Bochkareva E S, Lissin N M, Girshovich A S
Institute of Protein Research, Academy of Sciences of the USSR, Moscow Region.
Nature. 1988 Nov 17;336(6196):254-7. doi: 10.1038/336254a0.
It has been suggested that newly synthesized proteins are maintained in their unfolded state by cellular ATP-driven factors which may prevent or reverse the formation of misfolded structures or promote the correct assembly of oligomeric proteins or post-translational secretion. Using a photocross-linking approach, we have identified the 20S heat-shock GroEL protein as the major cytosolic component which forms a complex with the unfolded newly synthesized pre-beta-lactamase or chloramphenicol acetyltransferase in Escherichia coli. Dissociation of these complexes is ATP-dependent. The unfolded state of pre-beta-lactamase, maintained by the transient interaction with GroEL, may be essential for the secretion of this protein.
有人提出，新合成的蛋白质通过细胞内由ATP驱动的因子维持其未折叠状态，这些因子可能会阻止或逆转错误折叠结构的形成，或促进寡聚蛋白的正确组装或翻译后分泌。我们采用光交联方法，确定了20S热休克GroEL蛋白是大肠杆菌中与未折叠的新合成前β-内酰胺酶或氯霉素乙酰转移酶形成复合物的主要胞质成分。这些复合物的解离是ATP依赖性的。前β-内酰胺酶通过与GroEL的短暂相互作用维持的未折叠状态，可能对该蛋白的分泌至关重要。
