ArticlePloS one2012
Double domain swapping in bovine seminal RNase: formation of distinct N- and C-swapped tetramers and multimers with increasing biological activities.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Structure of angiogenin dimer bound to double-stranded RNA.Acta crystallographica. Section F, Structural biology communications · 2022Article
- Emerging biological functions of ribonuclease 1 and angiogenin.Critical reviews in biochemistry and molecular biology · 2022Review
- Dimerization of Human Angiogenin and of Variants Involved in Neurodegenerative Diseases.International journal of molecular sciences · 2021Article
- Unveiling the dimer/monomer propensities of Smad MH1-DNA complexes.Computational and structural biotechnology journal · 2021Article
- The Cytotoxicity of RNase-Derived Peptides.Biomolecules · 2020Article
- Biological Activities of Secretory RNases: Focus on Their Oligomerization to Design Antitumor Drugs.Frontiers in immunology · 2019Review
- Homodimerisation-independent cleavage of dsRNA by a pestiviral nicking endoribonuclease.Scientific reports · 2018Article
- Immune Modulation by Human Secreted RNases at the Extracellular Space.Frontiers in immunology · 2018Review
- The Native Monomer of Bacillus Pumilus Ribonuclease Does Not Exist Extracellularly.BioMed research international · 2018Article
- Amino-acid composition after loop deletion drives domain swapping.Protein science : a publication of the Protein Society · 2017Article
- Small Molecule-Induced Domain Swapping as a Mechanism for Controlling Protein Function and Assembly.Scientific reports · 2017Article
- Formation and carbon monoxide-dependent dissociation of Allochromatium vinosum cytochrome c' oligomers using domain-swapped dimers.Protein science : a publication of the Protein Society · 2017Article
- Three-Dimensional Domain Swapping Changes the Folding Mechanism of the Forkhead Domain of FoxP1.Biophysical journal · 2016Article
- Engineered Domain Swapping as an On/Off Switch for Protein Function.Chemistry & biology · 2015Article
- Allosteric modulation of protein oligomerization: an emerging approach to drug design.Frontiers in chemistry · 2014Review
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7 authors.
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Abstract
Bovine seminal (BS) RNase, the unique natively dimeric member of the RNase super-family, represents a special case not only for its additional biological actions but also for the singular features of 3D domain swapping. The native enzyme is indeed a mixture of two isoforms: M = M, a dimer held together by two inter-subunit disulfide bonds, and MxM, 70% of the total, which, besides the two mentioned disulfides, is additionally stabilized by the swapping of its N-termini.When lyophilized from 40% acetic acid, BS-RNase oligomerizes as the super-family proto-type RNase A does. In this paper, we induced BS-RNase self-association and analyzed the multimers by size-exclusion chromatography, cross-linking, electrophoresis, mutagenesis, dynamic light scattering, molecular modelling. Finally, we evaluated their enzymatic and cytotoxic activities.Several BS-RNase domain-swapped oligomers were detected, including two tetramers, one exchanging only the N-termini, the other being either N- or C-swapped. The C-swapping event, confirmed by results on a BS-K113N mutant, has been firstly seen in BS-RNase here, and probably stabilizes also multimers larger than tetramers.Interestingly, all BS-RNase oligomers are more enzymatically active than the native dimer and, above all, they display a cytotoxic activity that definitely increases with the molecular weight of the multimers. This latter feature, to date unknown for BS-RNase, suggests again that the self-association of RNases strongly modulates their biological and potentially therapeutic properties.
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