yeast killer plasmid pGKL1 encodes a DNA polymerase belonging to the family B DNA polymerases
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چکیده
منابع مشابه
A DNA polymerase from the archaeon Sulfolobus solfataricus shows sequence similarity to family B DNA polymerases.
The gene encoding the thermostable DNA polymerase from the archaeon Sulfolobus solfataricus (strain MT 4) was isolated by means of two degenerate oligonucleotide probes. They were designed on the basis of partial enzyme amino acid sequences. The gene was found to encode a 882 residues polypeptide chain with a deduced molecular mass of about 100 kDa. By comparison with other archaeal genes, puta...
متن کاملPlasmid-based lacZalpha assay for DNA polymerase fidelity: application to archaeal family-B DNA polymerase
The preparation of a gapped pUC18 derivative, containing the lacZa reporter gene in the singlestranded region, is described. Gapping is achieved by flanking the lacZa gene with sites for two related nicking endonucleases, enabling the excision of either the coding or non-coding strand. However, the excised strand remains annealed to the plasmid through non-covalent Watson–Crick base-pairing; it...
متن کاملPlasmid-based lacZα assay for DNA polymerase fidelity: application to archaeal family-B DNA polymerase
The preparation of a gapped pUC18 derivative, containing the lacZalpha reporter gene in the single-stranded region, is described. Gapping is achieved by flanking the lacZalpha gene with sites for two related nicking endonucleases, enabling the excision of either the coding or non-coding strand. However, the excised strand remains annealed to the plasmid through non-covalent Watson-Crick base-pa...
متن کاملThe yeast linear DNA killer plasmids, pGKL1 and pGKL2, possess terminally attached proteins.
The terminal structures of linear DNA killer plasmids from yeast, pGKL1 and pGKL2, were analyzed. Results obtained by exonuclease treatments of these plasmids show that both pGKL plasmids have free hydroxyl 3'-ends and blocked 5'-ends. Electrophoretic analysis of the terminal restriction fragments treated with proteases revealed that pGKL1 and pGKL2 have proteins bound at 5'termini and that the...
متن کاملStructures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases.
Replicative DNA polymerases (DNAPs) move along template DNA in a processive manner. The structural basis of the mechanism of translocation has been better studied in the A-family of polymerases than in the B-family of replicative polymerases. To address this issue, we have determined the X-ray crystal structures of phi29 DNAP, a member of the protein-primed subgroup of the B-family of polymeras...
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ژورنال
عنوان ژورنال: Nucleic Acids Research
سال: 1987
ISSN: 0305-1048,1362-4962
DOI: 10.1093/nar/15.21.9088