Substrate specificity of monomeric and dimeric alpha-sarcin.
The substrate specificity of monomeric and dimeric forms of alpha-sarcin was investigated by membrane blotting procedures. Dimeric alpha-sarcin fails to inactivate ribosomes as well as to hydrolyze mini-stem-loop RNA, whereas monomeric alpha-sarcin catalyzes both substrates. Both monomeric and dimeric alpha-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. alpha-Sarcin is also an effective deoxyribonuclease to supercoiled DNA. The action of alpha-sarcin as deoxyribonuclease and ribonuclease is inhibited by the presence of SDS (3.5 x 10(-6) M); the inhibition on ribonuclease, but not on deoxyribonuclease, is reversible if the proteins are renatured.
Cheung
J I
JI
Institute of Microbiology and Immunology, National Yang-Ming University, Taipei, Taiwan.
Wang
Y R
YR
Lin
A
A
D000818:Animals; D001482:Base Composition; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D004722:Endoribonucleases; D005656:Fungal Proteins / Q000737:chemistry / Q000378:metabolism*; D008567:Membranes, Artificial; D011145:Polyvinyls; D011485:Protein Binding; D011487:Protein Conformation; D012313:RNA / Q000737:chemistry / Q000378:metabolism; D012341:RNA, Ribosomal, 5S / Q000737:chemistry / Q000378:metabolism; D011817:Rabbits; D051381:Rats; D012270:Ribosomes / Q000378:metabolism; D012967:Sodium Dodecyl Sulfate / Q000737:chemistry; D013379:Substrate Specificity
D005656:Fungal Proteins; D008567:Membranes, Artificial; D011145:Polyvinyls; D012341:RNA, Ribosomal, 5S; C014801:alpha-sarcin; D012967:Sodium Dodecyl Sulfate; D012313:RNA; D004247:DNA; D004722:Endoribonucleases