Johnson Arthur E
Department of Molecular and Cellular Medicine, Texas A&M Health Science Center and Department of Chemistry and Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA.
J Cell Biol. 2009 Jun 1;185(5):765-7. doi: 10.1083/jcb.200902014. Epub 2009 May 25.
Ribosomes synthesizing secretory and membrane proteins are bound to translocons at the membrane of the endoplasmic reticulum (ER). Both the ribosome and translocon are complex macromolecular machines whose structural and functional interactions are poorly understood. A new study by Pool (Pool, M.R. 2009. J. Cell Biol. 185:889-902) has now shown that the structure of the translocon is dictated by the identity of the protein being synthesized by the ribosome, thereby demonstrating that the two macromolecular machines are structurally coupled for functional purposes. The study also identifies an unexpected component in the apparent molecular linkage that connects the two machines, a discovery that shows the current view of translocon structure is oversimplified.
合成分泌蛋白和膜蛋白的核糖体与内质网(ER)膜上的易位子结合。核糖体和易位子都是复杂的大分子机器,它们的结构和功能相互作用还知之甚少。Pool的一项新研究(Pool,M.R. 2009. J. Cell Biol. 185:889 - 902)现已表明,易位子的结构由核糖体正在合成的蛋白质的特性决定,从而证明这两个大分子机器在结构上是为了功能目的而耦合的。该研究还在连接这两个机器的明显分子连接中发现了一个意想不到的成分,这一发现表明目前关于易位子结构的观点过于简单化。