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Lyophyllin, a Mushroom Protein from the Peptidase M35 Superfamily Is an RNA N-Glycosidase.
Lu, Jia-Qi; Shi, Wei-Wei; Xiao, Meng-Jie; Tang, Yun-Sang; Zheng, Yong-Tang; Shaw, Pang-Chui.
Affiliation
  • Lu JQ; Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong, China.
  • Shi WW; Li Dak Sum Yip Yio Chin R & D Centre for Chinese Medicine, The Chinese University of Hong Kong, Hong Kong, China.
  • Xiao MJ; BayRay Innovation Center, Shenzhen Bay Laboratory, Shenzhen 518107, China.
  • Tang YS; Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong, China.
  • Zheng YT; Li Dak Sum Yip Yio Chin R & D Centre for Chinese Medicine, The Chinese University of Hong Kong, Hong Kong, China.
  • Shaw PC; Centre for Protein Science and Crystallography, School of Life Sciences, The Chinese University of Hong Kong, Hong Kong, China.
Int J Mol Sci ; 22(21)2021 Oct 27.
Article in En | MEDLINE | ID: mdl-34769028
Ribosome-inactivating proteins (RIPs) hydrolyze the N-glycosidic bond and depurinate a specific adenine residue (A-4324 in rat 28S ribosomal RNA, rRNA) in the conserved α-sarcin/ricin loop (α-SRL) of rRNA. In this study, we have purified and characterized lyophyllin, an unconventional RIP from Lyophyllum shimeji, an edible mushroom. The protein resembles peptidase M35 domain of peptidyl-Lys metalloendopeptidases. Nevertheless, protein either from the mushroom or in recombinant form possessed N-glycosidase and protein synthesis inhibitory activities. A homology model of lyophyllin was constructed. It was found that the zinc binding pocket of this protein resembles the catalytic cleft of a classical RIP, with key amino acids that interact with the adenine substrate in the appropriate positions. Mutational studies showed that E122 may play a role in stabilizing the positively charged oxocarbenium ion and H121 for protonating N-3 of adenine. The tyrosine residues Y137 and Y104 may be used for stacking the target adenine ring. This work first shows a protein in the peptidase M35 superfamily based on conserved domain search possessing N-glycosidase activity.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptide Hydrolases / Agaricales / Ribosome Inactivating Proteins Limits: Animals / Humans Language: En Journal: Int J Mol Sci Year: 2021 Document type: Article Affiliation country: Country of publication:

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Peptide Hydrolases / Agaricales / Ribosome Inactivating Proteins Limits: Animals / Humans Language: En Journal: Int J Mol Sci Year: 2021 Document type: Article Affiliation country: Country of publication: