Primary structure of a base non-specific and adenylic acid preferential ribonuclease from the fruit bodies of Lentinus edodes.
The complete primary structure of a base non-specific and adenylic acid preferential RNase (RNase Le2) from the fruit bodies of Lentinus edodes was analyzed. The sequence was mostly determined by analysis of the peptides generated by V8 protease digestion and BrCN cleavage (including alpha-chymotryptic, and V8 protease digest of BrCN fragments). It consists of 239 amino acid residues. The molecular weight is 25831. The location of 10 half cystine residues were almost superimposable on those of known fungal RNases of the RNase T2 family. The sequence homologies between RNase Le2 and four known fungal RNases of the RNase T2 family, RNase T2, RNase M, RNase Trv, and RNase Rh, are 102, 103, 109, and 74, respectively. The homologous sequences are concentrated around the three histidines, which are supposed to form the active site of RNase T2 family RNases.
Kobayashi
H
H
Department of Microbiology, College of Pharmacy, Nihon University, Chiba, Japan.
Inokuchi
N
N
Koyama
T
T
Watanabe
H
H
Iwama
M
M
Ohgi
K
K
Irie
M
M
D000363:Agaricales / Q000201:enzymology* / Q000235:genetics; D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid / Q000379:methods; D003488:Cyanogen Bromide; D010450:Endopeptidases; D004722:Endoribonucleases / Q000737:chemistry*; D005658:Fungi / Q000201:enzymology / Q000235:genetics; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000302:isolation & purification; D010449:Peptide Mapping / Q000379:methods; D010802:Phylogeny; D012260:Ribonucleases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity
D010446:Peptide Fragments; D004722:Endoribonucleases; D012260:Ribonucleases; C022543:ribonuclease T(2); D010450:Endopeptidases; D003488:Cyanogen Bromide