The phage λ major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system

被引:222
作者
Pell, Lisa G. [1 ,3 ]
Kanelis, Voula [3 ,4 ]
Donaldson, Logan W. [5 ]
Howell, P. Lynne [1 ,3 ]
Davidson, Alan R. [1 ,2 ]
机构
[1] Univ Toronto, Dept Biochem, Toronto, ON M5S 1A8, Canada
[2] Univ Toronto, Dept Mol Genet, Toronto, ON M5S 1A8, Canada
[3] Hosp Sick Children, Res Inst, Toronto, ON M5G 1X8, Canada
[4] Univ Toronto, Dept Chem & Phys Sci, Mississauga, ON L5L 1C6, Canada
[5] York Univ, Dept Biol, N York, ON M3J 1P3, Canada
基金
加拿大健康研究院; 加拿大创新基金会;
关键词
NMR structure; disordered regions; macromolecular assembly; PSEUDOMONAS-AERUGINOSA; BACTERIOPHAGE-LAMBDA; ESCHERICHIA-COLI; SIMILARITIES; GENES; FOLD; NMR;
D O I
10.1073/pnas.0900044106
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
Most bacteriophages possess long tails, which serve as the conduit for genome delivery. We report the solution structure of the N-terminal domain of gpV, the protein comprising the major portion of the noncontractile phage lambda tail tube. This structure is very similar to a previously solved tail tube protein from a contractile-tailed phage, providing the first direct evidence of an evolutionary connection between these 2 distinct types of phage tails. A remarkable structural similarity is also seen to Hcp1, a component of the bacterial type VI secretion system. The hexameric structure of Hcp1 and its ability to form long tubes are strikingly reminiscent of gpV when it is polymerized into a tail tube. These data coupled with other similarities between phage and type VI secretion proteins support an evolutionary relationship between these systems. Using Hcp1 as a model, we propose a polymerization mechanism for gpV involving several disorder-to-order transitions.
引用
收藏
页码:4160 / 4165
页数:6
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