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Literature summary for 1.2.1.12 extracted from

  • Demarse, N.A.; Ponnusamy, S.; Spicer, E.K.; Apohan, E.; Baatz, J.E.; Ogretmen, B.; Davies, C.
    Direct binding of glyceraldehyde 3-phosphate dehydrogenase to telomeric DNA protects telomeres against chemotherapy-induced rapid degradation (2009), J. Mol. Biol., 394, 789-803.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
doxorubicin treatment results in increased nuclear localization of expressed wild-type GAPDH, where it protects telomeres against rapid degradation, concomitant with increased resistance to the growth-inhibitory effects of the drug Homo sapiens
gemcitabine treatment results in increased nuclear localization of expressed wild-type GAPDH, where it protects telomeres against rapid degradation, concomitant with increased resistance to the growth-inhibitory effects of the drug Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Homo sapiens

Protein Variants

Protein Variants Comment Organism
C149A mutant has almost completely lost the ability to bind telomere. Upon expression in A-549 cells, mutant localizes to the nucleus but is unable to confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition Homo sapiens
D32A mutant is unable to bind NAD+, is enzymatically inactive and has almost completely lost the ability to bind telomere. Upon expression in A-549 cells, mutant localizes to the nucleus but is unable to confer any significant protection of telomeres against chemotherapy-induced degradation or growth inhibition Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Homo sapiens 5829
-
nucleus
-
Homo sapiens 5634
-

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
A-549 cell
-
Homo sapiens
-
liver
-
Homo sapiens
-

Subunits

Subunits Comment Organism
More recombinant GAPDH binds directly with high affinity to a single-stranded oligonucleotide comprising three telomeric DNA repeats. Nucleotides T1, G5, and G6 of the TTAGGG repeat are essential for binding.The stoichiometry of the interaction is 2:1 DNA:GAPDH, and GAPDH appears to form a high-molecular-weight complex when bound to the oligonucleotide Homo sapiens