Selective recognition of peptide sequences by glutathione transferases: a possible mechanism for modulation of cellular stress-induced signaling pathways.
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.
Edalat
Maryam
M
Department of Biochemistry, Uppsala University, Biomedical Center, Box 576, S-751 23 Uppsala, Sweden.
Persson
Mats A A
MA
Mannervik
Bengt
B
D000595:Amino Acid Sequence; D005982:Glutathione Transferase / Q000096:biosynthesis / Q000378:metabolism*; D006801:Humans; D007527:Isoenzymes / Q000096:biosynthesis / Q000378:metabolism; D008969:Molecular Sequence Data; D019151:Peptide Library; D010455:Peptides / Q000737:chemistry*; D011485:Protein Binding; D015398:Signal Transduction / Q000502:physiology*; D013312:Stress, Physiological / Q000503:physiopathology*
D007527:Isoenzymes; D019151:Peptide Library; D010455:Peptides; D005982:Glutathione Transferase