Mutational analysis of Escherichia coli topoisomerase IV: II. ATPase negative mutants of ParE induce hyper-DNA cleavage Journal Article
| Authors: | Nurse, P.; Bahng, S.; Mossessova, E.; Marians, K. J. |
| Article Title: | Mutational analysis of Escherichia coli topoisomerase IV: II. ATPase negative mutants of ParE induce hyper-DNA cleavage |
| Abstract: | ParE is the ATP-binding subunit of topoisomerase IV (Topo IV). During topoisomerization, the ATP-binding and hydrolysis cycle must be coordinated with the cycle of DNA cleavage and religation. We have isolated three dominant-negative mutant alleles of parE that encode ParE proteins that fail to hydrolyze ATP when reconstituted with ParC to form Topo IV. ParE G110S Topo IV and ParE S123L Topo IV failed to bind ATP at all, whereas ParE T201A could bind ATP. All three mutant Topo IV proteins exhibited an elevated level of spontaneous DNA cleavage that could be associated with a decreased rate of DNA resealing. In ParE T201A Topo IV, this defect appeared to result from an increased likelihood that the tetrameric enzyme would fall apart after DNA cleavage. Thus, while ATP is not required for DNA cleavage, the properties of these mutant enzymes suggests that ATP-hydrolysis informs DNA religation. |
| Keywords: | mutation; dna-binding proteins; nonhuman; mutant protein; animals; protein dna binding; bacterial proteins; escherichia coli; models, molecular; dimerization; dna mutational analysis; adenosine triphosphate; adenosine triphosphatase; enzyme subunit; adenosine triphosphatases; hydrolysis; dna topoisomerases, type ii; chromatography, gel; dna cleavage; dna topoisomerase iv; dna topoisomerase; dna, superhelical; prokaryota; negibacteria; priority journal; article; adenylyl imidodiphosphate; crithidia fasciculata |
| Journal Title: | Journal of Biological Chemistry |
| Volume: | 275 |
| Issue: | 6 |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Date Published: | 2000-02-11 |
| Start Page: | 4104 |
| End Page: | 4111 |
| Language: | English |
| DOI: | 10.1074/jbc.275.6.4104 |
| PUBMED: | 10660570 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 18 November 2015 -- Source: Scopus |
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