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Humanin binds MPP8: mapping interaction sites of the peptide and protein
Author(s) -
Maximov Vadim V.,
Martynenko Alina V.,
Arman Inga P.,
Tarantul Vyacheslav Z.
Publication year - 2013
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.2500
Subject(s) - phosphoprotein , immunoprecipitation , peptide , binding site , peptide sequence , complementary dna , microbiology and biotechnology , protein–protein interaction , biology , chemistry , cdna library , two hybrid screening , biochemistry , gene
Humanin (HN), a 24‐amino acid peptide encoded by the mitochondrial 16S rRNA gene, was discovered by screening a cDNA library from the occipital cortex of a patient with Alzheimer's disease (AD) for a protection factor against AD‐relevant insults. Earlier, using the yeast two‐hybrid system, we have identified the M‐phase phosphoprotein 8 (MPP8) as a binding partner for HN. In the present work, we further confirmed interaction of HN with MPP8 in co‐immunoprecipitation experiments and localized an MPP8‐binding site in the region between 5 and 12 aa. of HN. We have also shown that an MPP8 fragment (residues 431–560) is sufficient to bind HN. Further studies on functional consequences of the interaction between the potential oncopetide and the oncoprotein may elucidate some aspects of the molecular mechanisms of carcinogenesis. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.