Yeast DNA polymerase--DNA primase complex; cloning of PRI 1, a single essential gene related to DNA primase activity.
AUTOR(ES)
Lucchini, G
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=553458Documentos Relacionados
- A single essential gene, PRI2, encodes the large subunit of DNA primase in Saccharomyces cerevisiae.
- The nucleotide sequence of the PRI1 gene related to DNA primase in Saccharomyces cerevisiae.
- Uranyl mediated photofootprinting reveals strong E. coli RNA polymerase--DNA backbone contacts in the +10 region of the DeoP1 promoter open complex.
- Characterization of a stable, major DNA polymerase alpha species devoid of DNA primase activity.
- Helicase-primase complex of herpes simplex virus type 1: a mutation in the UL52 subunit abolishes primase activity.
