Escherichia coli ribosomal protein L3 stimulates the helicase activity of the Bacillus stearothermophilus PcrA helicase.
AUTOR(ES)
Soultanas, P
RESUMO
Escherichia coli ribosomal protein L3 stimulates the in vitro helicase activity of Bacillus stearothermophilus PcrA helicase upon a variety of different substrates. L3 has no intrinsic helicase or ATPase activity nor is it able to stimulate the ATPase activity of PcrA. Gel mobility shift assays revealed that the affinity of PcrA for a variety of different DNA species (single-stranded, nicked and 3'-tailed) was enhanced in the presence of L3. We suggest that the stimulatory effect of L3 upon the helicase activity of PcrA is mediated via a protein-protein interaction which promotes cooperative binding of PcrA to its DNA substrate. This activity of L3 appears to be specific for PcrA helicase.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=147557Documentos Relacionados
- Plasmid replication initiator protein RepD increases the processivity of PcrA DNA helicase.
- Characterisation of Bacillus stearothermophilus PcrA helicase: evidence against an active rolling mechanism.
- Purification and Characterization of the PcrA Helicase of Bacillus anthracis
- Escherichia coli RecQ protein is a DNA helicase.
- Structure-specific DNA binding and bipolar helicase activities of PcrA