The extreme C terminus of primase is required for interaction with DnaB at the replication fork Journal Article
| Authors: | Tougu, K.; Marians, K. J. |
| Article Title: | The extreme C terminus of primase is required for interaction with DnaB at the replication fork |
| Abstract: | We have shown previously that a protein-protein interaction between DnaG and DnaB is required to attract the primase to the replication fork. This interaction was mediated by the C-terminal 16-kDa domain (p16) of the primase. A screen was developed that allowed the detection of mutant p16 proteins that did not interact with DnaB. Various mutagenesis protocols were used to localize this interaction domain to the extreme C terminus of the primase. A mutant primase missing only the C-terminal 16 amino acids was isolated and its activities examined. This mutant enzyme was fully active as a primase, but was incapable of interacting with DnaB. Thus, the mutant primase could not support DNA synthesis in either the general priming reaction or during φX174 complementary strand DNA replication. Alanine cluster mutagenesis and deletion analysis in p16 allowed the further localization of the interaction domain to the extreme C-terminal 8 amino acids in primase. |
| Keywords: | controlled study; sequence deletion; nonhuman; mutant protein; dna replication; dna synthesis; protein domain; amino acid substitution; carboxy terminal sequence; protein protein interaction; protein binding; bacterial proteins; molecular sequence data; escherichia coli; base sequence; mutagenesis, site-directed; alanine; dna primers; site directed mutagenesis; dna helicases; complementary dna; dna b; dna primase; dnab helicases; rna nucleotidyltransferases; bacteriophage phi x 174; priority journal; article; bacteriophage phi |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 271 |
| Issue: | 35 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 1996-08-30 |
| Start Page: | 21391 |
| End Page: | 21397 |
| Language: | English |
| DOI: | 10.1074/jbc.271.35.21391 |
| PUBMED: | 8702920 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Article -- Export Date: 22 November 2017 -- Source: Scopus |
