Linked Life Data

10471279

Source:http://linkedlifedata.com/resource/pubmed/id/10471279

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
35
pubmed:dateCreated
1999-9-28
pubmed:abstractText
Saccharomyces cerevisiae possesses two functional homologues (Ntg1p and Ntg2p) of the Escherichia coli endonuclease III protein, a DNA base excision repair N-glycosylase with a broad substrate specificity directed primarily against oxidatively damaged pyrimidines. The substrate specificities of Ntg1p and Ntg2p are similar but not identical, and differences in their amino acid sequences as well as inducibility by DNA damaging agents suggest that the two proteins may have different biological roles and subcellular locations. Experiments performed on oligonucleotides containing a variety of oxidative base damages indicated that dihydrothymine, urea, and uracil glycol are substrates for Ntg1p and Ntg2p, although dihydrothymine was a poor substrate for Ntg2p. Vectors encoding Ntg1p-green fluorescent protein (GFP) and Ntg2p-GFP fusions under the control of their respective endogenous promoters were utilized to observe the subcellular targeting of Ntg1p and Ntg2p in S. cerevisiae. Fluorescence microscopy of pNTG1-GFP and pNTG2-GFP transformants revealed that Ntg1p localizes primarily to the mitochondria with some nuclear localization, whereas Ntg2p localizes exclusively to the nucleus. In addition, the subcellular location of Ntg1p and Ntg2p confers differential sensitivities to the alkylating agent MMS. These results expand the known substrate specificities of Ntg1p and Ntg2p, indicating that their base damage recognition ranges show distinct differences and that these proteins mediate different roles in the repair of DNA base damage in the nucleus and mitochondria of yeast.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11298-306
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:10471279-Base Sequence, pubmed-meshheading:10471279-Cell Nucleus, pubmed-meshheading:10471279-DNA, Mitochondrial, pubmed-meshheading:10471279-DNA Damage, pubmed-meshheading:10471279-DNA Repair, pubmed-meshheading:10471279-DNA-(Apurinic or Apyrimidinic Site) Lyase, pubmed-meshheading:10471279-Gamma Rays, pubmed-meshheading:10471279-Green Fluorescent Proteins, pubmed-meshheading:10471279-Hydrogen Peroxide, pubmed-meshheading:10471279-Luminescent Proteins, pubmed-meshheading:10471279-Microscopy, Fluorescence, pubmed-meshheading:10471279-Molecular Sequence Data, pubmed-meshheading:10471279-N-Glycosyl Hydrolases, pubmed-meshheading:10471279-Oxidation-Reduction, pubmed-meshheading:10471279-Recombinant Fusion Proteins, pubmed-meshheading:10471279-Saccharomyces cerevisiae, pubmed-meshheading:10471279-Saccharomyces cerevisiae Proteins, pubmed-meshheading:10471279-Substrate Specificity
pubmed:year
1999
pubmed:articleTitle
Saccharomyces cerevisiae Ntg1p and Ntg2p: broad specificity N-glycosylases for the repair of oxidative DNA damage in the nucleus and mitochondria.
pubmed:affiliation
Department of Biochemistry, Division of Cancer Biology, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't