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J. Biochem, 1990, Vol. 108, No. 2 303-310
© 1990 Japanese Biochemical Society

research-article

Primary Structure of a Base Non-Specific and Adenylic Acid Preferential Ribonuclease from Aspergillus saitoi

Hideaki Watanabe*, Akiko Naitoh*, Yuka Suyama*, Norio Inokuchi**, Hiroko Shimada**, Takashi Koyama**, Kazuko Ohgi* and Masachika Irie*,1

*Department of Microbiology, Hoshi College of Pharmacy Shmagawa-ku, Tokyo 142
**College of Pharmacy, Nihon University Narashino, Chiba 274

1To whom correspondence should be addressed

The complete primary structure of a base non-specific and adenylic acid preferential RNase (RNase M) from Aspergillus saitoi was determined. The sequence was determined by analysis of the peptides generated by digestion of heat-denatured RNase M with lysylen dopeptidase, and the peptides generated from RCM RNase M by digestion with staphylococ cal V8 protease or chemical cleavage with BrCN. It consisted of 238 amino acid residues and carbohydrate moiety attached to the 74th asparaglne residue. The molecular weight of the protein moiety deduced from the sequence was 26,596. The locations of 10 half cystine residues are almost superimposable on those of RNase Rh from Rhizopus niveus and RNase T2 from Aspergillus oryzae which have similar base specificity. The homology between RNase M and RNase Rh and RNase T amounted to 97 and 160 amino acid residues, respectively. The amino acid sequences conserved in the three RNases are concentrated around the three histidine residues, which are supposed to form part of the acitve sites of these RNases.


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