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The antitumor action of seminal ribonuclease and its quaternary conformations
Author(s) -
Cafaro Valeria,
De Lorenzo Claudia,
Piccoli Renata,
Bracale Aurora,
Mastronicola Maria Rosaria,
Di Donato Alberto,
D'Alessio Giuseppe
Publication year - 1995
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(94)01450-f
Subject(s) - rnase p , protein quaternary structure , ribonuclease , bovine pancreatic ribonuclease , chemistry , enzyme , stereochemistry , s tag , ribonuclease iii , biochemistry , rnase mrp , protein subunit , microbiology and biotechnology , biology , rna , rna interference , gene
It has been previously shown that the antitumor action of bovine seminal ribonuclease (BS‐RNase) is dependent on its dimeric structure. However, two distinct quaternary structures, each in equilibrium with the other, have been described for the enzyme: one in which the two subunits exchange their N‐terminal ends, the other with no exchange. Antitumor activity assays, carried out on homogeneous quaternary forms of the enzyme, as well as on dimeric mutants of bovine pancreatic RNase A, reveal that another structural determinant of the antitumor activity of BS‐RNase is the exchange of N‐terminal ends between subunits.