دورية أكاديمية
أعرض في EDS

Structure of Importin-α from a Filamentous Fungus in Complex with a Classical Nuclear Localization Signal.

التفاصيل البيبلوغرافية
العنوان: Structure of Importin-α from a Filamentous Fungus in Complex with a Classical Nuclear Localization Signal.
المؤلفون: Bernardes NE; Departamento de Física e Biofísica, Instituto de Biociências, Universidade Estadual Paulista, UNESP, Botucatu, SP, Brazil., Takeda AA; Departamento de Física e Biofísica, Instituto de Biociências, Universidade Estadual Paulista, UNESP, Botucatu, SP, Brazil., Dreyer TR; Departamento de Física e Biofísica, Instituto de Biociências, Universidade Estadual Paulista, UNESP, Botucatu, SP, Brazil., Freitas FZ; Departamento de Bioquímica e Tecnologia Química, Instituto de Química, Universidade Estadual Paulista, UNESP, Araraquara, SP, Brazil., Bertolini MC; Departamento de Bioquímica e Tecnologia Química, Instituto de Química, Universidade Estadual Paulista, UNESP, Araraquara, SP, Brazil., Fontes MR; Departamento de Física e Biofísica, Instituto de Biociências, Universidade Estadual Paulista, UNESP, Botucatu, SP, Brazil.
المصدر: PloS one [PLoS One] 2015 Jun 19; Vol. 10 (6), pp. e0128687. Date of Electronic Publication: 2015 Jun 19 (Print Publication: 2015).
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Public Library of Science Country of Publication: United States NLM ID: 101285081 Publication Model: eCollection Cited Medium: Internet ISSN: 1932-6203 (Electronic) Linking ISSN: 19326203 NLM ISO Abbreviation: PLoS One Subsets: MEDLINE
أسماء مطبوعة: Original Publication: San Francisco, CA : Public Library of Science
مواضيع طبية MeSH: Nuclear Localization Signals*/chemistry , Nuclear Localization Signals*/genetics, Neurospora crassa/*metabolism , alpha Karyopherins/*metabolism, Amino Acid Sequence ; Binding Sites ; Models, Molecular ; Neurospora crassa/genetics ; Protein Binding ; Protein Conformation ; alpha Karyopherins/chemistry ; alpha Karyopherins/genetics
مستخلص: Neurospora crassa is a filamentous fungus that has been extensively studied as a model organism for eukaryotic biology, providing fundamental insights into cellular processes such as cell signaling, growth and differentiation. To advance in the study of this multicellular organism, an understanding of the specific mechanisms for protein transport into the cell nucleus is essential. Importin-α (Imp-α) is the receptor for cargo proteins that contain specific nuclear localization signals (NLSs) that play a key role in the classical nuclear import pathway. Structures of Imp-α from different organisms (yeast, rice, mouse, and human) have been determined, revealing that this receptor possesses a conserved structural scaffold. However, recent studies have demonstrated that the Impα mechanism of action may vary significantly for different organisms or for different isoforms from the same organism. Therefore, structural, functional, and biophysical characterization of different Impα proteins is necessary to understand the selectivity of nuclear transport. Here, we determined the first crystal structure of an Impα from a filamentous fungus which is also the highest resolution Impα structure already solved to date (1.75 Å). In addition, we performed calorimetric analysis to determine the affinity and thermodynamic parameters of the interaction between Imp-α and the classical SV40 NLS peptide. The comparison of these data with previous studies on Impα proteins led us to demonstrate that N. crassa Imp-α possess specific features that are distinct from mammalian Imp-α but exhibit important similarities to rice Imp-α, particularly at the minor NLS binding site.
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المشرفين على المادة: 0 (Nuclear Localization Signals)
0 (alpha Karyopherins)
تواريخ الأحداث: Date Created: 20150620 Date Completed: 20160413 Latest Revision: 20230106
رمز التحديث: 20231215
مُعرف محوري في PubMed: PMC4474859
DOI: 10.1371/journal.pone.0128687
PMID: 26091498
قاعدة البيانات: MEDLINE
الوصف
تدمد:1932-6203
DOI:10.1371/journal.pone.0128687