Biochemical evidence for conformational variants in the
anti-viral and pro-metastatic protein IFITM1

J 2024

Biochemical evidence for conformational variants in the anti-viral and pro-metastatic protein IFITM1

NEKULOVÁ, Marta; Marta WYSZKOWSKA; Nela FRIEDLOVÁ; Lukáš UHRÍK; Filip ZAVADIL KOKÁŠ et al.

Základní údaje

Originální název

Biochemical evidence for conformational variants in the anti-viral and pro-metastatic protein IFITM1

Autoři

NEKULOVÁ, Marta; Marta WYSZKOWSKA; Nela FRIEDLOVÁ; Lukáš UHRÍK; Filip ZAVADIL KOKÁŠ; Václav HRABAL; Lenka HERNYCHOVÁ; Bořivoj VOJTĚŠEK; Ted R. HUPP a Michał SZYMAŃSKI

Vydání

Biological Chemistry, GERMANY, Walter de Gruyter GmbH, 2024, 1431-6730

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 2.400

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14310/24:00136749

Organizační jednotka

Přírodovědecká fakulta

Klíčová slova anglicky

hydrogen deuterium exchange; IFITM proteins; oligomerization; protein conformation; protein structure

Štítky

14314010, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 28. 1. 2025 10:06, Mgr. Marie Novosadová Šípková, DiS.

Anotace

V originále

Interferon induced transmembrane proteins (IFITMs) play a dual role in the restriction of RNA viruses and in cancer progression, yet the mechanism of their action remains unknown. Currently, there is no data about the basic biochemical features or biophysical properties of the IFITM1 protein. In this work, we report on description and biochemical characterization of three conformational variants/oligomeric species of recombinant IFITM1 protein derived from an Escherichia coli expression system. The protein was extracted from the membrane fraction, affinity purified, and separated by size exclusion chromatography where two distinct oligomeric species were observed in addition to the expected monomer. These species remained stable upon re-chromatography and were designated as “dimer” and “oligomer” according to their estimated molecular weight. The dimer was found to be less stable compared to the oligomer using circular dichroism thermal denaturation and incubation with a reducing agent. A two-site ELISA and HDX mass spectrometry suggested the existence of structural motif within the N-terminal part of IFITM1 which might be significant in oligomer formation. Together, these data show the unusual propensity of recombinant IFITM1 to naturally assemble into very stable oligomeric species whose study might shed light on IFITM1 anti-viral and pro-oncogenic functions in cells.

Citovat

NEKULOVÁ, Marta; Marta WYSZKOWSKA; Nela FRIEDLOVÁ; Lukáš UHRÍK; Filip ZAVADIL KOKÁŠ; Václav HRABAL; Lenka HERNYCHOVÁ; Bořivoj VOJTĚŠEK; Ted R. HUPP a Michał SZYMAŃSKI. Biochemical evidence for conformational variants in the anti-viral and pro-metastatic protein IFITM1. Biological Chemistry. GERMANY: Walter de Gruyter GmbH, 2024, roč. 405, č. 5, s. 311-324. ISSN 1431-6730. Dostupné z: https://doi.org/10.1515/hsz-2023-0327.

@article{2422717,
   author = {Nekulová, Marta and Wyszkowska, Marta and Friedlová, Nela and Uhrík, Lukáš and Zavadil Kokáš, Filip and Hrabal, Václav and Hernychová, Lenka and Vojtěšek, Bořivoj and Hupp, Ted R. and Szymański, Michał},
   article_location = {GERMANY},
   article_number = {5},
   doi = {https://doi.org/10.1515/hsz-2023-0327},
   keywords = {hydrogen deuterium exchange; IFITM proteins; oligomerization; protein conformation; protein structure},
   language = {eng},
   issn = {1431-6730},
   journal = {Biological Chemistry},
   title = {Biochemical evidence for conformational variants in the anti-viral and pro-metastatic protein IFITM1},
   url = {https://www.degruyter.com/document/doi/10.1515/hsz-2023-0327/html},
   volume = {405},
   year = {2024}
}

TY  - JOUR
ID  - 2422717
AU  - Nekulová, Marta - Wyszkowska, Marta - Friedlová, Nela - Uhrík, Lukáš - Zavadil Kokáš, Filip - Hrabal, Václav - Hernychová, Lenka - Vojtěšek, Bořivoj - Hupp, Ted R. - Szymański, Michał
PY  - 2024
TI  - Biochemical evidence for conformational variants in the anti-viral and pro-metastatic protein IFITM1
JF  - Biological Chemistry
VL  - 405
IS  - 5
SP  - 311-324
EP  - 311-324
PB  - Walter de Gruyter GmbH
SN  - 14316730
KW  - hydrogen deuterium exchange
KW  - IFITM proteins
KW  - oligomerization
KW  - protein conformation
KW  - protein structure
UR  - https://www.degruyter.com/document/doi/10.1515/hsz-2023-0327/html
N2  - Interferon induced transmembrane proteins (IFITMs) play a dual role in the restriction of RNA viruses and in cancer progression, yet the mechanism of their action remains unknown. Currently, there is no data about the basic biochemical features or biophysical properties of the IFITM1 protein. In this work, we report on description and biochemical characterization of three conformational variants/oligomeric species of recombinant IFITM1 protein derived from an Escherichia coli expression system. The protein was extracted from the membrane fraction, affinity purified, and separated by size exclusion chromatography where two distinct oligomeric species were observed in addition to the expected monomer. These species remained stable upon re-chromatography and were designated as “dimer” and “oligomer” according to their estimated molecular weight. The dimer was found to be less stable compared to the oligomer using circular dichroism thermal denaturation and incubation with a reducing agent. A two-site ELISA and HDX mass spectrometry suggested the existence of structural motif within the N-terminal part of IFITM1 which might be significant in oligomer formation. Together, these data show the unusual propensity of recombinant IFITM1 to naturally assemble into very stable oligomeric species whose study might shed light on IFITM1 anti-viral and pro-oncogenic functions in cells.
ER  -

NEKULOVÁ, Marta; Marta WYSZKOWSKA; Nela FRIEDLOVÁ; Lukáš UHRÍK; Filip ZAVADIL KOKÁŠ; Václav HRABAL; Lenka HERNYCHOVÁ; Bořivoj VOJTĚŠEK; Ted R. HUPP a Michał SZYMA$\backslash$'NSKI. Biochemical evidence for conformational variants in the anti-viral and pro-metastatic protein IFITM1. \textit{Biological Chemistry}. GERMANY: Walter de Gruyter GmbH, 2024, roč.~405, č.~5, s.~311-324. ISSN~1431-6730. Dostupné z: https://doi.org/10.1515/hsz-2023-0327.

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