BS‐RNase tetramers: An example of domain‐swapped oligomers

FEBS Letters

Sica, Filomena²  Piccoli, Renata¹  Mazzarella, Lelio²  Adinolfi, Salvatore² 

[1] Dipartimento di Chimica Organica e Biologica, Università Federico II di Napoli, Via Mezzocannone 16, 80134 Napoli, Italy;CNR, Centro di Studio di Biocristallographia and Dipartimento di Chimica, Università Federico II di Napoli, Via Mezzocannone 4, 80134 Napoli, Italy

关键词: Seminal ribonuclease;    Domain swapping;    Oligomeric structure;    BS-RNase;    bovine seminal RNase;    RNase A;    bovine pancreatic RNase;    cyd-2′:3′-P;    cytidine-2′:3′-cyclic phosphate;    DTT;    dithiothreitol;    DFDNB;    1;    5-difluoro-2;    4-dinitrobenzene;   

DOI  :  10.1016/S0014-5793(96)01034-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown