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BS‐RNase tetramers: An example of domain‐swapped oligomers
Author(s) -
Adinolfi Salvatore,
Piccoli Renata,
Sica Filomena,
Mazzarella Lelio
Publication year - 1996
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(96)01034-4
Subject(s) - tetramer , rnase p , ribonuclease , rnase mrp , chemistry , rnase h , hydrolase , rnase ph , domain (mathematical analysis) , enzyme , stereochemistry , biochemistry , rna , gene , mathematical analysis , mathematics
In the ribonuclease superfamily, dimericity is a unique feature of bovine seminal RNase (BS‐RNase). In about two‐thirds of native BS‐RNase molecules, the two subunits interchange their N‐terminal tails, thus generating domain‐swapped dimers (MxM), which mostly responsible for enzyme biological activities and allostericity. Higher molecular weight BS‐RNase oligomers can also be prepared [Libonati, M. (1969) Ital. J. Biochem. 18, 407–417.]. This paper reports on BS‐RNase tetrameric derivatives which were isolated and enzymatically characterized. The data collected and the analysis of the crystal packing of MxM dimers suggested a structural model for tetramer assembly, in which the four subunits are enchained by multiple domain‐swapping events.