The T4-encoded cochaperonin, gp31, has unique properties that explain its requirement for the folding of the T4 major capsid protein

被引:22
作者
Bakkes, PJ [1 ]
Faber, BW [1 ]
van Heerikhuizen, H [1 ]
van der Vies, SM [1 ]
机构
[1] Free Univ Amsterdam, Fac Sci, Sect Biochem & Mol Biol, NL-1081 HV Amsterdam, Netherlands
关键词
chaperones; protein folding; viral capsid assembly;
D O I
10.1073/pnas.0500048102
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:8144 / 8149
页数:6
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