Imp7:ImpB:H1.0 / Importin / Histone H1 / nuclear import / disordered interactions / TRANSPORT PROTEIN
機能・相同性
機能・相同性情報
RNA import into nucleus / Inhibition of nitric oxide production / mitotic chromosome movement towards spindle pole / endoplasmic reticulum tubular network / importin-alpha family protein binding / positive regulation of transcription regulatory region DNA binding / astral microtubule organization / establishment of mitotic spindle localization / Transport of Ribonucleoproteins into the Host Nucleus / negative regulation of DNA recombination ...RNA import into nucleus / Inhibition of nitric oxide production / mitotic chromosome movement towards spindle pole / endoplasmic reticulum tubular network / importin-alpha family protein binding / positive regulation of transcription regulatory region DNA binding / astral microtubule organization / establishment of mitotic spindle localization / Transport of Ribonucleoproteins into the Host Nucleus / negative regulation of DNA recombination / Regulation of cholesterol biosynthesis by SREBP (SREBF) / NS1 Mediated Effects on Host Pathways / NLS-dependent protein nuclear import complex / NLS-bearing protein import into nucleus / Apoptosis induced DNA fragmentation / Initiation of Nuclear Envelope (NE) Reformation / nuclear localization sequence binding / ribosomal protein import into nucleus / Nuclear import of Rev protein / chromosome condensation / Postmitotic nuclear pore complex (NPC) reformation / nuclear import signal receptor activity / nucleosomal DNA binding / mitotic metaphase chromosome alignment / Formation of Senescence-Associated Heterochromatin Foci (SAHF) / minor groove of adenine-thymine-rich DNA binding / mitotic spindle assembly / nuclear pore / nucleosome binding / transcription repressor complex / Assembly of the ORC complex at the origin of replication / Hsp90 protein binding / positive regulation of cholesterol biosynthetic process / euchromatin / small GTPase binding / chromatin DNA binding / ISG15 antiviral mechanism / specific granule lumen / protein import into nucleus / cytoplasmic stress granule / SARS-CoV-1 activates/modulates innate immune responses / Interferon alpha/beta signaling / structural constituent of chromatin / nucleosome / nuclear envelope / heterochromatin formation / nucleosome assembly / actin cytoskeleton / double-stranded DNA binding / nuclear membrane / ficolin-1-rich granule lumen / nuclear body / protein domain specific binding / Neutrophil degranulation / chromatin / enzyme binding / Golgi apparatus / RNA binding / extracellular exosome / extracellular region / zinc ion binding / nucleoplasm / nucleus / membrane / cytosol / cytoplasm 類似検索 - 分子機能
ジャーナル: Mol Cell / 年: 2019 タイトル: Fuzzy Interactions Form and Shape the Histone Transport Complex. 著者: Nives Ivic / Mia Potocnjak / Victor Solis-Mezarino / Franz Herzog / Silvija Bilokapic / Mario Halic / 要旨: Protein transport into the nucleus is mediated by transport receptors. Import of highly charged proteins, such as histone H1 and ribosomal proteins, requires a dimer of two transport receptors. In ...Protein transport into the nucleus is mediated by transport receptors. Import of highly charged proteins, such as histone H1 and ribosomal proteins, requires a dimer of two transport receptors. In this study, we determined the cryo-EM structure of the Imp7:Impβ:H1.0 complex, showing that the two importins form a cradle that accommodates the linker histone. The H1.0 globular domain is bound to Impβ, whereas the acidic loops of Impβ and Imp7 chaperone the positively charged C-terminal tail. Although it remains disordered, the H1 tail serves as a zipper that closes and stabilizes the structure through transient non-specific interactions with importins. Moreover, we found that the GGxxF and FxFG motifs in the Imp7 C-terminal tail are essential for Imp7:Impβ dimerization and H1 import, resembling importin interaction with nucleoporins, which, in turn, promote complex disassembly. The architecture of many other complexes might be similarly defined by rapidly exchanging electrostatic interactions mediated by disordered regions.