Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.25.1 (deoxyribonuclease)
 1,471 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Coupled transcription and translation of plasmid-ColE1 DNA in vitro under optimized conditions gave one major product. This has an apparent weight of 71 000, the same N-terminal sequence as colicin E1 and was not digested by deoxyribonuclease or ribonuclease. It differed from colicin E1 in its C-terminal residue and amino acid composition. It had lower specific activities in cell killing and in the fluorescence-enhancement in vitro assay of Phillips & Cramer [(1973) Biochemistry 12, 1170--1176] than did colicin E1, but both proteins bound in equimolar amounts to colicin-sensitive and colicin-resistant cells. The product of plasmid-ColE1-DNA-directed protein synthesis was converted into a protein indistinguishable in structure and activity from colicin E1 by incubation in the reaction mixture, after deoxyribonuclease and ribonuclease treatment, for a further 20 h at 37 degrees C. A protein with similar properties to the 71 000-dalton product in vitro was identified in extracts of a ColE1+ colicin-tolerant mutant of Escherichia coli K12. It is concluded that this protein probably represents a pre-form of colicin E1 which may be involved in colicin-E1 secretion or cellular colicin-E1 immunity in colicin-E-producing cells, or both of these processes.
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PMID:Precolicin E1, the major gene product of plasmid-ColE1 deoxyribonucleic acid in vitro. 699 10

Some effects of two uncouplers of oxidative phosphorylation on infection of Escherichia coli K12 by bacteriophage lambda deoxyribonucleic acid (DNA) are described. Dinitrophenol did not interfere with the initial interaction of the cells with free DNA, and neither dinitrophenol nor carbonyl cyanide m-chlorophenylhydrazone affected the linear portion of the infection reaction. However, the process by which lambda-DNA bound to the bacterial cell became insensitive to deoxyribonuclease was strongly inhibited by both uncoupling agents. These results support the conclusion that successful infection of E. coli with phage lambda-DNA is coupled to cellular energy metabolism and localize a portion of the infection reaction which is sensitive to the uncoupling of oxidative phosphorylation. Possible energy-requiring steps in the infection process are discussed.
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PMID:Effects of uncouplers of oxidative phosphorylation on the infection of Escherichia coli K12 by phage-lambda DNA. 1861 68