Abstract
PriB is a primosomal protein required for PriA helicase-dependent DNA replication restart. Escherichia coli PriB protein (EcPriB) exists as a homodimer, and each polypeptide has 104 residues. Significant variation is found in length of priB gene from different organisms. In Klebsiella pneumoniae (Kp), the priB gene consisted of 168 nucleotides encoding a gene product of 55 amino acid residues. Sequence alignment indicates that KpPriB lacks an N-terminal region (aa 1-49) found in EcPriB, in which several key residues have proved to be a major role for interactions with PriA helicase and DnaT. In the present study, the properties of single-stranded DNA (ssDNA) binding, self-association, and primosome assembly of KpPriB were further investigated. Based on these results, the structure-function relationships of KpPriB are discussed.
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