Substrate specificity of monomeric and dimeric α‐sarcin

FEBS Letters

Cheung, Jin-I.²  Wang, Yuh-Ru¹  Lin, Alan¹ 

[1] Institute of Genetics, National Yang-Ming University, Shih-Pai, Taipei, Taiwan;Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, Taiwan

关键词: Ribotoxin;    Ribosomes;    Stem-loop RNA;    Supercoiled DNA;    Membrane blotting hydrolysis;   

DOI  :  10.1016/0014-5793(96)00404-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The substrate specificity of monomeric and dimeric forms of α-sarcin was investigated by membrane blotting procedures. Dimeric α-sarcin fails to inactivate ribosomes as well as to hydrolyze mini-stem-loop RNA, whereas monomeric α-sarcin catalyzes both substrates. Both monomeric and dimeric α-sarcin are effective ribonucleases that are displayed by in situ RNA-impregnated gel electrophoresis. The same purine base specificity was detected for both dimeric and monomeric forms. α-Sarcin is also an effective deoxyribonuclease to supercoiled DNA. The action of α-sarcin as deoxyribonuclease and ribonuclease is inhibited by the presence of SDS (3.5 × 10⁻⁶ M); the inhibition on ribonuclease, but not on deoxyribonuclease, is reversible if the proteins are renatured.

【 授权许可】

Unknown