由T4编码的伴侣蛋白gp31具有独特的性质，这解释了其在T4主要衣壳蛋白折叠过程中的必要性。
The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein.
作者信息
Bakkes Patrick J, Faber Bart W, van Heerikhuizen Harm, van der Vies Saskia M
机构信息
Section of Biochemistry and Molecular Biology, Faculty of Sciences, Vrije Universiteit, De Boelelaan 1083, 1081 HV, Amsterdam, The Netherlands.
出版信息
Proc Natl Acad Sci U S A. 2005 Jun 7;102(23):8144-9. doi: 10.1073/pnas.0500048102. Epub 2005 May 26.
The morphogenesis of bacteriophage T4 requires a specialized bacteriophage-encoded molecular chaperone (gp31) that is essential for the folding of the T4 major capsid protein (gp23). gp31 is related to GroES, the chaperonin of the Escherichia coli host because it displays a similar overall structure and properties. Why GroES is unable to fold the T4 capsid protein in conjunction with GroEL is unknown. Here we show that gp23 binds to the GroEL heptameric ring opposite to the ring that is bound by gp31 (the so-called trans-ring), while no binding to the trans-ring of the GroEL-GroES complex is observed. Although gp23 can be enclosed within the folding cage of the GroEL-gp31 complex, encapsulation within the GroEL-GroES complex is not possible. So it appears that folding of the T4 major capsid protein requires a gp31-dependent cis-folding mechanism likely inside an enlarged "Anfinsen cage" provided by GroEL and gp31.
噬菌体T4的形态发生需要一种特殊的、由噬菌体编码的分子伴侣（gp31），它对于T4主要衣壳蛋白（gp23）的折叠至关重要。gp31与大肠杆菌宿主的伴侣蛋白GroES相关，因为它具有相似的整体结构和性质。GroES为何无法与GroEL一起折叠T4衣壳蛋白尚不清楚。在此我们表明，gp23与GroEL七聚体环结合，其位置与gp31结合的环相对（即所谓的反式环），而未观察到与GroEL-GroES复合物的反式环结合。虽然gp23可以被包裹在GroEL-gp31复合物的折叠笼中，但无法被包裹在GroEL-GroES复合物中。因此，T4主要衣壳蛋白的折叠似乎需要一种依赖gp31的顺式折叠机制，可能是在由GroEL和gp31提供的扩大的“安芬森笼”内进行。
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