Site-directed mutagenesis in the DNA linking site of bacteriophage o29 terminal protein: isolation and characterization of a Ser232->Thr mutant | Zendy

Cristina Garmendia | Zendy; Margarita Salas | Zendy; José M. Hermoso | Zendy

Open Access

Site-directed mutagenesis in the DNA linking site of bacteriophage o29 terminal protein: isolation and characterization of a Ser232->Thr mutant

Author(s) -

Cristina Garmendia,

Margarita Salas,

José M. Hermoso

Publication year - 1988

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/16.13.5727

Subject(s) - biology , site directed mutagenesis , mutant , mutagenesis , dna clamp , dna polymerase , dna replication , dna , microbiology and biotechnology , biochemistry , genetics , gene , reverse transcriptase , polymerase chain reaction

By site-directed mutagenesis we have changed the serine residue 232 of the phi 29 terminal protein, involved in the covalent linkage to dAMP for the initiation of replication, into a threonine residue. The mutant terminal protein has been purified to homogeneity and shown to be inactive in the formation of the initiation complex; nevertheless, the mutant protein retains its ability to interact with the phi 29 DNA polymerase and with the DNA. The results obtained indicate a high specificity in the linking site of the terminal protein.

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