| Popis: |
Cells coordinate chaperones at the exit site of the ribosome. Albeit the types and mechanisms of ribosome-associated chaperones differ in the three kingdoms of life, they all share the ability to protect nascent polypeptides from off pathways such as aggregation and degradation and, at least in some cases, support initial folding steps of newly synthesized proteins. Recent progress was made in understanding the nascent interactome of these ribosome-associated chaperones. While the bacteria-specific chaperone trigger factor (TF) binds to almost every nascent polypeptide made by ribosomes except for membrane proteins, the substrate pool of the two eukaryotic ribosome-associated chaperone systems, nascent polypeptide-associated complex (NAC) and ribosome-associated complex (RAC), is more distinct. |
