Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains.

YB-1, a multifunctional DNA- and RNA-binding nucleocytoplasmic protein, is involved in the majority of DNA- and mRNA-dependent events in the cell. It consists of three structurally different domains: its central cold shock domain has the structure of a β-barrel, while the flanking domains are predic...

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Autores principales:	Sergey G Guryanov, Olga M Selivanova, Alexey D Nikulin, Gennady A Enin, Bogdan S Melnik, Dmitry A Kretov, Igor N Serdyuk, Lev P Ovchinnikov
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2012
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/57a51c42e35f492e81d22ee014454dd1
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spelling	oai:doaj.org-article:57a51c42e35f492e81d22ee014454dd12021-11-18T07:19:23ZFormation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains.1932-620310.1371/journal.pone.0036969https://doaj.org/article/57a51c42e35f492e81d22ee014454dd12012-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22590640/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203YB-1, a multifunctional DNA- and RNA-binding nucleocytoplasmic protein, is involved in the majority of DNA- and mRNA-dependent events in the cell. It consists of three structurally different domains: its central cold shock domain has the structure of a β-barrel, while the flanking domains are predicted to be intrinsically disordered. Recently, we showed that YB-1 is capable of forming elongated fibrils under high ionic strength conditions. Here we report that it is the cold shock domain that is responsible for formation of YB-1 fibrils, while the terminal domains differentially modulate this process depending on salt conditions. We demonstrate that YB-1 fibrils have amyloid-like features, including affinity for specific dyes and a typical X-ray diffraction pattern, and that in contrast to most of amyloids, they disassemble under nearly physiological conditions.Sergey G GuryanovOlga M SelivanovaAlexey D NikulinGennady A EninBogdan S MelnikDmitry A KretovIgor N SerdyukLev P OvchinnikovPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 7, Iss 5, p e36969 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Sergey G Guryanov Olga M Selivanova Alexey D Nikulin Gennady A Enin Bogdan S Melnik Dmitry A Kretov Igor N Serdyuk Lev P Ovchinnikov Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains.
description	YB-1, a multifunctional DNA- and RNA-binding nucleocytoplasmic protein, is involved in the majority of DNA- and mRNA-dependent events in the cell. It consists of three structurally different domains: its central cold shock domain has the structure of a β-barrel, while the flanking domains are predicted to be intrinsically disordered. Recently, we showed that YB-1 is capable of forming elongated fibrils under high ionic strength conditions. Here we report that it is the cold shock domain that is responsible for formation of YB-1 fibrils, while the terminal domains differentially modulate this process depending on salt conditions. We demonstrate that YB-1 fibrils have amyloid-like features, including affinity for specific dyes and a typical X-ray diffraction pattern, and that in contrast to most of amyloids, they disassemble under nearly physiological conditions.
format	article
author	Sergey G Guryanov Olga M Selivanova Alexey D Nikulin Gennady A Enin Bogdan S Melnik Dmitry A Kretov Igor N Serdyuk Lev P Ovchinnikov
author_facet	Sergey G Guryanov Olga M Selivanova Alexey D Nikulin Gennady A Enin Bogdan S Melnik Dmitry A Kretov Igor N Serdyuk Lev P Ovchinnikov
author_sort	Sergey G Guryanov
title	Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains.
title_short	Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains.
title_full	Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains.
title_fullStr	Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains.
title_full_unstemmed	Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains.
title_sort	formation of amyloid-like fibrils by y-box binding protein 1 (yb-1) is mediated by its cold shock domain and modulated by disordered terminal domains.
publisher	Public Library of Science (PLoS)
publishDate	2012
url	https://doaj.org/article/57a51c42e35f492e81d22ee014454dd1
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Formation of amyloid-like fibrils by Y-box binding protein 1 (YB-1) is mediated by its cold shock domain and modulated by disordered terminal domains.

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