前衣壳蛋白在真核体外系统中的行为与野生型前衣壳蛋白完全相同,我们提出在真核系统中观察到的ATP依赖性反应不能替代原核系统中的膜电位依赖性反应。