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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Jackson, A. P. Maxwell, A. |
| Description | Author Affiliation: Jackson AP ( Department of Biochemistry, University of Leicester, United Kingdom.); |
| Abstract | We propose a mechanism for the hydrolysis of ATP by the DNA gyrase B protein in which Glu42 acts as a general base and His38 has a role in aligning and polarizing the glutamate residue. We have tested this mechanism by site-directed mutagenesis, converting Glu42 to Ala, Asp, and Gln, and His38 to Ala. In the presence of wild-type A protein, B proteins bearing the mutations Ala42 and Gln42 show no detectable supercoiling or ATPase activities, while Asp42 and Ala38 proteins have reduced activities. In the DNA cleavage and relaxation reactions of gyrase, which do not require ATP hydrolysis, wild-type and mutant proteins have similar activities. When the 43-kDa N-terminal fragment of the gyrase B protein (which hydrolyzes ATP) contained the mutations Ala42 or Gln42, ATP was bound but not hydrolyzed, supporting the idea that Glu42 is involved in hydrolysis but not nucleotide binding. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 23 |
| Volume Number | 90 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 1993-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adenosine Triphosphatases Chemistry DNA Topoisomerases, Type II Adenosine Triphosphate Metabolism Amino Acid Sequence Bacterial Proteins Binding Sites Catalysis DNA, Superhelical Escherichia Coli Enzymology Lymphocyte Activation Molecular Sequence Data Mutagenesis, Site-Directed Peptide Fragments Sequence Alignment Sequence Homology, Amino Acid Structure-Activity Relationship Comparative Study Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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