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Inhibition of protein A24 lyase by nitrosoureas
Author(s) -
Markussen Gunnar,
Smith-Kielland Ingrid,
Dornish John M.
Publication year - 1984
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 - 10.1016/0014-5793(84)81211-9
Subject(s) - chemistry , isocyanate , enzyme , biochemistry , cytoplasm , ubiquitin , histone , organic chemistry , polyurethane , gene
The protein A24 content of Ehrlich ascites tumor cells increased several‐fold following treatment of cell cultures with nitrosoureas, but did not increase when other alkylating agents not containing carbamoyl moieties were tested. The same nitrosoureas and, in addition, 2‐chloroethyl isocyanate inhibited an A24 lyase‐containing cytoplasmic extract in cleaving protein A24 into histone H2A and ubiquitin. It appears that carbamoylation of A24 lyase by nitrosoureas inhibits the enzyme and is responsible for the measured increases in cellular protein A24 content due to reduced turnover of this protein.