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Электронный каталог: Sudarev, V. V. - Ferritin-Based Fusion Protein Shows Octameric Deadlock State of Self-Assembly
Sudarev, V. V. - Ferritin-Based Fusion Protein Shows Octameric Deadlock State of Self-Assembly
Статья
Автор: Sudarev, V. V.
Biochemical and Biophysical Research Communications [Electronic resource]: Ferritin-Based Fusion Protein Shows Octameric Deadlock State of Self-Assembly
б.г.
ISBN отсутствует
Автор: Sudarev, V. V.
Biochemical and Biophysical Research Communications [Electronic resource]: Ferritin-Based Fusion Protein Shows Octameric Deadlock State of Self-Assembly
б.г.
ISBN отсутствует
Статья
Sudarev, V.V.
Ferritin-Based Fusion Protein Shows Octameric Deadlock State of Self-Assembly / V.V.Sudarev, A.I.Kuklin, Yu.L.Ryzhykau, A.V.Vlasov, [et al.] // Biochemical and Biophysical Research Communications [Electronic resource]. – 2024. – Vol. 690. – P. 149276. – URL: https://doi.org/10.1016/j.bbrc.2023.149276. – Bibliogr.: 30.
Ferritin is a universal protein complex responsible for iron perception in almost all living organisms and has applications from fundamental biophysics to drug delivery and structure-based immunogen design. Different platforms based on ferritin share similar technological challenges limiting their development – control of self-assembling processes of ferritin itself as well as ferritin-based chimeric recombinant protein complexes. In our research, we studied self-assembly processes of ferritin-based protein complexes under different expression conditions. We fused a ferritin subunit with a SMT3 protein tag, a homolog of human Small Ubiquitin-like Modifier (SUMO-tag), which was taken to destabilize ferritin 3-fold channel contacts and increase ferritin-SUMO subunits solubility. We first obtained the octameric protein complex of ferritin-SUMO (8xFer-SUMO) and studied its structural organization by small-angle X-ray scattering (SAXS). Obtained SAXS data correspond well with the high-resolution models predicted by AlphaFold and CORAL software of an octameric assembly around the 4-fold channel of ferritin without formation of 3-fold channels. Interestingly, three copies of 8xFer-SUMO do not assemble into 24-meric globules. Thus, we first obtained and structurally characterized ferritin-based self-assembling oligomers in a deadlock state. Deadlock oligomeric states of ferritin extend the known scheme of its self-assembly process, being new potential tools for a number of applications. Finally, our results might open new directions for various biotechnological platforms utilizing ferritin-based tools.
Спец.(статьи,препринты) = С 332.8 - Синхротронное излучение. Лазеры на свободных электронах. Получение и использование рентгеновских лучей
Спец.(статьи,препринты) = 28.0 - Биология$
ОИЯИ = ОИЯИ (JINR)2024
Ключевых слов = 20/024
Sudarev, V.V.
Ferritin-Based Fusion Protein Shows Octameric Deadlock State of Self-Assembly / V.V.Sudarev, A.I.Kuklin, Yu.L.Ryzhykau, A.V.Vlasov, [et al.] // Biochemical and Biophysical Research Communications [Electronic resource]. – 2024. – Vol. 690. – P. 149276. – URL: https://doi.org/10.1016/j.bbrc.2023.149276. – Bibliogr.: 30.
Ferritin is a universal protein complex responsible for iron perception in almost all living organisms and has applications from fundamental biophysics to drug delivery and structure-based immunogen design. Different platforms based on ferritin share similar technological challenges limiting their development – control of self-assembling processes of ferritin itself as well as ferritin-based chimeric recombinant protein complexes. In our research, we studied self-assembly processes of ferritin-based protein complexes under different expression conditions. We fused a ferritin subunit with a SMT3 protein tag, a homolog of human Small Ubiquitin-like Modifier (SUMO-tag), which was taken to destabilize ferritin 3-fold channel contacts and increase ferritin-SUMO subunits solubility. We first obtained the octameric protein complex of ferritin-SUMO (8xFer-SUMO) and studied its structural organization by small-angle X-ray scattering (SAXS). Obtained SAXS data correspond well with the high-resolution models predicted by AlphaFold and CORAL software of an octameric assembly around the 4-fold channel of ferritin without formation of 3-fold channels. Interestingly, three copies of 8xFer-SUMO do not assemble into 24-meric globules. Thus, we first obtained and structurally characterized ferritin-based self-assembling oligomers in a deadlock state. Deadlock oligomeric states of ferritin extend the known scheme of its self-assembly process, being new potential tools for a number of applications. Finally, our results might open new directions for various biotechnological platforms utilizing ferritin-based tools.
Спец.(статьи,препринты) = С 332.8 - Синхротронное излучение. Лазеры на свободных электронах. Получение и использование рентгеновских лучей
Спец.(статьи,препринты) = 28.0 - Биология$
ОИЯИ = ОИЯИ (JINR)2024
Ключевых слов = 20/024