A seven-transmembrane methyltransferase catalysing N-terminal histidine methylation of lytic polysaccharide monooxygenases

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

A seven-transmembrane methyltransferase catalysing N-terminal histidine methylation of lytic polysaccharide monooxygenases. / Batth, Tanveer S.; Simonsen, Jonas L.; Hernández-Rollán, Cristina; Brander, Søren; Morth, Jens Preben; Johansen, Katja S.; Nørholm, Morten H.H.; Hoof, Jakob B.; Olsen, Jesper V.

In: Nature Communications, Vol. 14, 4202, 2023.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Batth, TS, Simonsen, JL, Hernández-Rollán, C, Brander, S, Morth, JP, Johansen, KS, Nørholm, MHH, Hoof, JB & Olsen, JV 2023, 'A seven-transmembrane methyltransferase catalysing N-terminal histidine methylation of lytic polysaccharide monooxygenases', Nature Communications, vol. 14, 4202. https://doi.org/10.1038/s41467-023-39875-7

APA

Batth, T. S., Simonsen, J. L., Hernández-Rollán, C., Brander, S., Morth, J. P., Johansen, K. S., Nørholm, M. H. H., Hoof, J. B., & Olsen, J. V. (2023). A seven-transmembrane methyltransferase catalysing N-terminal histidine methylation of lytic polysaccharide monooxygenases. Nature Communications, 14, [4202]. https://doi.org/10.1038/s41467-023-39875-7

Vancouver

Batth TS, Simonsen JL, Hernández-Rollán C, Brander S, Morth JP, Johansen KS et al. A seven-transmembrane methyltransferase catalysing N-terminal histidine methylation of lytic polysaccharide monooxygenases. Nature Communications. 2023;14. 4202. https://doi.org/10.1038/s41467-023-39875-7

Author

Batth, Tanveer S. ; Simonsen, Jonas L. ; Hernández-Rollán, Cristina ; Brander, Søren ; Morth, Jens Preben ; Johansen, Katja S. ; Nørholm, Morten H.H. ; Hoof, Jakob B. ; Olsen, Jesper V. / A seven-transmembrane methyltransferase catalysing N-terminal histidine methylation of lytic polysaccharide monooxygenases. In: Nature Communications. 2023 ; Vol. 14.

Bibtex

@article{5ce0660b4b014d8cbb05ffdc9dabdd6d,
title = "A seven-transmembrane methyltransferase catalysing N-terminal histidine methylation of lytic polysaccharide monooxygenases",
abstract = "Lytic polysaccharide monooxygenases (LPMOs) are oxidative enzymes that help break down lignocellulose, making them highly attractive for improving biomass utilization in industrial biotechnology. The catalytically essential N-terminal histidine (His1) of LPMOs is post-translationally modified by methylation in filamentous fungi to protect them from auto-oxidative inactivation, however, the responsible methyltransferase enzyme is unknown. Using mass-spectrometry-based quantitative proteomics in combination with systematic CRISPR/Cas9 knockout screening in Aspergillus nidulans, we identify the N-terminal histidine methyltransferase (NHMT) encoded by the gene AN4663. Targeted proteomics confirm that NHMT was solely responsible for His1 methylation of LPMOs. NHMT is predicted to encode a unique seven-transmembrane segment anchoring a soluble methyltransferase domain. Co-localization studies show endoplasmic reticulum residence of NHMT and co-expression in the industrial production yeast Komagataella phaffii with LPMOs results in His1 methylation of the LPMOs. This demonstrates the biotechnological potential of recombinant production of proteins and peptides harbouring this specific post-translational modification.",
author = "Batth, {Tanveer S.} and Simonsen, {Jonas L.} and Cristina Hern{\'a}ndez-Roll{\'a}n and S{\o}ren Brander and Morth, {Jens Preben} and Johansen, {Katja S.} and N{\o}rholm, {Morten H.H.} and Hoof, {Jakob B.} and Olsen, {Jesper V.}",
note = "Publisher Copyright: {\textcopyright} 2023, The Author(s).",
year = "2023",
doi = "10.1038/s41467-023-39875-7",
language = "English",
volume = "14",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - A seven-transmembrane methyltransferase catalysing N-terminal histidine methylation of lytic polysaccharide monooxygenases

AU - Batth, Tanveer S.

AU - Simonsen, Jonas L.

AU - Hernández-Rollán, Cristina

AU - Brander, Søren

AU - Morth, Jens Preben

AU - Johansen, Katja S.

AU - Nørholm, Morten H.H.

AU - Hoof, Jakob B.

AU - Olsen, Jesper V.

N1 - Publisher Copyright: © 2023, The Author(s).

PY - 2023

Y1 - 2023

N2 - Lytic polysaccharide monooxygenases (LPMOs) are oxidative enzymes that help break down lignocellulose, making them highly attractive for improving biomass utilization in industrial biotechnology. The catalytically essential N-terminal histidine (His1) of LPMOs is post-translationally modified by methylation in filamentous fungi to protect them from auto-oxidative inactivation, however, the responsible methyltransferase enzyme is unknown. Using mass-spectrometry-based quantitative proteomics in combination with systematic CRISPR/Cas9 knockout screening in Aspergillus nidulans, we identify the N-terminal histidine methyltransferase (NHMT) encoded by the gene AN4663. Targeted proteomics confirm that NHMT was solely responsible for His1 methylation of LPMOs. NHMT is predicted to encode a unique seven-transmembrane segment anchoring a soluble methyltransferase domain. Co-localization studies show endoplasmic reticulum residence of NHMT and co-expression in the industrial production yeast Komagataella phaffii with LPMOs results in His1 methylation of the LPMOs. This demonstrates the biotechnological potential of recombinant production of proteins and peptides harbouring this specific post-translational modification.

AB - Lytic polysaccharide monooxygenases (LPMOs) are oxidative enzymes that help break down lignocellulose, making them highly attractive for improving biomass utilization in industrial biotechnology. The catalytically essential N-terminal histidine (His1) of LPMOs is post-translationally modified by methylation in filamentous fungi to protect them from auto-oxidative inactivation, however, the responsible methyltransferase enzyme is unknown. Using mass-spectrometry-based quantitative proteomics in combination with systematic CRISPR/Cas9 knockout screening in Aspergillus nidulans, we identify the N-terminal histidine methyltransferase (NHMT) encoded by the gene AN4663. Targeted proteomics confirm that NHMT was solely responsible for His1 methylation of LPMOs. NHMT is predicted to encode a unique seven-transmembrane segment anchoring a soluble methyltransferase domain. Co-localization studies show endoplasmic reticulum residence of NHMT and co-expression in the industrial production yeast Komagataella phaffii with LPMOs results in His1 methylation of the LPMOs. This demonstrates the biotechnological potential of recombinant production of proteins and peptides harbouring this specific post-translational modification.

U2 - 10.1038/s41467-023-39875-7

DO - 10.1038/s41467-023-39875-7

M3 - Journal article

C2 - 37452022

AN - SCOPUS:85164754351

VL - 14

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 4202

ER -

ID: 361437585