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Rings and filaments of β protein from bacteriophage λ suggest a superfamily of recombination proteins
被引:83
作者:
Passy, SI
Yu, XN
Li, ZF
Radding, CM
Egelman, EH
[1
]
机构:
[1] Univ Minnesota, Sch Med, Dept Cell Biol & Neuroanat, Minneapolis, MN 55455 USA
[2] Yale Univ, Sch Med, Dept Genet, New Haven, CT 06520 USA
来源:
关键词:
D O I:
10.1073/pnas.96.8.4279
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 beta protein of bacteriophage A acts in homologous genetic recombination by catalyzing the annealing of complementary single-stranded DNA produced by the A exonuclease. It has been shown that the beta protein binds to the products of the annealing reaction more tightly than to the initial substrates. We find that beta protein exists in three structural states. In the absence of DNA, beta protein forms inactive rings with approximate to 12 subunits, The active form of the beta protein in the presence of oligonucleotides or single-stranded DNA is a ring, composed of approximate to 15-18 subunits, The double-stranded products of the annealing reaction catalyzed by the rings are bound by beta protein in a left-handed helical structure, which protects the products from nucleolytic degradation. These observations suggest structural homology for a family of proteins, including the phage P22 erf, the bacterial RecT, and the eukaryotic Rad52 proteins, all of which are involved in homologous recombination.
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页码:4279 / 4284
页数:6
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