M. jannaschii FtsZ, a key protein in bacterial cell division, is inactivated by peroxyl radical-mediated methionine oxidation

Research output: Contribution to journalJournal articlepeer-review

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M. jannaschii FtsZ, a key protein in bacterial cell division, is inactivated by peroxyl radical-mediated methionine oxidation. / Reyes, Juan Sebastián; Fuentes-Lemus, Eduardo; Aspée, Alexis; Davies, Michael J.; Monasterio, Octavio; López-Alarcón, Camilo.

In: Free Radical Biology and Medicine, Vol. 166, 2021, p. 53-66.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Reyes, JS, Fuentes-Lemus, E, Aspée, A, Davies, MJ, Monasterio, O & López-Alarcón, C 2021, 'M. jannaschii FtsZ, a key protein in bacterial cell division, is inactivated by peroxyl radical-mediated methionine oxidation', Free Radical Biology and Medicine, vol. 166, pp. 53-66. https://doi.org/10.1016/j.freeradbiomed.2021.02.003

APA

Reyes, J. S., Fuentes-Lemus, E., Aspée, A., Davies, M. J., Monasterio, O., & López-Alarcón, C. (2021). M. jannaschii FtsZ, a key protein in bacterial cell division, is inactivated by peroxyl radical-mediated methionine oxidation. Free Radical Biology and Medicine, 166, 53-66. https://doi.org/10.1016/j.freeradbiomed.2021.02.003

Vancouver

Reyes JS, Fuentes-Lemus E, Aspée A, Davies MJ, Monasterio O, López-Alarcón C. M. jannaschii FtsZ, a key protein in bacterial cell division, is inactivated by peroxyl radical-mediated methionine oxidation. Free Radical Biology and Medicine. 2021;166:53-66. https://doi.org/10.1016/j.freeradbiomed.2021.02.003

Author

Reyes, Juan Sebastián ; Fuentes-Lemus, Eduardo ; Aspée, Alexis ; Davies, Michael J. ; Monasterio, Octavio ; López-Alarcón, Camilo. / M. jannaschii FtsZ, a key protein in bacterial cell division, is inactivated by peroxyl radical-mediated methionine oxidation. In: Free Radical Biology and Medicine. 2021 ; Vol. 166. pp. 53-66.

Bibtex

@article{194bdeadb7144574a2f6596b59731227,
title = "M. jannaschii FtsZ, a key protein in bacterial cell division, is inactivated by peroxyl radical-mediated methionine oxidation",
abstract = "Oxidation and inactivation of FtsZ is of interest due to the key role of this protein in bacterial cell division. In the present work, we studied peroxyl radical (from AAPH, 2,2′-azobis(2-methylpropionamidine)dihydrochloride) mediated oxidation of the highly stable FtsZ protein (MjFtsZ) from M. jannaschii, a thermophilic microorganism. MjFtsZ contains eleven Met, and single Tyr and Trp residues which would be expected to be susceptible to oxidation. We hypothesized that exposure of MjFtsZ to AAPH-derived radicals would induce Met oxidation, and cross-linking (via di-Tyr and di-Trp formation), with concomitant loss of its functional polymerization and depolymerization (GTPase) activities. Solutions containing MjFtsZ and AAPH (10 or 100 mM) were incubated at 37 °C for 3 h. Polymerization/depolymerization were assessed by light scattering, while changes in mass were analyzed by SDS-PAGE. Amino acid consumption was quantified by HPLC with fluorescence detection, or direct fluorescence (Trp). Oxidation products and modifications at individual Met residues were quantified by UPLC with mass detection. Oxidation inhibited polymerization-depolymerization activity, and yielded low levels of irreversible protein dimers. With 10 mM AAPH only Trp and Met were consumed giving di-alcohols, kynurenine and di-Trp (from Trp) and the sulfoxide (from Met). With 100 mM AAPH low levels of Tyr oxidation (but not di-Tyr formation) were also observed. Correlation with the functional analyses indicates that Met oxidation, and particularly Met164 is the key driver of MjFtsZ inactivation, probably as a result of the position of this residue at the protein-protein interface of longitudinal interactions and in close proximity to the GTP binding site.",
keywords = "AAPH, di-tryptophan bonds, FtsZ, Methanococcus jannaschii, Methionine oxidation, Peroxyl radicals, Thermophiles, Tubulin",
author = "Reyes, {Juan Sebasti{\'a}n} and Eduardo Fuentes-Lemus and Alexis Asp{\'e}e and Davies, {Michael J.} and Octavio Monasterio and Camilo L{\'o}pez-Alarc{\'o}n",
note = "Publisher Copyright: {\textcopyright} 2021 Elsevier Inc.",
year = "2021",
doi = "10.1016/j.freeradbiomed.2021.02.003",
language = "English",
volume = "166",
pages = "53--66",
journal = "Free Radical Biology & Medicine",
issn = "0891-5849",
publisher = "Elsevier",

}

RIS

TY - JOUR

T1 - M. jannaschii FtsZ, a key protein in bacterial cell division, is inactivated by peroxyl radical-mediated methionine oxidation

AU - Reyes, Juan Sebastián

AU - Fuentes-Lemus, Eduardo

AU - Aspée, Alexis

AU - Davies, Michael J.

AU - Monasterio, Octavio

AU - López-Alarcón, Camilo

N1 - Publisher Copyright: © 2021 Elsevier Inc.

PY - 2021

Y1 - 2021

N2 - Oxidation and inactivation of FtsZ is of interest due to the key role of this protein in bacterial cell division. In the present work, we studied peroxyl radical (from AAPH, 2,2′-azobis(2-methylpropionamidine)dihydrochloride) mediated oxidation of the highly stable FtsZ protein (MjFtsZ) from M. jannaschii, a thermophilic microorganism. MjFtsZ contains eleven Met, and single Tyr and Trp residues which would be expected to be susceptible to oxidation. We hypothesized that exposure of MjFtsZ to AAPH-derived radicals would induce Met oxidation, and cross-linking (via di-Tyr and di-Trp formation), with concomitant loss of its functional polymerization and depolymerization (GTPase) activities. Solutions containing MjFtsZ and AAPH (10 or 100 mM) were incubated at 37 °C for 3 h. Polymerization/depolymerization were assessed by light scattering, while changes in mass were analyzed by SDS-PAGE. Amino acid consumption was quantified by HPLC with fluorescence detection, or direct fluorescence (Trp). Oxidation products and modifications at individual Met residues were quantified by UPLC with mass detection. Oxidation inhibited polymerization-depolymerization activity, and yielded low levels of irreversible protein dimers. With 10 mM AAPH only Trp and Met were consumed giving di-alcohols, kynurenine and di-Trp (from Trp) and the sulfoxide (from Met). With 100 mM AAPH low levels of Tyr oxidation (but not di-Tyr formation) were also observed. Correlation with the functional analyses indicates that Met oxidation, and particularly Met164 is the key driver of MjFtsZ inactivation, probably as a result of the position of this residue at the protein-protein interface of longitudinal interactions and in close proximity to the GTP binding site.

AB - Oxidation and inactivation of FtsZ is of interest due to the key role of this protein in bacterial cell division. In the present work, we studied peroxyl radical (from AAPH, 2,2′-azobis(2-methylpropionamidine)dihydrochloride) mediated oxidation of the highly stable FtsZ protein (MjFtsZ) from M. jannaschii, a thermophilic microorganism. MjFtsZ contains eleven Met, and single Tyr and Trp residues which would be expected to be susceptible to oxidation. We hypothesized that exposure of MjFtsZ to AAPH-derived radicals would induce Met oxidation, and cross-linking (via di-Tyr and di-Trp formation), with concomitant loss of its functional polymerization and depolymerization (GTPase) activities. Solutions containing MjFtsZ and AAPH (10 or 100 mM) were incubated at 37 °C for 3 h. Polymerization/depolymerization were assessed by light scattering, while changes in mass were analyzed by SDS-PAGE. Amino acid consumption was quantified by HPLC with fluorescence detection, or direct fluorescence (Trp). Oxidation products and modifications at individual Met residues were quantified by UPLC with mass detection. Oxidation inhibited polymerization-depolymerization activity, and yielded low levels of irreversible protein dimers. With 10 mM AAPH only Trp and Met were consumed giving di-alcohols, kynurenine and di-Trp (from Trp) and the sulfoxide (from Met). With 100 mM AAPH low levels of Tyr oxidation (but not di-Tyr formation) were also observed. Correlation with the functional analyses indicates that Met oxidation, and particularly Met164 is the key driver of MjFtsZ inactivation, probably as a result of the position of this residue at the protein-protein interface of longitudinal interactions and in close proximity to the GTP binding site.

KW - AAPH

KW - di-tryptophan bonds

KW - FtsZ

KW - Methanococcus jannaschii

KW - Methionine oxidation

KW - Peroxyl radicals

KW - Thermophiles

KW - Tubulin

UR - http://www.scopus.com/inward/record.url?scp=85101347890&partnerID=8YFLogxK

U2 - 10.1016/j.freeradbiomed.2021.02.003

DO - 10.1016/j.freeradbiomed.2021.02.003

M3 - Journal article

C2 - 33588048

AN - SCOPUS:85101347890

VL - 166

SP - 53

EP - 66

JO - Free Radical Biology & Medicine

JF - Free Radical Biology & Medicine

SN - 0891-5849

ER -

ID: 280182330