DMA-tudor interaction modules control the specificity of in vivo condensates
Biomolecular condensation is a widespread mechanism of cellular compartmentalization. Because the “survival of motor neuron protein” (SMN) is implicated in the formation of three different membraneless organelles (MLOs), we hypothesized that SMN promotes condensation. Unexpectedly, we found that SMN...
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| Published in | Cell Vol. 184; no. 14; pp. 3612 - 3625.e17 |
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| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
Elsevier Inc
08.07.2021
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Biomolecular condensation is a widespread mechanism of cellular compartmentalization. Because the “survival of motor neuron protein” (SMN) is implicated in the formation of three different membraneless organelles (MLOs), we hypothesized that SMN promotes condensation. Unexpectedly, we found that SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo, whereas its two intrinsically disordered regions (IDRs) were not. Binding to dimethylarginine (DMA) modified protein ligands was required for condensate formation by the tudor domains in SMN and at least seven other fly and human proteins. Remarkably, asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs—gems and Cajal bodies—were separate or “docked” to one another. This substructure depended on the presence of either asymmetric or symmetric DMA as visualized with sub-diffraction microscopy. Thus, DMA-tudor interaction modules—combinations of tudor domains bound to their DMA ligand(s)—represent versatile yet specific regulators of MLO assembly, composition, and morphology.
[Display omitted]
•The tudor domain of SMN promotes condensation by binding dimethylarginine (DMA)•DMA-tudor condensation is a shared property of numerous other tudor domains•Each tudor domain has a specific dependence on symmetric or asymmetric DMA•aDMA and sDMA levels define the composition and substructure of Cajal bodies
The SMN tudor domain is sufficient for condensation by binding to dimethylarginine (DMA) modified protein ligands. Asymmetric versus symmetric DMA determines whether gems and Cajal bodies were separate or “docked” to one another. |
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| AbstractList | Biomolecular condensation is a widespread mechanism of cellular compartmentalization. Because the ‘survival of motor neuron protein’ (SMN) is implicated in the formation of three different membraneless organelles (MLOs), we hypothesized that SMN promotes condensation. Unexpectedly, we found that SMN’s globular tudor domain was sufficient for dimerization-induced condensation
in vivo
, while its two intrinsically disordered regions (IDRs) were not. Binding to dimethylarginine (DMA) modified protein ligands was required for condensate formation by the tudor domains in SMN and at least seven other fly and human proteins. Remarkably, asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs – gems and Cajal bodies – were separate or “docked” to one another. This substructure depended on the presence of either asymmetric or symmetric DMA as visualized with sub-diffraction microscopy. Thus, DMA-tudor interaction modules – combinations of tudor domains bound to their DMA ligand(s) – represent versatile yet specific regulators of MLO assembly, composition, and morphology.
The SMN tudor domain is sufficient for condensation by binding to dimethylarginine (DMA) modified protein ligands. Asymmetric versus symmetric DMA determines whether gems and Cajal bodies were separate or “docked” to one another. Biomolecular condensation is a widespread mechanism of cellular compartmentalization. Because the "survival of motor neuron protein" (SMN) is implicated in the formation of three different membraneless organelles (MLOs), we hypothesized that SMN promotes condensation. Unexpectedly, we found that SMN's globular tudor domain was sufficient for dimerization-induced condensation in vivo, whereas its two intrinsically disordered regions (IDRs) were not. Binding to dimethylarginine (DMA) modified protein ligands was required for condensate formation by the tudor domains in SMN and at least seven other fly and human proteins. Remarkably, asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs-gems and Cajal bodies-were separate or "docked" to one another. This substructure depended on the presence of either asymmetric or symmetric DMA as visualized with sub-diffraction microscopy. Thus, DMA-tudor interaction modules-combinations of tudor domains bound to their DMA ligand(s)-represent versatile yet specific regulators of MLO assembly, composition, and morphology.Biomolecular condensation is a widespread mechanism of cellular compartmentalization. Because the "survival of motor neuron protein" (SMN) is implicated in the formation of three different membraneless organelles (MLOs), we hypothesized that SMN promotes condensation. Unexpectedly, we found that SMN's globular tudor domain was sufficient for dimerization-induced condensation in vivo, whereas its two intrinsically disordered regions (IDRs) were not. Binding to dimethylarginine (DMA) modified protein ligands was required for condensate formation by the tudor domains in SMN and at least seven other fly and human proteins. Remarkably, asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs-gems and Cajal bodies-were separate or "docked" to one another. This substructure depended on the presence of either asymmetric or symmetric DMA as visualized with sub-diffraction microscopy. Thus, DMA-tudor interaction modules-combinations of tudor domains bound to their DMA ligand(s)-represent versatile yet specific regulators of MLO assembly, composition, and morphology. Biomolecular condensation is a widespread mechanism of cellular compartmentalization. Because the “survival of motor neuron protein” (SMN) is implicated in the formation of three different membraneless organelles (MLOs), we hypothesized that SMN promotes condensation. Unexpectedly, we found that SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo, whereas its two intrinsically disordered regions (IDRs) were not. Binding to dimethylarginine (DMA) modified protein ligands was required for condensate formation by the tudor domains in SMN and at least seven other fly and human proteins. Remarkably, asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs—gems and Cajal bodies—were separate or “docked” to one another. This substructure depended on the presence of either asymmetric or symmetric DMA as visualized with sub-diffraction microscopy. Thus, DMA-tudor interaction modules—combinations of tudor domains bound to their DMA ligand(s)—represent versatile yet specific regulators of MLO assembly, composition, and morphology. Biomolecular condensation is a widespread mechanism of cellular compartmentalization. Because the "survival of motor neuron protein" (SMN) is implicated in the formation of three different membraneless organelles (MLOs), we hypothesized that SMN promotes condensation. Unexpectedly, we found that SMN's globular tudor domain was sufficient for dimerization-induced condensation in vivo, whereas its two intrinsically disordered regions (IDRs) were not. Binding to dimethylarginine (DMA) modified protein ligands was required for condensate formation by the tudor domains in SMN and at least seven other fly and human proteins. Remarkably, asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs-gems and Cajal bodies-were separate or "docked" to one another. This substructure depended on the presence of either asymmetric or symmetric DMA as visualized with sub-diffraction microscopy. Thus, DMA-tudor interaction modules-combinations of tudor domains bound to their DMA ligand(s)-represent versatile yet specific regulators of MLO assembly, composition, and morphology. Biomolecular condensation is a widespread mechanism of cellular compartmentalization. Because the “survival of motor neuron protein” (SMN) is implicated in the formation of three different membraneless organelles (MLOs), we hypothesized that SMN promotes condensation. Unexpectedly, we found that SMN’s globular tudor domain was sufficient for dimerization-induced condensation in vivo, whereas its two intrinsically disordered regions (IDRs) were not. Binding to dimethylarginine (DMA) modified protein ligands was required for condensate formation by the tudor domains in SMN and at least seven other fly and human proteins. Remarkably, asymmetric versus symmetric DMA determined whether two distinct nuclear MLOs—gems and Cajal bodies—were separate or “docked” to one another. This substructure depended on the presence of either asymmetric or symmetric DMA as visualized with sub-diffraction microscopy. Thus, DMA-tudor interaction modules—combinations of tudor domains bound to their DMA ligand(s)—represent versatile yet specific regulators of MLO assembly, composition, and morphology. [Display omitted] •The tudor domain of SMN promotes condensation by binding dimethylarginine (DMA)•DMA-tudor condensation is a shared property of numerous other tudor domains•Each tudor domain has a specific dependence on symmetric or asymmetric DMA•aDMA and sDMA levels define the composition and substructure of Cajal bodies The SMN tudor domain is sufficient for condensation by binding to dimethylarginine (DMA) modified protein ligands. Asymmetric versus symmetric DMA determines whether gems and Cajal bodies were separate or “docked” to one another. |
| Author | Bewersdorf, Joerg Neugebauer, Karla M. Barentine, Andrew E.S. Courchaine, Edward M. Lee, Dong-Ryoung Straube, Korinna |
| AuthorAffiliation | 1 Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA 3 Biomedical Engineering, Yale University, New Haven, CT, 06520, USA 2 Cell Biology, Yale University, New Haven, CT, 06520, USA |
| AuthorAffiliation_xml | – name: 3 Biomedical Engineering, Yale University, New Haven, CT, 06520, USA – name: 2 Cell Biology, Yale University, New Haven, CT, 06520, USA – name: 1 Molecular Biophysics and Biochemistry, Yale University, New Haven, CT, 06520, USA |
| Author_xml | – sequence: 1 givenname: Edward M. surname: Courchaine fullname: Courchaine, Edward M. organization: Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA – sequence: 2 givenname: Andrew E.S. orcidid: 0000-0002-7673-9771 surname: Barentine fullname: Barentine, Andrew E.S. organization: Cell Biology, Yale University, New Haven, CT 06520, USA – sequence: 3 givenname: Korinna surname: Straube fullname: Straube, Korinna organization: Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA – sequence: 4 givenname: Dong-Ryoung orcidid: 0000-0002-3495-3390 surname: Lee fullname: Lee, Dong-Ryoung organization: Cell Biology, Yale University, New Haven, CT 06520, USA – sequence: 5 givenname: Joerg surname: Bewersdorf fullname: Bewersdorf, Joerg organization: Cell Biology, Yale University, New Haven, CT 06520, USA – sequence: 6 givenname: Karla M. surname: Neugebauer fullname: Neugebauer, Karla M. email: karla.neugebauer@yale.edu organization: Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520, USA |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/34115980$$D View this record in MEDLINE/PubMed |
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| Keywords | MLO biomolecular condensation membraneless organelle dimethylarginine tudor domains Cajal body nuclear gem DMA post-translational modification |
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| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 E.C. and K.M.N. designed the study. K.S. generated all constructs. E.C. prepared cell lines and performed experiments. E.C. and A.E.S.B. carried out image analysis. D.R.L. performed isoSTED data collection and image processing. J.B. and K.M.N. supervised the study. All authors contributed to writing the manuscript. Author contributions |
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| SubjectTerms | Animals Arginine - analogs & derivatives Arginine - metabolism Biomolecular Condensates - metabolism biomolecular condensation Cajal body Cell Nucleus - metabolism Coiled Bodies - metabolism condensates dimethylarginine DMA Drosophila melanogaster - metabolism HEK293 Cells HeLa Cells Humans Ligands membraneless organelle Methylation Mice microscopy MLO Models, Biological motor neurons NIH 3T3 Cells nuclear gem organelles post-translational modification Protein Binding Protein Domains Protein Multimerization Ribonucleoproteins, Small Nuclear - metabolism SMN Complex Proteins - chemistry SMN Complex Proteins - metabolism tudor domains |
| Title | DMA-tudor interaction modules control the specificity of in vivo condensates |
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