Lu, L., Zhai, X., Li, X., Wang, S., Zhang, L., Wang, L., Jin, X., Liang, L., Deng, Z., Li, Z., Wang, Y., Fu, X., Hu, H., Wang, J., Mei, Z., He, Z., & Wang, F. (2022). Met1-specific motifs conserved in OTUB subfamily of green plants enable rice OTUB1 to hydrolyse Met1 ubiquitin chains. Nature Communications, 13(1), Article 4672. https://doi.org/10.1038/s41467-022-32364-3
Lu, Lining ; Zhai, Xiaoguo ; Li, Xiaolong et al. / Met1-specific motifs conserved in OTUB subfamily of green plants enable rice OTUB1 to hydrolyse Met1 ubiquitin chains. In: Nature Communications. 2022 ; Vol. 13, No. 1.
@article{70ef552c8c004878851c19de9017eb00,
title = "Met1-specific motifs conserved in OTUB subfamily of green plants enable rice OTUB1 to hydrolyse Met1 ubiquitin chains",
abstract = "Linear (Met1-linked) ubiquitination is involved inflammatory and innate immune signaling. Previous studies have characterized enzymes regulating the addition and removal of this modification in mammalian systems. However, only a few plant-derived deubiquitinases targeting Met1-linked ubiquitin chains have been reported and their mechanism of action remains elusive. Here, using a dehydroalanine-bearing Met1-diubiquitin suicide probe, we discover OTUB1 from Oryza sativa (OsOTUB1) as a Met1-linked ubiquitin chain-targeting deubiquitinase. By solving crystal structures of apo OsOTUB1 and an OsOTUB1/Met1-diubiquitin complex, we find that Met1 activity is conferred by Met1-specific motifs in the S1{\textquoteright} pocket of OsOTUB1. Large-scale sequence alignments and hydrolysis experiments provide evidence that these motifs are a general determinant of Met1 activity in the OTUB subfamily across species. Analysis of the species distribution of OTUBs capable of hydrolysing Met1-linked ubiquitin chains shows that this activity is conserved in green plants (Viridiplantae) and does not exist in metazoans, providing insights into the evolutionary differentiation between primitive plants and animals.",
author = "Lining Lu and Xiaoguo Zhai and Xiaolong Li and Shuansuo Wang and Lijun Zhang and Luyang Wang and Xi Jin and Lujun Liang and Zhiheng Deng and Zichen Li and Yanfeng Wang and Xiangdong Fu and Honggang Hu and Jiawei Wang and Ziqing Mei and Zhengguo He and Feng Wang",
note = "Publisher Copyright: {\textcopyright} 2022, The Author(s).",
year = "2022",
month = dec,
doi = "10.1038/s41467-022-32364-3",
language = "English",
volume = "13",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",
number = "1",
}
Lu, L, Zhai, X, Li, X, Wang, S, Zhang, L, Wang, L, Jin, X, Liang, L, Deng, Z, Li, Z, Wang, Y, Fu, X, Hu, H, Wang, J, Mei, Z, He, Z & Wang, F 2022, 'Met1-specific motifs conserved in OTUB subfamily of green plants enable rice OTUB1 to hydrolyse Met1 ubiquitin chains', Nature Communications, vol. 13, no. 1, 4672. https://doi.org/10.1038/s41467-022-32364-3
Met1-specific motifs conserved in OTUB subfamily of green plants enable rice OTUB1 to hydrolyse Met1 ubiquitin chains. / Lu, Lining; Zhai, Xiaoguo; Li, Xiaolong et al.
In:
Nature Communications, Vol. 13, No. 1, 4672, 12.2022.
Research output: Contribution to journal › Article › peer-review
TY - JOUR
T1 - Met1-specific motifs conserved in OTUB subfamily of green plants enable rice OTUB1 to hydrolyse Met1 ubiquitin chains
AU - Lu, Lining
AU - Zhai, Xiaoguo
AU - Li, Xiaolong
AU - Wang, Shuansuo
AU - Zhang, Lijun
AU - Wang, Luyang
AU - Jin, Xi
AU - Liang, Lujun
AU - Deng, Zhiheng
AU - Li, Zichen
AU - Wang, Yanfeng
AU - Fu, Xiangdong
AU - Hu, Honggang
AU - Wang, Jiawei
AU - Mei, Ziqing
AU - He, Zhengguo
AU - Wang, Feng
N1 - Publisher Copyright:
© 2022, The Author(s).
PY - 2022/12
Y1 - 2022/12
N2 - Linear (Met1-linked) ubiquitination is involved inflammatory and innate immune signaling. Previous studies have characterized enzymes regulating the addition and removal of this modification in mammalian systems. However, only a few plant-derived deubiquitinases targeting Met1-linked ubiquitin chains have been reported and their mechanism of action remains elusive. Here, using a dehydroalanine-bearing Met1-diubiquitin suicide probe, we discover OTUB1 from Oryza sativa (OsOTUB1) as a Met1-linked ubiquitin chain-targeting deubiquitinase. By solving crystal structures of apo OsOTUB1 and an OsOTUB1/Met1-diubiquitin complex, we find that Met1 activity is conferred by Met1-specific motifs in the S1’ pocket of OsOTUB1. Large-scale sequence alignments and hydrolysis experiments provide evidence that these motifs are a general determinant of Met1 activity in the OTUB subfamily across species. Analysis of the species distribution of OTUBs capable of hydrolysing Met1-linked ubiquitin chains shows that this activity is conserved in green plants (Viridiplantae) and does not exist in metazoans, providing insights into the evolutionary differentiation between primitive plants and animals.
AB - Linear (Met1-linked) ubiquitination is involved inflammatory and innate immune signaling. Previous studies have characterized enzymes regulating the addition and removal of this modification in mammalian systems. However, only a few plant-derived deubiquitinases targeting Met1-linked ubiquitin chains have been reported and their mechanism of action remains elusive. Here, using a dehydroalanine-bearing Met1-diubiquitin suicide probe, we discover OTUB1 from Oryza sativa (OsOTUB1) as a Met1-linked ubiquitin chain-targeting deubiquitinase. By solving crystal structures of apo OsOTUB1 and an OsOTUB1/Met1-diubiquitin complex, we find that Met1 activity is conferred by Met1-specific motifs in the S1’ pocket of OsOTUB1. Large-scale sequence alignments and hydrolysis experiments provide evidence that these motifs are a general determinant of Met1 activity in the OTUB subfamily across species. Analysis of the species distribution of OTUBs capable of hydrolysing Met1-linked ubiquitin chains shows that this activity is conserved in green plants (Viridiplantae) and does not exist in metazoans, providing insights into the evolutionary differentiation between primitive plants and animals.
UR - http://www.scopus.com/inward/record.url?scp=85135627040&partnerID=8YFLogxK
U2 - 10.1038/s41467-022-32364-3
DO - 10.1038/s41467-022-32364-3
M3 - Article
C2 - 35945250
AN - SCOPUS:85135627040
SN - 2041-1723
VL - 13
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 4672
ER -
Lu L, Zhai X, Li X, Wang S, Zhang L, Wang L et al. Met1-specific motifs conserved in OTUB subfamily of green plants enable rice OTUB1 to hydrolyse Met1 ubiquitin chains. Nature Communications. 2022 Dec;13(1):4672. doi: 10.1038/s41467-022-32364-3
