Ali P Shaik Syed, John Jasmine, Selvaraj Manikandan, Kek Teh Lay, Salleh Mohd Zaki
Institute of Biophysical Chemistry, Goethe University, Max-von-Laue-Str. 9, Frankfurt 60438, Germany.
Integrative Pharmacogenomics Institute (iPROMISE), Universiti Teknologi, MARA, 42300 Puncak Alam, Selangor, Malaysia.
Microbiol Immunol. 2015 May;59(5):299-304. doi: 10.1111/1348-0421.12253.
Nodamura virus (NoV) B2, a suppressor of RNA interference, binds double stranded RNAs (dsRNAs) and small interfering RNAs (siRNAs) corresponding to Dicer substrates and products. Here, we report that the amino terminal domain of NoV B2 (NoV B2 79) specifically binds siRNAs but not dsRNAs. NoV B2 79 oligomerizes on binding to 27 nucleotide siRNA. Mutation of the residues phenylalanine49 and alanine60 to cysteine and methionine, respectively enhances the RNA binding affinity of NoV B2 79. Circular dichroism spectra demonstrated that the wild type and mutant NoV B2 79 have similar secondary structure conformations.
诺达木拉病毒（NoV）B2是一种RNA干扰抑制因子，可结合与Dicer底物和产物相对应的双链RNA（dsRNA）和小干扰RNA（siRNA）。在此，我们报道NoV B2的氨基末端结构域（NoV B2 79）特异性结合siRNA而非dsRNA。NoV B2 79在与27个核苷酸的siRNA结合时会发生寡聚化。分别将苯丙氨酸49和丙氨酸60残基突变为半胱氨酸和甲硫氨酸可增强NoV B2 79的RNA结合亲和力。圆二色光谱表明野生型和突变型NoV B2 79具有相似的二级结构构象。
