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Query: EC:3.1.25.1 (deoxyribonuclease)
 1,471 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A deoxyribonuclease has been purified more than 2000-fold from the green algae, Chlamydomonas reinhardii. The enzyme is most active on denatured DNA. Optimum activity is at pH 8.5, in 80 mM Tris-HCl buffer and 2 mM CaCl2. Other divalent cations can replace Ca2+ with varying lower efficiency. EDTA and inorganic phosphate are strongly inhibitory, while ATP and high concentrations of 2-mercaptoethanol are slightly inhibitory. The molecular weight is approximately 35 000, the Stokes radius is 2.7 nm, and the sedimentation coefficient 2.8 S. It is a single polypeptide chain, and the frictional ratio of 1.27 suggests it is only slightly asymetrical. The isoelectric point is 9.5. This enzyme has been termed exonuclease 1.
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PMID:A deoxyribonuclease from Chlamydomonas reinhardii. 1. Purification and properties. 1 43

We have found a unique deoxyribonuclease in extracts of the eukaryotic green alga Chlamydomonas. When incubated with viral DNA from adenovirus-2, this enzyme produces discrete fragments that form bands upon electrophoresis in an agarose gel. Site specificity of the enzymatic cleavage examined by identifying the 5'-terminal nucleotides in cleaved adenovirus-2 DNA and by studies with synthetic polynucleotides of defined sequence, indicates that the initial endonucleolytic cleavage occurs at a site containing a deoxythymidine residue. Electron microscopy of cleaved adenovirus-2 DNA revealed single-strand segments within duplex DNA. We propose that the enzyme acts by making initial site-specific single-strand incisions, followed by subsequent excision on the same strand, producing a gapped duplex molecule; and that double-strand scissions result from limited occurrence of overlapping single-strand gaps on complementary strands.
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PMID:A site-specific single-strand endonuclease from the eukaryote Chlamydomonas. 26 18

The properties of three DNA polymerase species A, B and C, purified from Chlamydomonas reinhardii were compared. DNA polymerases A and B have Km values with respect to deoxyribonucleoside triphosphates of 19 micron and 3 micron respectively. DNA polymerase A is most active with activated DNA, but will also use native DNA and synthetic RNA and DNA templates with DNA primers. DNA polymerase B is also most active with activated DNA, but will use denatured DNA and synthetic DNA templates. It is inactive with RNA templates. DNA polymerase B is completely inactive in the presence of 100 micron-heparin, which has no effect on DNA polymerase A activity. Heparin dissociates DNA polymerase B into subunits that are still catalytically active, but which heparin inhibited. DNA polymerase B possesses deoxyribonuclease activity that is inhibited by 5 micron-heparin, suggesting that the deoxyribonuclease is an integral part of the DNA polymerase moiety. DNA polymerase A is devoid of nuclease activity. DNA polymerase C is similar to DNA polymerase B in all these properties, though it is more active with RNA primers and has greater heat-sensitivity.
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PMID:DNA polymerases from Chlamydomonas reinhardii. Further characterization, action of inhibitors and associated nuclease activities. 64 18

A deoxyribonuclease purified Chlamydomonas reinhardii has been shown to be specific for single-stranded DNA. The enzyme is most active on thermally denatured DNA, but also degrades single-stranded termini from double-stranded DNA. The enzyme has no effect on single-stranded or double-stranded intact circular phiX174DNA, suggesting that it requires DNA termini for activity. DNA is digested progressively to oligonucleotides and then mononucleotides. The product of the reaction is nucleoside 5'-monophosphates. The enzyme has no effect on RNA, nor does it possess phosphatase or phosphodiesterase activity. No specificity was demonstrated for phosphate or hydroxyl groups at either the 5' or 3' termini of DNA. The enzyme may be able to initiate hydrolysis at either the 3' or the 5' termini, since radioactivity was released more rapidly from 5' and 3' termini than from bulk DNA. The enzyme has been tentatively named Chlamydomonas reinhardii exonuclease 1.
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PMID:A deoxyribonuclease from Chlamydomonas reinhardii. 2. Substrate specificity, mode of action and products. 88 35

An endodeoxyribonuclease, designated CreI, was purified 16,000-fold from zygotes of the eukaryote Chlamydomonas reinhardtii. CreI preferentially attacks the sequence TATA producing double strand breaks with 3'-phosphomonoester and 5'-hydroxyl termini. The endonuclease has an Mr = 27,000 and requires Ca2+ at pH 7.5 for optimal activity.
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PMID:An endonuclease from Chlamydomonas reinhardtii that cleaves the sequence TATA. 300 78

1. The activities of DNA polymerase preparations from the algae Euglena gracilis, Chlamydomonas reinhardtii, Chlorella pyrenoidosa, Anabaena variabilis and Anacystis nidulans were measured. The blue-green algae Anabaena and Anacystis contain a 5-20-fold higher activity of the enzyme than do the green algae. DNA polymerases from the blue-green algae show a pH optimum of 9 and prefer a relatively low Mg(2+) concentration (1-3mm). DNA polymerases from the green algae, however, display a pH optimum between 7.5 and 8.5 and an optimum Mg(2+) concentration of 8mm. With all algae, a higher polymerase activity was obtained with denatured salmon sperm DNA as template than with native DNA. All four deoxyribonucleoside 5'-triphosphates must be present for full activity of the polymerases. 2. With one exception, the deoxyribonuclease activities in the preparations, measured under conditions of the DNA polymerase assay, are low compared with corresponding preparations from Escherichia coli. Chlamydomonas extracts contain a high deoxyribonuclease activity. 3. After purification on columns of DEAE-cellulose, the polymerase activity was linear over a wide range of protein concentrations, except for Chlamydomonas preparations, where the observed deviation from linearity was probably attributable to the high nuclease activity. 4. DNA polymerases from all these algae bind strongly to DNA-cellulose; 6-40-fold purifications of the enzyme were obtained by chromatography on columns of DNA-cellulose. 5. The partially purified polymerases of Euglena and Anacystis are heat-labile but become much more heat-stable when tested in the presence of DNA.
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PMID:The activity of deoxyribonucleic acid polymerase in some species of algae. 462 75

The chloroplast of Chlamydomonas moewusii was examined by electron microscopic and cytochemical methods for the possible presence of DNA. Both the Feulgen reaction and acridine orange indicated the presence within the chloroplast of one or more irregularly shaped DNA-containing bodies generally in the vicinity of the pyrenoid. Electron micrographs revealed 25 A microfibrils in these areas which correspond to DNA macromolecules with respect to their location, morphology, and sensitivity to deoxyribonuclease digestion. The possibility that this material is the genetic system of the chloroplast and the hypothesis that the chloroplast represents an evolved endosymbiont are discussed.
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PMID:Ultrastructure of DNA-containing areas in the chloroplast of Chlamydomonas. 1449 36