Bacillus subtilis DnaG primase stabilises the bacteriophage SPP1 G40P helicase-ssDNA complex

被引：20

作者：

Ayora, S

Langer, U

Alonso, JC

机构：

[1] CSIC, Ctr Nacl Biotecnol, Dept Biotecnol Microbioana, E-28049 Madrid, Spain

[2] Max Planck Inst Mol Genet, D-14195 Berlin, Germany

来源：

FEBS LETTERS | 1998年 / 439卷 / 1-2期

关键词：

phage biology; SPP1; DNA replication; replication initiation protein; DNA helicase; DNA primase;

D O I：

10.1016/S0014-5793(98)01337-4

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Purified Bacillus subtilis DnaG primase (predicted molecular mass 68.8 kDa) behaves as a monomer in solution. We demonstrate that DnaG physically interacts with bacteriophage SPP1 hexameric helicase G40P (G40P(6)) in the absence of ATP, G40P(6)-ATP forms an unstable complex with ssDNA, and by itself carries out ATP-driven translocation along a ssDNA template with low processivity, The presence of DnaG in the reaction mixture increased the helicase activity of G40P(6) about 3-fold, but not the ATPase activity. The results presented here suggest that the DnaG protein stabilises the G40P(6)-ssDNA complexes. (C) 1998 Federation of European Biochemical Societies.

引用

页码：59 / 62

页数：4

共 22 条

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Matson SW, 1995, METHOD ENZYMOL, V262, P389

[12] The replisome organizer (G38P) of Bacillus subtilis bacteriophage SPP1 forms specialized nucleoprotein complexes with two discrete distant regions of the SPP1 genome [J].