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Specific binding of glucosaminylmuramyl peptides to histones
Author(s) -
Golovina Tatyana,
Fattakhova Gulnara,
Swiderek Kristine,
Makarov Eugeni,
Bovin Nikolai,
Shively John,
Nesmeyanov Vladimir
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00689-4
Subject(s) - muramyl dipeptide , peptide , dipeptide , biochemistry , trypsin , chemistry , histone , intracellular , blot , microbiology and biotechnology , biology , in vitro , enzyme , gene
Intracellular N ‐acetylglucosaminylmuramyl peptide‐binding proteins of murine macrophages and myelomonocytic WEHI‐3 cells were characterized. SDS‐PAGE and Western blotting revealed proteins with molecular masses of 18, 32 and 34 kDa retaining the ability to specifically bind glucosaminylmuramyl dipeptide. The inhibition analysis demonstrated that only biologically active muramyl peptides but not inactive analogs or fragments of glucosaminylmuramyl dipeptide could inhibit glucosaminylmuramyl dipeptide‐binding to these proteins. Purification of these proteins and sequencing of peptides obtained after in‐gel trypsin digestion enabled us to identify the above mentioned proteins as histones H1 and H3. These findings suggest that nuclear histones might be target molecules for muramyl peptides.