Purification of phi X174 gene C protein

Autor: R Mukai, R K Hamatake, M Hayashi, A Aoyama
Rok vydání: 1983
Předmět:
Zdroj: Journal of Biological Chemistry. 258:5798-5803
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(20)81964-4
Popis: The product of gene C of bacteriophage phi X174 is required for the replication of phiX174 single-stranded DNA in Escherichia coli cells infected with phi X174. The protein has been purified to homogeneity using an in vitro complementation system. The protein exhibits a molecular weight of 5800 under denaturing conditions. The NH2-terminal amino acid sequence of the protein is (NH2)-Met-Arg-Lys, which is consistent with the sequence predicted from the nucleotide sequence of gene C. The protein has an affinity for single-stranded DNA but less for double-stranded DNA.
Databáze: OpenAIRE