Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-11-21
pubmed:databankReference
pubmed:abstractText
Glyoxalase II is part of the glutathione-dependent glyoxalase detoxification system. In addition to its role in the detoxification of cytotoxic 2-oxo-aldehydes, specifically methylglyoxal, it has been suggested that the glyoxalase system may also play a role in controlling cell differentiation and proliferation. During the analysis of a T-DNA-tagged mutant of Arabidopsis we identified the gene for a glyoxalase II isozyme (GLY1) that appears to be mitochondrially localized. The cDNA encoding a glyoxalase II cytoplasmic isozyme (GLY2) was also isolated and characterized. Southern blot and sequence analyses indicate that glyoxalase II proteins are encoded by at least two multigene families in Arabidopsis. Escherichia coli cells expressing either GLY1 or GLY2 exhibit increased glyoxalase II activity, confirming that they do, in fact, encode glyoxalase II proteins. Northern analysis shows that the two genes are differentially expressed. Transcripts for the mitochondrial isozyme are most abundant in roots, while those for the cytoplasmic isozyme are highest in flower buds. The identification of glyoxalase II isozymes that are differentially expressed suggests that they may play different roles in the cell.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0167-4412
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
471-81
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Molecular characterization of glyoxalase II from Arabidopsis thaliana.
pubmed:affiliation
Department of Chemistry, Miami University, Oxford, OH 45056, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.