ArticleBMC cell biology2010
The methylated N-terminal tail of RCC1 is required for stabilisation of its interaction with chromatin by Ran in live cells.
Article in BMC cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- Characterizations of Protein Arginine Deiminase 1 as a Substrate of NTMT1: Implications of Nα-Methylation in Protein Stability and Interaction.Journal of proteome research · 2024Article
- Impact of Protein NLife (Basel, Switzerland) · 2023Review
- Site-specific methylation on α-N-terminus of peptides through chemical and enzymatic methods.Methods in enzymology · 2023Article
- Past, present, and perspectives of protein N-terminal methylation.Current opinion in chemical biology · 2021Review
- Selective Peptidomimetic Inhibitors of NTMT1/2: Rational Design, Synthesis, Characterization, and Crystallographic Studies.Journal of medicinal chemistry · 2020Article
- The Multifaceted Roles of RCC1 in Tumorigenesis.Frontiers in molecular biosciences · 2020Review
- Chemical Biology of Protein N-Terminal Methyltransferases.Chembiochem : a European journal of chemical biology · 2019Review
- Discovery of Bisubstrate Inhibitors for Protein N-Terminal Methyltransferase 1.Journal of medicinal chemistry · 2019Article
- Three-dimensional context rather than NLS amino acid sequence determines importin α subtype specificity for RCC1.Nature communications · 2017Article
- Revisiting chromatin binding of the Arabidopsis UV-B photoreceptor UVR8.BMC plant biology · 2016Article
- Chromatin binding of RCC1 during mitosis is important for its nuclear localization in interphase.Molecular biology of the cell · 2016Article
- Structural basis for substrate recognition by the human N-terminal methyltransferase 1.Genes & development · 2015Article
- Design, synthesis, and kinetic analysis of potent protein N-terminal methyltransferase 1 inhibitors.Organic & biomolecular chemistry · 2015Article
- Importin-β modulates the permeability of the nuclear pore complex in a Ran-dependent manner.eLife · 2015Article
- RanBP1 governs spindle assembly by defining mitotic Ran-GTP production.Developmental cell · 2014Article
- Chromosomal gain promotes formation of a steep RanGTP gradient that drives mitosis in aneuploid cells.The Journal of cell biology · 2013Article
- Advanced fluorescence microscopy techniques--FRAP, FLIP, FLAP, FRET and FLIM.Molecules (Basel, Switzerland) · 2012Review
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4 authors at 3 institutions in 1 country.
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Abstract
backgroundRegulator of chromosome condensation 1 (RCC1) is the guanine nucleotide exchange factor for Ran GTPase. Localised generation of Ran-GTP by RCC1 on chromatin is critical for nucleocytoplasmic transport, mitotic spindle assembly and nuclear envelope formation. Both the N-terminal tail of RCC1 and its association with Ran are important for its interaction with chromatin in cells. In vitro, the association of Ran with RCC1 induces a conformational change in the N-terminal tail that promotes its interaction with DNA.
resultsWe have investigated the mechanism of the dynamic interaction of the alpha isoform of human RCC1 (RCC1alpha) with chromatin in live cells using fluorescence recovery after photobleaching (FRAP) of green fluorescent protein (GFP) fusions. We show that the N-terminal tail stabilises the interaction of RCC1alpha with chromatin and this function can be partially replaced by another lysine-rich nuclear localisation signal. Removal of the tail prevents the interaction of RCC1alpha with chromatin from being stabilised by RanT24N, a mutant that binds stably to RCC1alpha. The interaction of RCC1alpha with chromatin is destabilised by mutation of lysine 4 (K4Q), which abolishes alpha-N-terminal methylation, and this interaction is no longer stabilised by RanT24N. However, alpha-N-terminal methylation of RCC1alpha is not regulated by the binding of RanT24N. Conversely, the association of Ran with precipitated RCC1alpha does not require the N-terminal tail of RCC1alpha or its methylation. The mobility of RCC1alpha on chromatin is increased by mutation of aspartate 182 (D182A), which inhibits guanine-nucleotide exchange activity, but RCC1alphaD182A can still bind nucleotide-free Ran and its interaction with chromatin is stabilised by RanT24N.
conclusionsThese results show that the stabilisation of the dynamic interaction of RCC1alpha with chromatin by Ran in live cells requires the N-terminal tail of RCC1alpha. alpha-N-methylation is not regulated by formation of the binary complex with Ran, but it promotes chromatin binding through the tail. This work supports a model in which the association of RCC1alpha with chromatin is promoted by a conformational change in the alpha-N-terminal methylated tail that is induced allosterically in the binary complex with Ran.
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