Das Debasis, Das Anindita, Samanta Dibyendu, Ghosh Jaydip, Dasgupta Santanu, Bhattacharya Arpita, Basu Arunima, Sanyal Suparna, Das Gupta Chanchal
Department of Biophysics, Molecular Biology and Genetics, University College of Science, Kolkata, India.
Biotechnol J. 2008 Aug;3(8):999-1009. doi: 10.1002/biot.200800098.
In all organisms, the ribosome synthesizes and folds full length polypeptide chains into active three-dimensional conformations. The nascent protein goes through two major interactions, first with the ribosome which synthesizes the polypeptide chain and holds it for a considerable length of time, and then with the chaperones. Some of the chaperones are found in solution as well as associated to the ribosome. A number of in vitro and in vivo experiments revealed that the nascent protein folds through specific interactions of some amino acids with the nucleotides in the peptidyl transferase center (PTC) in the large ribosomal subunit. The mechanism of this folding differs from self-folding. In this article, we highlight the folding of nascent proteins on the ribosome and the influence of chaperones etc. on protein folding.
在所有生物体中,核糖体将全长多肽链合成并折叠成具有活性的三维构象。新生蛋白质会经历两种主要相互作用,首先是与合成多肽链并将其保持相当长时间的核糖体相互作用,然后是与分子伴侣相互作用。一些分子伴侣既存在于溶液中,也与核糖体相关联。大量体外和体内实验表明,新生蛋白质通过一些氨基酸与大核糖体亚基肽基转移酶中心(PTC)中的核苷酸的特异性相互作用进行折叠。这种折叠机制不同于自我折叠。在本文中,我们着重介绍核糖体上新生蛋白质的折叠以及分子伴侣等对蛋白质折叠的影响。