A new type of RNase T2 ribonuclease in two Basidiomycetes fungi, Lentinus edodes and Irpex lacteus.
Two new RNase T2 Ribonucleases, RNase Le37 and Irp3, with a molecular mass of 45 kDa, have been isolated from Basidiomycetes fungi, Lentinus edodes and Irpex lacteus, respectively. The ribonucleases consisted of three domains: an RNase active domain, a Ser/Thr rich domain similar to that of many fungal glycanhydrolases, and a C-terminal 10 kDa domain similar to that of RNase Rny1 in yeast. The locations of hydrophobic amino acids and Pro in the 10 kDa domain of the two basidiomycetous enzymes are very similar to those of RNase Rny1, indicating that these domains may have similar roles.
Kobayashi
Hiroko
H
Department of Microbiology, College of Pharmacy, Nihon University, Narashinodai, Funabashi, Chiba, Japan.
Itagaki
Tadashi
T
Inokuchi
Norio
N
Ohgi
Kazuko
K
Wada
Tatsuya
T
Iwama
Masanori
M
Irie
Masachika
M
D000595:Amino Acid Sequence; D001487:Basidiomycota / Q000201:enzymology*; D004722:Endoribonucleases / Q000737:chemistry* / Q000302:isolation & purification; D057927:Hydrophobic and Hydrophilic Interactions; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D020942:Shiitake Mushrooms / Q000201:enzymology
D004722:Endoribonucleases; C022543:ribonuclease T(2)