Lyophyllin, a Mushroom Protein from the Peptidase M35 Superfamily Is an RNA N-Glycosidase

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 <i...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Jia-Qi Lu, Wei-Wei Shi, Meng-Jie Xiao, Yun-Sang Tang, Yong-Tang Zheng, Pang-Chui Shaw
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	ribosome-inactivating proteins lyophyllin peptidase M35 superfamily N-glycosidase Biology (General) QH301-705.5 Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/306391f613684f86b2abf996d4a2218d
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:306391f613684f86b2abf996d4a2218d
record_format	dspace
spelling	oai:doaj.org-article:306391f613684f86b2abf996d4a2218d2021-11-11T17:04:40ZLyophyllin, a Mushroom Protein from the Peptidase M35 Superfamily Is an RNA N-Glycosidase10.3390/ijms2221115981422-00671661-6596https://doaj.org/article/306391f613684f86b2abf996d4a2218d2021-10-01T00:00:00Zhttps://www.mdpi.com/1422-0067/22/21/11598https://doaj.org/toc/1661-6596https://doaj.org/toc/1422-0067Ribosome-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 <i>Lyophyllum shimeji</i>, 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.Jia-Qi LuWei-Wei ShiMeng-Jie XiaoYun-Sang TangYong-Tang ZhengPang-Chui ShawMDPI AGarticleribosome-inactivating proteinslyophyllinpeptidase M35 superfamilyN-glycosidaseBiology (General)QH301-705.5ChemistryQD1-999ENInternational Journal of Molecular Sciences, Vol 22, Iss 11598, p 11598 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	ribosome-inactivating proteins lyophyllin peptidase M35 superfamily N-glycosidase Biology (General) QH301-705.5 Chemistry QD1-999
spellingShingle	ribosome-inactivating proteins lyophyllin peptidase M35 superfamily N-glycosidase Biology (General) QH301-705.5 Chemistry QD1-999 Jia-Qi Lu Wei-Wei Shi Meng-Jie Xiao Yun-Sang Tang Yong-Tang Zheng Pang-Chui Shaw Lyophyllin, a Mushroom Protein from the Peptidase M35 Superfamily Is an RNA N-Glycosidase
description	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 <i>Lyophyllum shimeji</i>, 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.
format	article
author	Jia-Qi Lu Wei-Wei Shi Meng-Jie Xiao Yun-Sang Tang Yong-Tang Zheng Pang-Chui Shaw
author_facet	Jia-Qi Lu Wei-Wei Shi Meng-Jie Xiao Yun-Sang Tang Yong-Tang Zheng Pang-Chui Shaw
author_sort	Jia-Qi Lu
title	Lyophyllin, a Mushroom Protein from the Peptidase M35 Superfamily Is an RNA N-Glycosidase
title_short	Lyophyllin, a Mushroom Protein from the Peptidase M35 Superfamily Is an RNA N-Glycosidase
title_full	Lyophyllin, a Mushroom Protein from the Peptidase M35 Superfamily Is an RNA N-Glycosidase
title_fullStr	Lyophyllin, a Mushroom Protein from the Peptidase M35 Superfamily Is an RNA N-Glycosidase
title_full_unstemmed	Lyophyllin, a Mushroom Protein from the Peptidase M35 Superfamily Is an RNA N-Glycosidase
title_sort	lyophyllin, a mushroom protein from the peptidase m35 superfamily is an rna n-glycosidase
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/306391f613684f86b2abf996d4a2218d
work_keys_str_mv	AT jiaqilu lyophyllinamushroomproteinfromthepeptidasem35superfamilyisanrnanglycosidase AT weiweishi lyophyllinamushroomproteinfromthepeptidasem35superfamilyisanrnanglycosidase AT mengjiexiao lyophyllinamushroomproteinfromthepeptidasem35superfamilyisanrnanglycosidase AT yunsangtang lyophyllinamushroomproteinfromthepeptidasem35superfamilyisanrnanglycosidase AT yongtangzheng lyophyllinamushroomproteinfromthepeptidasem35superfamilyisanrnanglycosidase AT pangchuishaw lyophyllinamushroomproteinfromthepeptidasem35superfamilyisanrnanglycosidase
_version_	1718432168304181248

Lyophyllin, a Mushroom Protein from the Peptidase M35 Superfamily Is an RNA N-Glycosidase

Ejemplares similares