Initiation of phage π29 DNA replication by the terminal protein modified at the carboxyl end
Author(s) -
Rafael P. Mellado,
Margarita Salas
Publication year - 1983
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/11.21.7397
Subject(s) - biology , dna replication , dna , microbiology and biotechnology , mutant , primer (cosmetics) , open reading frame , phagemid , start codon , genetics , bacteriophage , peptide sequence , gene , escherichia coli , chemistry , organic chemistry , base sequence
A mutant at the carboxyl end of the terminal protein, p3, of phage phi 29 DNA has been constructed by inserting an containing the stop translation codon TGA in the three possible reading frames, immediately downstream of a phage phi 29 DNA fragment coding for all but the last five amino acids of protein p3. The activity in the formation of the p3-dAMP initiation complex in vitro of this mutant as well as another one previously isolated, also mutated at the carboxyl end, have been tested. The results obtained suggest that an intact carboxyl end in the phage phi 29 terminal protein is essential for its normal primer function in DNA replication.
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