Linked Life Data

12730240

Source:http://linkedlifedata.com/resource/pubmed/id/12730240

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
2003-7-4
pubmed:abstractText
A truncated form (deltanMDH2) of yeast cytosolic malate dehydrogenase (MDH2) lacking 12 residues on the amino terminus was found to be inadequate for gluconeogenic function in vivo because the mutant enzyme fails to restore growth of a Deltamdh2 strain on minimal medium with ethanol or acetate as the carbon source. The DeltanMDH2 enzyme was also previously found to be refractory to the rapid glucose-induced inactivation and degradation observed for authentic MDH2. In contrast, kinetic properties measured for purified forms of MDH2 and deltanMDH2 enzymes are very similar. Yeast two-hybrid assays indicate weak interactions between MDH2 and yeast phosphoenolpyruvate carboxykinase (PCK1) and between MDH2 and fructose-1,6-bisphosphatase (FBP1). These interactions are not observed for deltanMDH2, suggesting that differences in cellular function between authentic and truncated forms of MDH2 may be related to their ability to interact with other gluconeogenic enzymes. Additional evidence was obtained for interaction of MDH2 with PCK1 using Hummel-Dreyer gel filtration chromatography, and for interactions of MDH2 with PCK1 and with FBP1 using surface plasmon resonance. Experiments with the latter technique demonstrated a much lower affinity for interaction of deltanMDH2 with PCK1 and no interaction between deltanMDH2 and FBP1. These results suggest that the interactions of MDH2 with other gluconeogenic enzymes are dependent on the amino terminus of the enzyme, and that these interactions are important for gluconeogenic function in vivo.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
278
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
25628-36
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:12730240-Amino Acid Sequence, pubmed-meshheading:12730240-Chromatography, Gel, pubmed-meshheading:12730240-Cytosol, pubmed-meshheading:12730240-Dimerization, pubmed-meshheading:12730240-Dose-Response Relationship, Drug, pubmed-meshheading:12730240-Fructose-Bisphosphatase, pubmed-meshheading:12730240-Glucose, pubmed-meshheading:12730240-Immunoblotting, pubmed-meshheading:12730240-Kinetics, pubmed-meshheading:12730240-Malate Dehydrogenase, pubmed-meshheading:12730240-Molecular Sequence Data, pubmed-meshheading:12730240-NAD, pubmed-meshheading:12730240-Oxaloacetate, pubmed-meshheading:12730240-Phosphoenolpyruvate Carboxykinase (ATP), pubmed-meshheading:12730240-Plasmids, pubmed-meshheading:12730240-Precipitin Tests, pubmed-meshheading:12730240-Protein Binding, pubmed-meshheading:12730240-Protein Structure, Tertiary, pubmed-meshheading:12730240-Saccharomyces cerevisiae Proteins, pubmed-meshheading:12730240-Sequence Homology, Amino Acid, pubmed-meshheading:12730240-Surface Plasmon Resonance, pubmed-meshheading:12730240-Thermodynamics, pubmed-meshheading:12730240-Two-Hybrid System Techniques
pubmed:year
2003
pubmed:articleTitle
Physical and genetic interactions of cytosolic malate dehydrogenase with other gluconeogenic enzymes.
pubmed:affiliation
Department of Biochemistry, University of Texas Health Science Center, San Antonio, Texas 78229-3900, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.