Mechanism of the concerted action of recA protein and helix-destabilizing proteins in homologous recombination.
AUTOR(ES)
Muniyappa, K
RESUMO
Secondary structure in single-stranded DNA impedes the presynaptic association of recA protein and consequently blocks the formation of joint molecules as evidenced by effects of temperature, nucleotide sequence, and ionic conditions. Escherichia coli single-strand-binding protein eliminates sequence-specific "cold spots" by removing folds even from sites of strong secondary structure. Thus, destabilization of secondary structure in single-stranded DNA is critical for the action of recA protein, whereas specific interactions directly between helix-destabilizing proteins and recA protein are unimportant.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=345149Documentos Relacionados
- Homologous pairing in genetic recombination: formation of D loops by combined action of recA protein and a helix-destabilizing protein.
- Helix-destabilizing properties of the adenovirus DNA-binding protein.
- Amino acid sequence of the T4 DNA helix-destabilizing protein.
- Identification and Characterization of the Helix-Destabilizing Activity of Rotavirus Nonstructural Protein NSP2
- Immunoreactive helix-destabilizing protein localized in transcriptionally active regions of Drosophila polytene chromosomes.
