TY - JOUR

T1 - Von-Hippel Lindau protein amyloid formation. The role of GST-tag

T2 - Von-Hippel Lindau protein amyloid formation. The role of GST-tag

AU - Кузьмина, Н. В.

AU - Гаврилова, А. А.

AU - Фефилова, А. С.

AU - Романович, Анна Эдуардовна

AU - Кузнецова, И. М.

AU - Туроверов, Константин

AU - Фонин, А В

N1 - Von-Hippel Lindau protein amyloid formation. The role of GST-tag / Kuzmina N. V., Gavrilova A. A., Fefilova A.S. [et. all] // Biochem Biophys Res Commun. –2024.– V. 715. – 715:150008. doi: 10.1016/j.bbrc.2024.150008. Epub 2024 Apr 25. PMID: 38685186.

PY - 2024/6/1

Y1 - 2024/6/1

N2 - n the last decade, much attention was given to the study of physiological amyloid fibrils. These structures include A-bodies, which are the nucleolar fibrillar formations that appear in the response to acidosis and heat shock, and disassemble after the end of stress. One of the proteins involved in the biogenesis of A-bodies, regardless of the type of stress, is Von-Hippel Lindau protein (VHL). Known also as a tumor suppressor, VHL is capable to form amyloid fibrils both in vitro and in vivo in response to the environment acidification. As with most amyloidogenic proteins fusion with various tags is used to increase the solubility of VHL. Here, we first performed AFM-study of fibrils formed by VHL protein and by VHL fused with GST-tag (GST-VHL) at acidic conditions. It was shown that formed by full-length VHL fibrils are short heterogenic structures with persistent length of 2400 nm and average contour length of 409 nm. GST-tag catalyzes VHL amyloid fibril formation, superimpose chirality, increases length and level of hierarchy, but decreases rigidity of amyloid fibrils. The obtained data indicate that tagging can significantly affect the fibrillogenesis of the target protein.

AB - n the last decade, much attention was given to the study of physiological amyloid fibrils. These structures include A-bodies, which are the nucleolar fibrillar formations that appear in the response to acidosis and heat shock, and disassemble after the end of stress. One of the proteins involved in the biogenesis of A-bodies, regardless of the type of stress, is Von-Hippel Lindau protein (VHL). Known also as a tumor suppressor, VHL is capable to form amyloid fibrils both in vitro and in vivo in response to the environment acidification. As with most amyloidogenic proteins fusion with various tags is used to increase the solubility of VHL. Here, we first performed AFM-study of fibrils formed by VHL protein and by VHL fused with GST-tag (GST-VHL) at acidic conditions. It was shown that formed by full-length VHL fibrils are short heterogenic structures with persistent length of 2400 nm and average contour length of 409 nm. GST-tag catalyzes VHL amyloid fibril formation, superimpose chirality, increases length and level of hierarchy, but decreases rigidity of amyloid fibrils. The obtained data indicate that tagging can significantly affect the fibrillogenesis of the target protein.

KW - amyloid fibrils, physiological amyloids, membrane-less organelles; A-bodies; intrinsically disordered proteins; protein aggregation

KW - A-bodies

KW - Amyloid fibrils

KW - Intrinsically disordered proteins

KW - Membrane-less organelles

KW - Physiological amyloids

KW - Protein aggregation

UR - https://www.mendeley.com/catalogue/333a648a-666f-331b-b3fd-05c8ae13cf2f/

U2 - 10.1016/j.bbrc.2024.150008

DO - 10.1016/j.bbrc.2024.150008

M3 - Article

VL - 715

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

M1 - 150008

ER -