Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
2000-10-23
pubmed:abstractText
We reported that plant ribosome inactivating proteins (RIP) have a unique DNA glycosylase activity that removes adenine from single-stranded DNA (Nicolas, E., Beggs, J. M., Haltiwanger, B. M., and Taraschi, T. F. (1998) J. Biol. Chem. 273, 17216-17220). In this investigation, we further characterized the interaction of the RIP gelonin with single-stranded oligonucleotides and investigated its activity on double-stranded oligonucleotides. At physiological pH, zinc and beta-mercaptoethanol stimulated the adenine DNA glycosylase activity of gelonin. Under these conditions, gelonin catalytically removed adenine from single-stranded DNA and, albeit to a lesser extent, from normal base pairs and mismatches in duplex DNA. Also unprecedented was the finding that activity on single-stranded and double-stranded oligonucleotides containing multiple adenines generated unstable products with several abasic sites, producing strand breakage and duplex melting, respectively. The results from competition experiments suggested similar interactions between gelonin's DNA-binding domain and oligonucleotides with and without adenine. A re-examination of the classification of gelonin as a DNA glycosylase/AP lyase using the borohydride trapping assay revealed that gelonin was similar to the DNA glycosylase MutY: both enzymes are monofunctional glycosylases, which are trappable to their DNA substrates. The k(cat) for the removal of adenine from single-stranded DNA was close to the values observed with multisubstrate DNA glycosylases, suggesting that the activity of RIPs on DNA may be physiologically relevant.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Adenine, http://linkedlifedata.com/resource/pubmed/chemical/Carbon-Oxygen Lyases, http://linkedlifedata.com/resource/pubmed/chemical/DNA, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Single-Stranded, http://linkedlifedata.com/resource/pubmed/chemical/DNA Glycosylases, http://linkedlifedata.com/resource/pubmed/chemical/DNA-(Apurinic or Apyrimidinic..., http://linkedlifedata.com/resource/pubmed/chemical/Deoxyribonuclease IV (Phage..., http://linkedlifedata.com/resource/pubmed/chemical/GEL protein, Gelonium multiflorum, http://linkedlifedata.com/resource/pubmed/chemical/Mercaptoethanol, http://linkedlifedata.com/resource/pubmed/chemical/N-Glycosyl Hydrolases, http://linkedlifedata.com/resource/pubmed/chemical/Oligonucleotides, http://linkedlifedata.com/resource/pubmed/chemical/Plant Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ribosome Inactivating Proteins..., http://linkedlifedata.com/resource/pubmed/chemical/Zinc
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31399-406
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed-meshheading:10906135-Adenine, pubmed-meshheading:10906135-Base Pair Mismatch, pubmed-meshheading:10906135-Carbon-Oxygen Lyases, pubmed-meshheading:10906135-DNA, pubmed-meshheading:10906135-DNA, Single-Stranded, pubmed-meshheading:10906135-DNA Glycosylases, pubmed-meshheading:10906135-DNA Repair, pubmed-meshheading:10906135-DNA-(Apurinic or Apyrimidinic Site) Lyase, pubmed-meshheading:10906135-Deoxyribonuclease IV (Phage T4-Induced), pubmed-meshheading:10906135-Dose-Response Relationship, Drug, pubmed-meshheading:10906135-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:10906135-Hydrogen-Ion Concentration, pubmed-meshheading:10906135-Kinetics, pubmed-meshheading:10906135-Mercaptoethanol, pubmed-meshheading:10906135-N-Glycosyl Hydrolases, pubmed-meshheading:10906135-Oligonucleotides, pubmed-meshheading:10906135-Plant Proteins, pubmed-meshheading:10906135-Ribosome Inactivating Proteins, Type 1, pubmed-meshheading:10906135-Time Factors, pubmed-meshheading:10906135-Zinc
pubmed:year
2000
pubmed:articleTitle
Gelonin is an unusual DNA glycosylase that removes adenine from single-stranded DNA, normal base pairs and mismatches.
pubmed:affiliation
Department of Pathology, Anatomy and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.