Abstract:
:Bacillus subtilis LrpC is a sequence-independent DNA-binding and DNA-bending protein, which binds both single-stranded (ss) and double-stranded (ds) DNA and facilitates the formation of higher order protein-DNA complexes in vitro. LrpC binds at different sites within the same DNA molecule promoting intramolecular ligation. When bound to separate molecules, it promotes intermolecular ligation, and joint molecule formation between a circular ssDNA and a homologous ssDNA-tailed linear dsDNA. LrpC binding showed a higher affinity for 4-way (Holliday) junctions in their open conformation, when compared with curved dsDNA. Consistent with these biochemical activities, an lrpC null mutant strain rendered cells sensitive to DNA damaging agents such as methyl methanesulfonate and 4-nitroquinoline-1-oxide, and showed a segregation defect. These findings collectively suggest that LrpC may be involved in DNA transactions during DNA repair and recombination.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
López-Torrejón G,Martínez-Jiménez MI,Ayora Sdoi
10.1093/nar/gkj418keywords:
subject
Has Abstractpub_date
2006-01-10 00:00:00pages
120-9issue
1eissn
0305-1048issn
1362-4962pii
34/1/120journal_volume
34pub_type
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