Biochemical evidence for conformational variants in the anti-viral and pro-metastatic protein IFITM1
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F24%3A00079658" target="_blank" >RIV/00209805:_____/24:00079658 - isvavai.cz</a>
Alternative codes found
RIV/00216224:14310/24:00136749
Result on the web
<a href="https://pubmed.ncbi.nlm.nih.gov/38379409/" target="_blank" >https://pubmed.ncbi.nlm.nih.gov/38379409/</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1515/hsz-2023-0327" target="_blank" >10.1515/hsz-2023-0327</a>
Alternative languages
Result language
angličtina
Original language name
Biochemical evidence for conformational variants in the anti-viral and pro-metastatic protein IFITM1
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/GA22-02940S" target="_blank" >GA22-02940S: Regulation of IFN-γ signaling pathway with HSP90 inhibitors</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2024
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Biological chemistry
ISSN
1431-6730
e-ISSN
1437-4315
Volume of the periodical
405
Issue of the periodical within the volume
5
Country of publishing house
DE - GERMANY
Number of pages
14
Pages from-to
311-324
UT code for WoS article
001173488600001
EID of the result in the Scopus database
2-s2.0-85185789619