Premium
Yeast DNA polymerase‐‐DNA primase complex; cloning of PRI 1, a single essential gene related to DNA primase activity.
Author(s) -
Lucchini G.,
Francesconi S.,
Foiani M.,
Badaracco G.,
Plevani P.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb04815.x
Subject(s) - primase , biology , dna polymerase , primer (cosmetics) , dna clamp , dna polymerase ii , genetics , replisome , dna , polymerase , microbiology and biotechnology , gene , circular bacterial chromosome , polymerase chain reaction , reverse transcriptase , chemistry , organic chemistry
The immunopurified yeast DNA polymerase‐‐DNA primase complex is constituted by DNA polymerase I polypeptides and by three other protein species, called p74, p58 and p48, which we show to be immunologically unrelated. The gene encoding the p48 polypeptide has been identified by immunological screening of a lambda gt11 yeast genomic DNA library. Antiserum specific for p48 inhibits DNA primase, and immunoreactive, inhibitory antibodies are affinity‐purified by the clone‐encoded protein, thus relating the p48 polypeptide to DNA primase activity. The entire gene has been cloned, and the 1.45‐kb p48 mRNA is overproduced in cells containing the gene in high copy number. Gene disruption and Southern hybridization experiments demonstrate that the p48 protein is encoded by a single gene and it performs an essential function.