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PMID:5263754
| Citation |
Center, MS, Studier, FW and Richardson, CC (1970) The structural gene for a T7 endonuclease essential for phage DNA synthesis. Proc. Natl. Acad. Sci. U.S.A. 65:242-8 |
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| Abstract |
Infection of Escherichia coli with bacteriophage T7 results in the appearance of an endonuclease activity capable of hydrolyzing both double-and single-stranded DNA. Treatment with chloramphenicol prevents the induction of the endonuclease. Amber mutants of phage T7 defective in gene 3 are unable to produce the enzyme after infection of the nonpermissive host, and mutants that produce a heat-labile endonuclease were found, indicating that this gene is the structural gene for the enzyme. Gene 3 mutants synthesize only a limited amount of DNA. In addition, they are defective in carrying out the degradation of host DNA, suggesting that the gene 3 endonuclease is involved in this function. |
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| Keywords |
Centrifugation, Density Gradient; Coliphages/enzymology; Coliphages/metabolism; DNA, Bacterial/metabolism; DNA, Viral/biosynthesis; Deoxyribonucleases/metabolism; Genes; Genetics, Microbial; Mutation |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:1990238: double-stranded DNA endodeoxyribonuclease activity |
ECO:0000315: |
F |
Figure 1 shows significant degradation of both double and single stranded DNA upon infection with T7. The researchers, therefore, mutated a number of genes, and found out that only the mutants in genes 1 or 3 did not induce an increased endonuclease activity. It is, furthermore, stated that the product of gene 1 (RNA polymerase factor) is needed for the transcription of most of the T7 genome. Mutants in gene 3 were still synthesizing all essential T7 proteins, only lacking the increased endonuclease activity. |
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Notes
See also
References
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