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Cited by 8Genomics and Chromatin DynamicsNuclear Structure and FunctionProtein Structure and Dynamics

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CODANIN-1 sequesters ASF1 by using a histone H3 mimic helix to regulate the histone supply

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Jeong, Tae-Kyeong, Frater, R. Ciaran MacKenzie, Yoon, Jongha, Groth, Anja, Song, Ji-Joon·2025·Nature Communications
DOI 10.1038/s41467-025-56976-7PMC PMC11880193

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Abstract

ASF1 is a major histone chaperone that regulates the supply of histone H3–H4 and facilitates nucleosome assembly to maintain chromatin structure during DNA replication and transcription. CODANIN-1 negatively regulates the function of ASF1. However, the molecular mechanism by which CODANIN-1 inhibits the ASF1-mediated histone supply remains elusive. Here, we present the cryo-EM structure of a human CODANIN-1_ASF1A complex at 3.75 Å resolution. The structure reveals that CODANIN-1 forms a dimer where each monomer holds two ASF1 molecules, utilizing two B-domains and two histone H3 mimic helices (HMHs). The interaction of CODANIN-1 with ASF1 via the HMH and B-domains inhibits the formation of an ASF1/H3–H4 complex and sequesters ASF1 in the cytoplasm. Our study provides a structural and molecular basis for the function of CODANIN-1 as negative regulator that highjacks ASF1 interaction sites with histones and downstream chaperones to inhibit nucleosome assembly. CODANIN-1 negatively regulates the function of ASF1, the key chaperone for histone H3-H4 supply. Here the authors present the cryo-EM structure of the CODANIN-1_ASF1A complex, showing that CODANIN-1 utilizes histone H3-mimic helices and B-domains to sequester ASF1A, thereby inhibiting ASF1 function.

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Fig. 1 Cryo-EM structure of the CODANIN-1 complex. a Schematic diagram of the CODANIN-1 complex composed of CODANIN-1 full-length (1–1227), C-terminal-truncated ASF1A1-172 (1–172 a.a.) and full-length CDIN1 (1–281 a.a.). The dotted boxes indicate the disordered region in the cryo-EM map. b Gel filtration profile and SDS‒PAGE analysis of the CODANIN-1 complex. The gel filtration profile is representative of n = 4 biological replicates. c Representative cryo-EM micrograph of the CODANIN-1 complex on a graphene oxide-covered grid and 2D class averages. The micrograph is representative of total 4075 selected micrographs. d Cryo-EM map of the CODANIN-1 complex. Two CODANIN-1 molecules in a dimer are colored pale blue and pale purple, the bound proximal ASF1A is yellow and orange, and the distal ASF1A is magenta. e Schematic diagram of the structure of the CODANIN-1_ASF1A complex. f The atomic structure of the CODANIN-1_ASF1A complex is shown in a ribbon diagram.
Fig. 1 Cryo-EM structure of the CODANIN-1 complex. a Schematic diagram of the CODANIN-1 complex composed of CODANIN-1 full-length (1–1227), C-terminal-truncated ASF1A1-172 (1–172 a.a.) and full-length CDIN1 (1–281 a.a.). The dotted boxes indicate the disordered region in the cryo-EM map. b Gel filtration profile and SDS‒PAGE analysis of the CODANIN-1 complex. The gel filtration profile is representative of n = 4 biological replicates. c Representative cryo-EM micrograph of the CODANIN-1 complex on a graphene oxide-covered grid and 2D class averages. The micrograph is representative of total 4075 selected micrographs. d Cryo-EM map of the CODANIN-1 complex. Two CODANIN-1 molecules in a dimer are colored pale blue and pale purple, the bound proximal ASF1A is yellow and orange, and the distal ASF1A is magenta. e Schematic diagram of the structure of the CODANIN-1_ASF1A complex. f The atomic structure of the CODANIN-1_ASF1A complex is shown in a ribbon diagram.CC BY-NC-ND · PubMed Central
Fig. 2 CODANIN-1 has two ASF1A binding modules, each of which is composed of a B-domain (BD) and a histone mimic helix (HMH). a CODANIN-1 forms a dimer, and each molecule binds two ASF1A molecules: proximal ASF1A (proxASF1A) in yellow or orange and distal ASF1A (distASF1A) in magenta. proxASF1A is encapsulated by BD-C, the αH28 helix, a loop linking the αH13 and αH14 helices, and the αH16 helix (HMH-C). distASF1A is sandwiched by BD-N and the αH5 helix (HMH-N). b, c Detailed interactions between distASF1A and BD-N (193–202 a.a.) (b) and between proxASF1A and BD-C (820–833 a.a.) (c). D37 and D58 in distASF1A (b) and proxASF1A (c) form salt bridges with R196 and R195 in BD-N and K826 and R825 in BD-C, respectively. d, e, f Interaction modes of HMH-N with distASF1A (d), HMH-C with proxASF1A (e) and between histone H3 and the ASF1A complex (PDB 2IO5) (f). HMH-N and HMH-C occupy the histone H3 αH3-binding pockets of ASF1A. V94 in distASF1A and proxASF1A form hydrophobic interactions with HMH-N L254 and with HMH-C L545 and L549, respectively. D88 and D54 in distASF1A and proxASF1A form salt bridges with HMH-N R258 and R251 and with HMH-C R541 and R548, respectively. g Sequence comparison between the two CODANIN-1 HMHs (CDAN1_HMH-N and CDAN1_HMH-C) and histone H3 αH3. The residues that interact with ASF1A are marked with asterisks. HMH-N is aligned with HMH-C and histone H3 αH3 in the C-to-N direction.
Fig. 2 CODANIN-1 has two ASF1A binding modules, each of which is composed of a B-domain (BD) and a histone mimic helix (HMH). a CODANIN-1 forms a dimer, and each molecule binds two ASF1A molecules: proximal ASF1A (proxASF1A) in yellow or orange and distal ASF1A (distASF1A) in magenta. proxASF1A is encapsulated by BD-C, the αH28 helix, a loop linking the αH13 and αH14 helices, and the αH16 helix (HMH-C). distASF1A is sandwiched by BD-N and the αH5 helix (HMH-N). b, c Detailed interactions between distASF1A and BD-N (193–202 a.a.) (b) and between proxASF1A and BD-C (820–833 a.a.) (c). D37 and D58 in distASF1A (b) and proxASF1A (c) form salt bridges with R196 and R195 in BD-N and K826 and R825 in BD-C, respectively. d, e, f Interaction modes of HMH-N with distASF1A (d), HMH-C with proxASF1A (e) and between histone H3 and the ASF1A complex (PDB 2IO5) (f). HMH-N and HMH-C occupy the histone H3 αH3-binding pockets of ASF1A. V94 in distASF1A and proxASF1A form hydrophobic interactions with HMH-N L254 and with HMH-C L545 and L549, respectively. D88 and D54 in distASF1A and proxASF1A form salt bridges with HMH-N R258 and R251 and with HMH-C R541 and R548, respectively. g Sequence comparison between the two CODANIN-1 HMHs (CDAN1_HMH-N and CDAN1_HMH-C) and histone H3 αH3. The residues that interact with ASF1A are marked with asterisks. HMH-N is aligned with HMH-C and histone H3 αH3 in the C-to-N direction.CC BY-NC-ND · PubMed Central
Fig. 3 HMH and the B-domain of CODANIN-1 synergistically contribute to ASF1A binding. a GST pulldowns of ASF1A with the GST-BD-N (183–217 a.a.), GST-HMH-N (255–285 a.a.), GST-HMH-C (520–557 a.a.) and GST-BD-N (816–843 a.a.) domains. For the bar graph, each dot represents a biological replicate (n = 3), error bars represent the mean ± SD. P-values were calculated with one-way analysis of variance (ANOVA) with Dunnett’s multiple comparisons test against GST (BD-N: p < 0.0001, HMH-N: p = 0.9998, HMH-C: p = 0.0043, BD-C: p > 0.9999). b GST pulldowns of ASF1A with GST-HMH-C mutants (R541A, R548A or LL/AA) and GST-BD-N mutants (BD-Nmut-R195A/R196A). For the bar graph, each dot represents a biological replicate (n = 3), error bars represent the mean ± SD. P-values were calculated with one-way analysis of variance (ANOVA) with Dunnett’s multiple comparisons test (BD-Nmut: p < 0.0001 against BD-Nwt, LL/AA, R548A and R541A: p < 0.0001 against HMH-Cwt, BD-Nwt and HMH-Cwt: p < 0.0001 against GST). c Biolayer interferometry (BLI) measurement of ASF1A binding to full-length CODANIN-1 and the indicated mutants. ASF1A was immobilized on the surface of the chips, and CODANIN-1 was injected at 8, 16, 32, 64, 128, 256, and 512 nM concentrations. The dotted line indicates the time points at which the analytes (CODANIN-1) were removed. Schematic diagram of the mutants (top panel): Mut1 (BD-Nmut), Mut2 (HMH-Nmut), Mut3 (HMH-Cmut), Mut4 (BD-Cmut), Mut5 (BD-Nmut/HMH-Nmut), Mut6 (HMH-Cmut/BD-Cmut), Mut7 (BD-Nmut/HMH-Cmut), Mut8 (BD-Nmut/BD-Cmut) and Mut9 (HMH-Nmut/HMH-Cmut). ND ( < 10−7 or no binding). None of the mutants bound to the chip surface without ASF1A immobilization (nonspecific binding). d GST pulldowns of full-length CODANIN-1 using wild-type GST-ASF1A and the indicated mutants. ASF1A mutants on the HMH binding surface (D88A, D54A, V94R), the B-domain binding surface in ASF1A (ED/AA: E36A/D37A), and double mutants of both (D88A + ED/AA, D54A + ED/AA, V94R + ED/AA) were tested. For the bar graph, each dot represents a biological replicate (n = 3), error bars represent the mean ± SD. P-values were calculated with one-way analysis of variance (ANOVA) with Dunnett’s multiple comparisons test against WT (GST: p < 0.0001, D88A: p = 0.3572, D54A: p > 0.9999, V94R: p = 0.2566, ED/AA: p = 0.0209, D88A + ED/AA: p = 0.0087, D54A + ED/AA: p = 0.0002, V94R + ED/AA: p = 0.0001). For the all bar graphs, ns: not significant, *: p < 0.05, **: p < 0.01, ***: p < 0.001, ****: p < 0.0001. Source data are provided as a Source Data file.
Fig. 3 HMH and the B-domain of CODANIN-1 synergistically contribute to ASF1A binding. a GST pulldowns of ASF1A with the GST-BD-N (183–217 a.a.), GST-HMH-N (255–285 a.a.), GST-HMH-C (520–557 a.a.) and GST-BD-N (816–843 a.a.) domains. For the bar graph, each dot represents a biological replicate (n = 3), error bars represent the mean ± SD. P-values were calculated with one-way analysis of variance (ANOVA) with Dunnett’s multiple comparisons test against GST (BD-N: p < 0.0001, HMH-N: p = 0.9998, HMH-C: p = 0.0043, BD-C: p > 0.9999). b GST pulldowns of ASF1A with GST-HMH-C mutants (R541A, R548A or LL/AA) and GST-BD-N mutants (BD-Nmut-R195A/R196A). For the bar graph, each dot represents a biological replicate (n = 3), error bars represent the mean ± SD. P-values were calculated with one-way analysis of variance (ANOVA) with Dunnett’s multiple comparisons test (BD-Nmut: p < 0.0001 against BD-Nwt, LL/AA, R548A and R541A: p < 0.0001 against HMH-Cwt, BD-Nwt and HMH-Cwt: p < 0.0001 against GST). c Biolayer interferometry (BLI) measurement of ASF1A binding to full-length CODANIN-1 and the indicated mutants. ASF1A was immobilized on the surface of the chips, and CODANIN-1 was injected at 8, 16, 32, 64, 128, 256, and 512 nM concentrations. The dotted line indicates the time points at which the analytes (CODANIN-1) were removed. Schematic diagram of the mutants (top panel): Mut1 (BD-Nmut), Mut2 (HMH-Nmut), Mut3 (HMH-Cmut), Mut4 (BD-Cmut), Mut5 (BD-Nmut/HMH-Nmut), Mut6 (HMH-Cmut/BD-Cmut), Mut7 (BD-Nmut/HMH-Cmut), Mut8 (BD-Nmut/BD-Cmut) and Mut9 (HMH-Nmut/HMH-Cmut). ND ( < 10−7 or no binding). None of the mutants bound to the chip surface without ASF1A immobilization (nonspecific binding). d GST pulldowns of full-length CODANIN-1 using wild-type GST-ASF1A and the indicated mutants. ASF1A mutants on the HMH binding surface (D88A, D54A, V94R), the B-domain binding surface in ASF1A (ED/AA: E36A/D37A), and double mutants of both (D88A + ED/AA, D54A + ED/AA, V94R + ED/AA) were tested. For the bar graph, each dot represents a biological replicate (n = 3), error bars represent the mean ± SD. P-values were calculated with one-way analysis of variance (ANOVA) with Dunnett’s multiple comparisons test against WT (GST: p < 0.0001, D88A: p = 0.3572, D54A: p > 0.9999, V94R: p = 0.2566, ED/AA: p = 0.0209, D88A + ED/AA: p = 0.0087, D54A + ED/AA: p = 0.0002, V94R + ED/AA: p = 0.0001). For the all bar graphs, ns: not significant, *: p < 0.05, **: p < 0.01, ***: p < 0.001, ****: p < 0.0001. Source data are provided as a Source Data file.CC BY-NC-ND · PubMed Central
Fig. 4 CODANIN-1 sequesters free ASF1A to prevent complex formation with histone H3–H4. a GST-ASF1A pulldown experiment using CODANIN-1 and histone H3–H4 (left panel). The ratio of histone H3–H4 to CODANIN-1 is indicated above each gel lane. Quantification of histone H3–H4 relative to GST-ASF1A (right panel). The value was normalized to the histone H3–H4 band in the absence of CODANIN-1 (1:0 ratio). b Pulldown of CODANIN-1 with a preformed GST-ASF1A/H3–H4 complex (left panel). The ratio of histone H3–H4 to CODANIN-1 is indicated. Quantification of histone H3–H4 relative to GST-ASF1A (right panel). The value was normalized to the histone H3–H4 band in the absence of CODANIN-1 (1:0 ratio). c FLAG-pulldown experiments in which FLAG-tagged full-length CODANIN-1 wild type and mutants (BD-Nmut, BD-Cmut, and BD-N/Cmut) were used for ASF1A/H3–H4 binding. A representative SDS‒PAGE gel is shown in the left panel, and the quantification of the binding (n = 3) is shown in the bar graphs. Each dot represents a biological replicate (n = 3), and bars and error bars represent the mean ± SD. P-values were calculated by one-way analysis of variance (ANOVA) with Dunnett’s multiple comparisons test against ‘Bead’ control (ns: not significant, ****: p < 0.0001, WT: p < 0.0001, BD-Nmut: p = 0.4762, BD-Cmut: p < 0.0001, BD-N/Cmut: p > 0.9999). Source data are provided as a Source Data file.
Fig. 4 CODANIN-1 sequesters free ASF1A to prevent complex formation with histone H3–H4. a GST-ASF1A pulldown experiment using CODANIN-1 and histone H3–H4 (left panel). The ratio of histone H3–H4 to CODANIN-1 is indicated above each gel lane. Quantification of histone H3–H4 relative to GST-ASF1A (right panel). The value was normalized to the histone H3–H4 band in the absence of CODANIN-1 (1:0 ratio). b Pulldown of CODANIN-1 with a preformed GST-ASF1A/H3–H4 complex (left panel). The ratio of histone H3–H4 to CODANIN-1 is indicated. Quantification of histone H3–H4 relative to GST-ASF1A (right panel). The value was normalized to the histone H3–H4 band in the absence of CODANIN-1 (1:0 ratio). c FLAG-pulldown experiments in which FLAG-tagged full-length CODANIN-1 wild type and mutants (BD-Nmut, BD-Cmut, and BD-N/Cmut) were used for ASF1A/H3–H4 binding. A representative SDS‒PAGE gel is shown in the left panel, and the quantification of the binding (n = 3) is shown in the bar graphs. Each dot represents a biological replicate (n = 3), and bars and error bars represent the mean ± SD. P-values were calculated by one-way analysis of variance (ANOVA) with Dunnett’s multiple comparisons test against ‘Bead’ control (ns: not significant, ****: p < 0.0001, WT: p < 0.0001, BD-Nmut: p = 0.4762, BD-Cmut: p < 0.0001, BD-N/Cmut: p > 0.9999). Source data are provided as a Source Data file.CC BY-NC-ND · PubMed Central
Fig. 5 Dimerization of the CODANIN-1 complex. a Detailed view of the dimer interface of the CODANIN-1 complex. The dashed-line boxes (Boxes 1 and 2) indicate the dimerization interfaces of CODANIN-1 and the enlarged view of the CODANIN-1 dimerization interface. The F581 residue of each CODANIN-1 is inserted into a hydrophobic pocket formed by the F581, M588, V643, L646, and P647 residues from the other CODANIN-1 (Box 1). The R447 and E652 residues from the two different CODANIN-1 molecules form a salt bridge (Box 2). b Size-exclusion chromatograms and negative-stain EM micrograph images of wild-type CODANIN-1 and DMmut (left panel). Box and whisker plot with all points shows the 2-dimensional area of the particles (minimum whisker: minimum value, lower quartile: 25% percentile, center line: median, upper quartile: 75% percentile, maximum whisker: maximum value). The number of particles used in the analysis 1405 for WT and 1862 for DMmut (right panel). c, GST-pulldown experiment with GST-ASF1A and CODANIN-1 wild-type and DMmut (top panel). The bar graph represents the quantification of CODANIN-1 relative to GST-ASF1A normalized to wild-type CODANIN-1 (right panel). For the bar graphs, each dot represents a biological replicate (n = 3), and bars and error bars represent the mean ± SD. The statistical P-values were calculated with one-way analysis of variance (ANOVA) with Dunnett’s multiple comparisons test against GST-ASF1A bound WT. (ns: not significant, ** p < 0.01, ***: p < 0.001, GST bound WT: p = 0.0009, GST bound DMmut: p = 0.0003, GST-ASF1A bound DMmut: p = 0.4153). Source data are provided as a Source Data file.
Fig. 5 Dimerization of the CODANIN-1 complex. a Detailed view of the dimer interface of the CODANIN-1 complex. The dashed-line boxes (Boxes 1 and 2) indicate the dimerization interfaces of CODANIN-1 and the enlarged view of the CODANIN-1 dimerization interface. The F581 residue of each CODANIN-1 is inserted into a hydrophobic pocket formed by the F581, M588, V643, L646, and P647 residues from the other CODANIN-1 (Box 1). The R447 and E652 residues from the two different CODANIN-1 molecules form a salt bridge (Box 2). b Size-exclusion chromatograms and negative-stain EM micrograph images of wild-type CODANIN-1 and DMmut (left panel). Box and whisker plot with all points shows the 2-dimensional area of the particles (minimum whisker: minimum value, lower quartile: 25% percentile, center line: median, upper quartile: 75% percentile, maximum whisker: maximum value). The number of particles used in the analysis 1405 for WT and 1862 for DMmut (right panel). c, GST-pulldown experiment with GST-ASF1A and CODANIN-1 wild-type and DMmut (top panel). The bar graph represents the quantification of CODANIN-1 relative to GST-ASF1A normalized to wild-type CODANIN-1 (right panel). For the bar graphs, each dot represents a biological replicate (n = 3), and bars and error bars represent the mean ± SD. The statistical P-values were calculated with one-way analysis of variance (ANOVA) with Dunnett’s multiple comparisons test against GST-ASF1A bound WT. (ns: not significant, ** p < 0.01, ***: p < 0.001, GST bound WT: p = 0.0009, GST bound DMmut: p = 0.0003, GST-ASF1A bound DMmut: p = 0.4153). Source data are provided as a Source Data file.CC BY-NC-ND · PubMed Central
Fig. 6 One B-domain and one HMH are required for cytoplasmic sequestration of ASF1A is required for cytoplasmic sequestration by CODANIN-1. a Western blot of endogenous CODANIN-1 after 48 h of siRNA treatment with control siRNA (siCtrl) or siRNA targeting CDAN1 (siCDAN1 #1 and #2). b Western blot showing the expression of HA-tagged CODANIN-1 after 24 h of treatment with doxycycline and Shield1. WT: wild type, HMH and B-domain mutants, DMmut: dimerization mutant, Neg: no exogenous CODANIN-1. The Western blot is representative of n = 2 biological replicates. c Representative images of ASF1A localization in cell lines complemented with exogenous WT and mutant CODANIN-1 as indicated. The siCtrl and siCDAN1 #2 panels represent the parental cell lines with control or CDAN1 knockdown, respectively. Each cell line was treated with CDAN1#2 siRNA for 48 h, and doxycycline and Shield1 were added for the last 24 h to induce the expression of exogenous CODANIN-1. d Cytoplasmic ASF1A intensity quantified in individual cells from a single biological replicate as in c. For complementation with exogenous CODANIN-1, only HA-expressing cells were included. The bars repserent the median and interquartile range of each condition. e Relative change in cytoplasmic ASF1A intensity compared with that of the control. For each condition the difference in median cytoplasmic ASF1A intensity compared with the median of siCtrl was calculated (% change). Each dot represents a biological replicate (n = 4), and the bars and error bars represent the means±SDs. P-values were calculated by two-sided paired t-test against siCtrl (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, WT: p = 4.4 × 10-4, LL/AA: p = 5 × 10-4, L549R: p = 1.6 × 10-3, BD-Nmut: p = 4.8 × 10-5, P672L: p = 1.5 × 10-2, DMmut: p = 1.2 × 10-2). f, g Nuclear ASF1A intensity quantified in HA-expressing cells using the same methods as in d,e. A minimum of 2000 cells HA-expressing were considered per condition. Each dot represents a biological replicate (n = 4), and bars and error bars represent the mean±SD. P-values were calculated by two-sided paired t-test against siCtrl (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, siCDAN1 #1: p = 8.3 × 10-3, siCDAN1 #2: p = 1.5 × 10-3, BD-Nmut + LL/AA: p = 4 × 10-2, P672L: p = 8.1 × 10−3, DMmut: p = 1 × 10−2). Source data are provided as a Source Data file.
Fig. 6 One B-domain and one HMH are required for cytoplasmic sequestration of ASF1A is required for cytoplasmic sequestration by CODANIN-1. a Western blot of endogenous CODANIN-1 after 48 h of siRNA treatment with control siRNA (siCtrl) or siRNA targeting CDAN1 (siCDAN1 #1 and #2). b Western blot showing the expression of HA-tagged CODANIN-1 after 24 h of treatment with doxycycline and Shield1. WT: wild type, HMH and B-domain mutants, DMmut: dimerization mutant, Neg: no exogenous CODANIN-1. The Western blot is representative of n = 2 biological replicates. c Representative images of ASF1A localization in cell lines complemented with exogenous WT and mutant CODANIN-1 as indicated. The siCtrl and siCDAN1 #2 panels represent the parental cell lines with control or CDAN1 knockdown, respectively. Each cell line was treated with CDAN1#2 siRNA for 48 h, and doxycycline and Shield1 were added for the last 24 h to induce the expression of exogenous CODANIN-1. d Cytoplasmic ASF1A intensity quantified in individual cells from a single biological replicate as in c. For complementation with exogenous CODANIN-1, only HA-expressing cells were included. The bars repserent the median and interquartile range of each condition. e Relative change in cytoplasmic ASF1A intensity compared with that of the control. For each condition the difference in median cytoplasmic ASF1A intensity compared with the median of siCtrl was calculated (% change). Each dot represents a biological replicate (n = 4), and the bars and error bars represent the means±SDs. P-values were calculated by two-sided paired t-test against siCtrl (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, WT: p = 4.4 × 10-4, LL/AA: p = 5 × 10-4, L549R: p = 1.6 × 10-3, BD-Nmut: p = 4.8 × 10-5, P672L: p = 1.5 × 10-2, DMmut: p = 1.2 × 10-2). f, g Nuclear ASF1A intensity quantified in HA-expressing cells using the same methods as in d,e. A minimum of 2000 cells HA-expressing were considered per condition. Each dot represents a biological replicate (n = 4), and bars and error bars represent the mean±SD. P-values were calculated by two-sided paired t-test against siCtrl (* p < 0.05, ** p < 0.01, *** p < 0.001, **** p < 0.0001, siCDAN1 #1: p = 8.3 × 10-3, siCDAN1 #2: p = 1.5 × 10-3, BD-Nmut + LL/AA: p = 4 × 10-2, P672L: p = 8.1 × 10−3, DMmut: p = 1 × 10−2). Source data are provided as a Source Data file.CC BY-NC-ND · PubMed Central

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Metadata

Authors
Jeong, T.-K., Frater, R. C. M., Yoon, J., Groth, A., & Song, J.-J.
Affiliations
  • Korea Advanced Institute of Science and Technology (KR)
  • University of Copenhagen (DK)
Corresponding author
  • Groth, Anja
  • Song, Ji-Joon
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2025-03-04
Volume
16
Issue
1
Pages
2181-2181
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-025-56976-7
PMC
PMC11880193
OpenAlex
W4408149786
Cited by
8
References
3
Citations by year
2026: 4 · 2025: 2
FWCI
1.80
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by-nc-nd)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by-nc-nd)
  • PubMed (publishedVersion)
  • Research at the University of Copenhagen (University of Copenhagen) (publishedVersion, cc-by-nc-nd)
  • RePEc: Research Papers in Economics (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
  • National Research Foundation of Korea (RS-2023-00266300, RS-2024-00440614)
  • Novo Nordisk Fonden (NNF21OC0067425, NNF14CC0001)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
Asf1, histone chaperone, nucleosome assembly, negative regulation, protein complex structure, B domain, cytoplasmic sequestration, chromatin structure
MeSH terms
Histones, Humans, Models, Molecular, Nucleosomes, Protein Binding, Transcription Factors, Cell Cycle Proteins, Molecular Chaperones, Cryoelectron Microscopy, Protein Multimerization, Histone Chaperones

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