Exogenous and endogenous agents including products
generated by oxidative stress, chemotherapeutics
and bacterial lipids, activate multiple cellular signaling
pathways, resulting either in mitogenesis or
in apoptosis. Glutathione transferases (GSTs) appear
not only to be prominent catalysts of detoxication reactions,
but also to play a pivotal role in signaling by
interacting with multiple proteins in pathways induced
by cellular stress.
Using two peptide libraries (a 9-mer and a 15-mer)
displayed on phage, novel GST-peptide interactions
were identified using human GST A1-1, GST P1-1 and
GST M2-2 as targets. The isolated peptides have high
sequence similarity with proteins such as TRAF4-associated
factor 1, G protein-coupled receptor MRGX3,
tumor necrosis factor superfamily (member 9), and
c-Jun N-terminal kinase 3.
Biological Chemistry keeps you up-to-date with the latest advances in the molecular life sciences. The journal publishes Research Articles, Short Communications, Reviews and Minireviews. Areas include: general biochemistry/pathobiochemistry, structural biology, molecular and cellular biology, genetics and epigenetics, virology, molecular medicine, plant molecular biology/biochemistry and novel experimental methodologies.