Primary Structure and Properties of Ribonuclease Bm2 (RNase Bm2) from Bryopsis maxima

DOI Web Site Web Site 参考文献76件
  • Itagaki Tadashi
    Department of Microbiology, College of Pharmacy, Nihon University
  • Koyama Hideki
    Department of Microbiology, College of Pharmacy, Nihon University
  • Daigo Satoshi
    Department of Microbiology, College of Pharmacy, Nihon University
  • Kobayashi Hiroko
    Department of Microbiology, College of Pharmacy, Nihon University
  • Koyama Takashi
    Department of Microbiology, College of Pharmacy, Nihon University
  • Iwama Masanori
    Department of Applied Microbiology, Faculty of Pharmaceutical Sciences, Hoshi University
  • Ohgi Kazuko
    Department of Applied Microbiology, Faculty of Pharmaceutical Sciences, Hoshi University
  • Irie Masachika
    Department of Applied Microbiology, Faculty of Pharmaceutical Sciences, Hoshi University
  • Inokuchi Norio
    Department of Microbiology, College of Pharmacy, Nihon University

この論文をさがす

説明

A base non-specific ribonuclease (RNase Bm2) was isolated from a green algae (Ulvophyceae, Bryopsis maxima) as a single band on SDS-PAGE, and its primary structure and enzymatic properties, including base specificity, were investigated. The amino acid sequence of RNase Bm2 was homologous to many RNase T2 family RNases, and their characteristic CAS sequences were also conserved. The molecular mass of RNase Bm2 was 24444 Da, and its optimal pH was 5.5. RNase Bm2 was a poly U preferential RNase, similar to RNase MC1 from bitter gourd. The base specificity of this RNase suggested that the base specificity of the B1- and B2-base binding sites of RNase Bm2 were G≥U>C≫A and U>G>C≫A, respectively. The estimated active site of RNase Bm2 was very similar to that of RNase MC1 from bitter gourds; however, a tyrosine residue at the B1-base binding site that is conserved for all RNase T2 family RNases was replaced by a tryptophan residue. Here we discuss the effect of this replacement on the base specificity of RNase Bm2 and the phylogenetic relationship of RNase T2 family enzymes.

収録刊行物

参考文献 (76)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ