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  • 标题:RecA protein filaments can juxtapose DNA ends: an activity that may reflect a function in DNA repair
  • 本地全文:下载
  • 作者:J C Register ; J Griffith
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1986
  • 卷号:83
  • 期号:3
  • 页码:624-628
  • DOI:10.1073/pnas.83.3.624
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:To further characterize the role of RecA protein-DNA filaments in general recombination and DNA repair, we have examined interactions of these filaments with themselves following formation. When linear double-stranded DNA was incubated with RecA in the presence of Mg2+ and adenosine 5'-[gamma-thio]triphosphate, monomer-length (1n) nucleoprotein filaments were observed. Following continued incubation, filaments having 2n, 3n, ... lengths were observed, indicating that an end-to-end joining of the monomer-length filaments had occurred. When linear single-stranded DNA was covered by RecA protein under several conditions, the ends of the resulting filaments joined together rapidly, producing circular filaments. The end-to-end joining of single-stranded DNA-RecA filaments appeared to require that 3' DNA ends be juxtaposed with 5' DNA ends, because double-stranded DNA molecules having long single-stranded DNA tails with only 3' or 5' termini did not join end-to-end. However, when both 5' and 3' ends were present in the reaction, joining was observed. We suggest that this end-to-end joining activity may help explain the role of RecA protein in both the protection of damaged DNA ends and the repair of double-stranded DNA breaks.
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