[{"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","oa_version":"Published Version","year":"2025","date_updated":"2025-12-29T14:52:17Z","has_accepted_license":"1","project":[{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery"}],"date_published":"2025-12-01T00:00:00Z","day":"01","publisher":"Elsevier","type":"journal_article","issue":"23","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"status":"public","doi":"10.1016/j.jmb.2025.169379","OA_place":"publisher","article_type":"original","OA_type":"hybrid","ddc":["540"],"citation":{"ista":"Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. 2025. Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. Journal of Molecular Biology. 437(23), 169379.","chicago":"Rohden, Darja, Federico Napoli, Anna Kapitonova, Benjamin Tatman, Roman J. Lichtenecker, and Paul Schanda. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” <i>Journal of Molecular Biology</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">https://doi.org/10.1016/j.jmb.2025.169379</a>.","apa":"Rohden, D., Napoli, F., Kapitonova, A., Tatman, B., Lichtenecker, R. J., &#38; Schanda, P. (2025). Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">https://doi.org/10.1016/j.jmb.2025.169379</a>","ama":"Rohden D, Napoli F, Kapitonova A, Tatman B, Lichtenecker RJ, Schanda P. Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme. <i>Journal of Molecular Biology</i>. 2025;437(23). doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">10.1016/j.jmb.2025.169379</a>","ieee":"D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R. J. Lichtenecker, and P. Schanda, “Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme,” <i>Journal of Molecular Biology</i>, vol. 437, no. 23. Elsevier, 2025.","mla":"Rohden, Darja, et al. “Arginine Dynamics Probed by Magic-Angle Spinning NMR with a Specific Isotope-Labeling Scheme.” <i>Journal of Molecular Biology</i>, vol. 437, no. 23, 169379, Elsevier, 2025, doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169379\">10.1016/j.jmb.2025.169379</a>.","short":"D. Rohden, F. Napoli, A. Kapitonova, B. Tatman, R.J. Lichtenecker, P. Schanda, Journal of Molecular Biology 437 (2025)."},"related_material":{"record":[{"status":"public","relation":"research_data","id":"19956"}]},"PlanS_conform":"1","article_processing_charge":"Yes (via OA deal)","title":"Arginine dynamics probed by magic-angle spinning NMR with a specific isotope-labeling scheme","month":"12","_id":"20258","isi":1,"intvolume":"       437","author":[{"first_name":"Darja","id":"81dc668a-19fa-11f0-bf31-d56534059ef3","last_name":"Rohden","full_name":"Rohden, Darja"},{"orcid":"0000-0002-9043-136X","full_name":"Napoli, Federico","last_name":"Napoli","first_name":"Federico","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b"},{"last_name":"Kapitonova","full_name":"Kapitonova, Anna","first_name":"Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471"},{"first_name":"Benjamin","id":"71cda2f3-e604-11ee-a1df-da10587eda3f","last_name":"Tatman","full_name":"Tatman, Benjamin"},{"first_name":"Roman J.","full_name":"Lichtenecker, Roman J.","last_name":"Lichtenecker"},{"orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","last_name":"Schanda","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"file_date_updated":"2025-12-29T14:51:40Z","scopus_import":"1","publication":"Journal of Molecular Biology","publication_identifier":{"eissn":["1089-8638"],"issn":["0022-2836"]},"oa":1,"acknowledgement":"This work was supported financially by the Austrian Science Fund (FWF, Grant No. I5812-B, “AlloSpace”). This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support Facility (LSF). We thank Petra Rovò and Margarita Valhondo Falcón for excellent support of the NMR facility.","file":[{"success":1,"access_level":"open_access","relation":"main_file","file_size":2270555,"creator":"dernst","file_name":"2025_JourMolecularBiology_Rohden.pdf","file_id":"20876","date_created":"2025-12-29T14:51:40Z","date_updated":"2025-12-29T14:51:40Z","checksum":"90d50594d8ea9860ac5da41297992847","content_type":"application/pdf"}],"language":[{"iso":"eng"}],"corr_author":"1","department":[{"_id":"PaSc"}],"external_id":{"isi":["001618289100020"]},"date_created":"2025-08-31T22:01:33Z","publication_status":"published","acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"abstract":[{"lang":"eng","text":"The specific introduction of ^1H-^13C or ^1H-^15N moieties into otherwise deuterated proteins holds great potential for high-resolution solution and magic-angle spinning (MAS) NMR studies of protein structure and dynamics. Arginine residues play key roles for example at active sites of enzymes. Taking advantage of a chemically synthesized Arg with a ^13C-^1H2 group in an otherwise deuterated backbone, we demonstrate here the usefulness of proton-detected MAS NMR approaches to probe arginine dynamics. In experiments with crystalline ubiquitin and the 134 kDa tetrameric enzyme malate dehydrogenase we detected a wide range of motions, from sites that are rigid on time scales of at least tens of milliseconds to residues undergoing predominantly nanosecond motions. Spin-relaxation and dipolar-coupling measurements enabled quantitative determination of these dynamics. We observed microsecond dynamics of residue Arg54 in crystalline ubiquitin, whose backbone is known to sample different β-turn conformations on this time scale. The labeling scheme and experiments presented here expand the toolkit for high-resolution proton-detected MAS NMR."}],"article_number":"169379","quality_controlled":"1","volume":437},{"file_date_updated":"2025-12-30T10:29:08Z","publication":"Journal of Molecular Biology","author":[{"last_name":"Knödlstorfer","full_name":"Knödlstorfer, Sonja","first_name":"Sonja"},{"id":"334a5e40-8747-11f0-b671-ba1f5154b4b4","first_name":"Giorgia","last_name":"Toscano","full_name":"Toscano, Giorgia"},{"first_name":"Aleksandra L.","last_name":"Ptaszek","full_name":"Ptaszek, Aleksandra L."},{"full_name":"Kontaxis, Georg","last_name":"Kontaxis","first_name":"Georg"},{"last_name":"Napoli","full_name":"Napoli, Federico","id":"d42e08e7-f4fc-11eb-af0a-d71e26138f1b","first_name":"Federico","orcid":"0000-0002-9043-136X"},{"full_name":"Schneider, Jakob","last_name":"Schneider","id":"64368429-eb97-11eb-a6c2-c980b1f44415","first_name":"Jakob"},{"first_name":"Katharina","last_name":"Maier","full_name":"Maier, Katharina"},{"full_name":"Kapitonova, Anna","last_name":"Kapitonova","first_name":"Anna","id":"9fb2a840-89e1-11ee-a8b7-cc5c7ba62471"},{"first_name":"Roman J.","full_name":"Lichtenecker, Roman J.","last_name":"Lichtenecker"},{"orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul"},{"full_name":"Konrat, Robert","last_name":"Konrat","first_name":"Robert"}],"scopus_import":"1","intvolume":"       437","pmid":1,"file":[{"checksum":"feb92f9c79032c261165f4ca573f444a","content_type":"application/pdf","date_updated":"2025-12-30T10:29:08Z","file_id":"20915","date_created":"2025-12-30T10:29:08Z","file_name":"2025_JourMolecularBiology_Knoedlstorfer.pdf","creator":"dernst","file_size":3076611,"relation":"main_file","access_level":"open_access","success":1}],"acknowledgement":"A.L.P and G.T were funded by the “New Ideas” program by Vienna Doctoral School in Chemistry. S.K. was funded by the Austrian Science Fund FWF P35098-B. This work was supported financially by the Austrian Science Fund (FWF, grant numbers I06223 and I5812-B, “AlloSpace”). This research was supported by the Scientific Service Units (SSU) of Institute of Science and Technology Austria (ISTA) through resources provided by the Nuclear Magnetic Resonance Facility and the Lab Support Facility (LSF). We thank Celina Sailer for assistance with the analysis of the NMR spectrum of HsTom70.","oa":1,"publication_identifier":{"eissn":["1089-8638"],"issn":["0022-2836"]},"date_created":"2025-10-26T23:01:35Z","department":[{"_id":"PaSc"},{"_id":"GradSch"}],"external_id":{"pmid":["41016549"]},"language":[{"iso":"eng"}],"publication_status":"published","article_number":"169465","abstract":[{"text":"In this study, we describe an integrated approach for methyl group assignment comprising precursor-based selective methyl group labeling, a novel pulse sequence for methyl to backbone coherence transfer and chemical shift predictions using UCBShift 2.0. The utility of this novel α-ketoacid isotopologue is shown by the adaptation of an HMBC-HMQC pulse sequence that simultaneously connects geminal methyl groups of leucine and valine residues to each other and to the protein backbone. By additional 13C,2H-labeling of residues other than valine and leucine residues of the protein, important chemical shift information about neighboring residues (following valine and leucine residues) can be achieved. Thus, different valine and leucine residues in a protein can be characterized as a specific chemical shift vector. Frequency matching with predicted chemical shifts via UCBShift 2.0 using experimental data taken from a subset of the BMRB database revealed a correct assignment performance of about 90%. With applications to proteins of 60.2 kDa and 134 kDa (4 × 33.5 kDa) in size, we demonstrate that the approach provides valuable information even for very large proteins.","lang":"eng"}],"acknowledged_ssus":[{"_id":"NMR"},{"_id":"LifeSc"}],"volume":437,"quality_controlled":"1","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","has_accepted_license":"1","date_published":"2025-12-01T00:00:00Z","project":[{"_id":"bdb9578d-d553-11ed-ba76-ed5d39fce6f0","grant_number":"I06223","name":"Structure and mechanism of the mitochondrial MIM insertase"},{"_id":"eb9c82eb-77a9-11ec-83b8-aadd536561cf","grant_number":"I05812","name":"AlloSpace. The emergence and mechanisms of allostery"}],"date_updated":"2025-12-30T10:29:20Z","year":"2025","oa_version":"Published Version","issue":"23","publisher":"Elsevier","day":"01","type":"journal_article","status":"public","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"article_type":"original","OA_type":"hybrid","OA_place":"publisher","doi":"10.1016/j.jmb.2025.169465","ddc":["540"],"article_processing_charge":"Yes (in subscription journal)","PlanS_conform":"1","citation":{"ista":"Knödlstorfer S, Toscano G, Ptaszek AL, Kontaxis G, Napoli F, Schneider J, Maier K, Kapitonova A, Lichtenecker RJ, Schanda P, Konrat R. 2025. A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. Journal of Molecular Biology. 437(23), 169465.","chicago":"Knödlstorfer, Sonja, Giorgia Toscano, Aleksandra L. Ptaszek, Georg Kontaxis, Federico Napoli, Jakob Schneider, Katharina Maier, et al. “A Novel HMBC-CC-HMQC NMR Strategy for Methyl Assignment Using Triple-13C-Labeled α-Ketoisovalerate Integrated with UCBShift 2.0.” <i>Journal of Molecular Biology</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">https://doi.org/10.1016/j.jmb.2025.169465</a>.","apa":"Knödlstorfer, S., Toscano, G., Ptaszek, A. L., Kontaxis, G., Napoli, F., Schneider, J., … Konrat, R. (2025). A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">https://doi.org/10.1016/j.jmb.2025.169465</a>","ama":"Knödlstorfer S, Toscano G, Ptaszek AL, et al. A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0. <i>Journal of Molecular Biology</i>. 2025;437(23). doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">10.1016/j.jmb.2025.169465</a>","ieee":"S. Knödlstorfer <i>et al.</i>, “A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0,” <i>Journal of Molecular Biology</i>, vol. 437, no. 23. Elsevier, 2025.","short":"S. Knödlstorfer, G. Toscano, A.L. Ptaszek, G. Kontaxis, F. Napoli, J. Schneider, K. Maier, A. Kapitonova, R.J. Lichtenecker, P. Schanda, R. Konrat, Journal of Molecular Biology 437 (2025).","mla":"Knödlstorfer, Sonja, et al. “A Novel HMBC-CC-HMQC NMR Strategy for Methyl Assignment Using Triple-13C-Labeled α-Ketoisovalerate Integrated with UCBShift 2.0.” <i>Journal of Molecular Biology</i>, vol. 437, no. 23, 169465, Elsevier, 2025, doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169465\">10.1016/j.jmb.2025.169465</a>."},"_id":"20538","month":"12","title":"A novel HMBC-CC-HMQC NMR strategy for methyl assignment using triple-13C-labeled α-ketoisovalerate integrated with UCBShift 2.0"},{"publication":"Journal of Molecular Biology","file_date_updated":"2025-12-30T08:18:07Z","scopus_import":"1","author":[{"first_name":"James","full_name":"Antoney, James","last_name":"Antoney"},{"orcid":"0000-0002-6709-2195","first_name":"Stephanie","id":"32CFBA64-F248-11E8-B48F-1D18A9856A87","full_name":"Kainrath, Stephanie","last_name":"Kainrath"},{"last_name":"Dubowsky","full_name":"Dubowsky, Joshua G.","first_name":"Joshua G."},{"full_name":"Ahmed, F. Hafna","last_name":"Ahmed","first_name":"F. Hafna"},{"full_name":"Kang, Suk Woo","last_name":"Kang","first_name":"Suk Woo"},{"last_name":"Mackie","full_name":"Mackie, Emily R.R.","first_name":"Emily R.R."},{"last_name":"Bracho Granado","full_name":"Bracho Granado, Gustavo","first_name":"Gustavo"},{"first_name":"Tatiana P.","full_name":"Soares Da Costa, Tatiana P.","last_name":"Soares Da Costa"},{"full_name":"Jackson, Colin J.","last_name":"Jackson","first_name":"Colin J."},{"first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","full_name":"Janovjak, Harald L","last_name":"Janovjak","orcid":"0000-0002-8023-9315"}],"isi":1,"intvolume":"       437","file":[{"checksum":"fb6e84ba7dc92faee97647fd2bc8cca8","content_type":"application/pdf","date_updated":"2025-12-30T08:18:07Z","creator":"dernst","file_name":"2025_JourMolecularBiology_Antoney.pdf","date_created":"2025-12-30T08:18:07Z","file_id":"20892","file_size":1682721,"access_level":"open_access","relation":"main_file","success":1}],"acknowledgement":"We thank J. Kaczmarski for advice on isothermal titration calorimetry and helpful comments, and Alexandra Tichy, Elliot Gerrard and Rahkesh T Sabapathy for assistance with experiments. This study was supported by grants of the Australian Research Council (FT200100519 and DP200102093, to H.J.; DE190100806, DP220101901, FT230100203, and DP250102939 to T.P.S.D.C; DP200102093, CE200100029 and CE200100012 to C.J.J.), the National Health and Medical Research Council (APP1187638, to H.J.). S.K. was supported by the graduate program MolecularDrugTargets (Austrian Science Fund FWF W1232). The Australian Regenerative Medicine Institute is supported by grants from the State Government of Victoria and the Australian Government. The EMBL Australia Partnership Laboratory (EMBL Australia) is supported by the National Collaborative Research Infrastructure Strategy (NCRIS) of the Australian Government. T.P.S.D.C. acknowledges the University of Adelaide for a Future Making Fellowship. E.R.R.M acknowledges the Grains Research and Development Corporation (9176977) for support through a PhD scholarship and operational funding. J.A. and E.R.R.M. were supported by Australian Research Training Program scholarship. MicroMon of Monash University provided Sanger sequencing services. Imaging was performed in the CellScreen SA screening center of Flinders University. C.J.J. thanks the ARC Centre of Excellence for Innovations in Peptide and Protein Science and the ARC Centre of Excellence in Synthetic Biology. We thank the staff of the MX2 beamline at the Australian Synchrotron, part of ANSTO, which made use of the Australian Cancer Research Foundation (ACRF) detector.","pmid":1,"oa":1,"publication_identifier":{"issn":["0022-2836"],"eissn":["1089-8638"]},"publication_status":"published","department":[{"_id":"CaGu"}],"external_id":{"isi":["001494762800001"],"pmid":["40324743"]},"date_created":"2025-05-25T22:16:39Z","language":[{"iso":"eng"}],"volume":437,"quality_controlled":"1","abstract":[{"lang":"eng","text":"Protein-protein interactions (PPIs) mediate many fundamental cellular processes. Control of PPIs through optically or chemically responsive protein domains has had a profound impact on basic research and some clinical applications. Most chemogenetic methods induce the association, i.e., dimerization or oligomerization, of target proteins, whilst the few available dissociation approaches either break large oligomeric protein clusters or heteromeric complexes. Here, we have exploited the controlled dissociation of a homodimeric oxidoreductase from mycobacteria (MSMEG_2027) by its native cofactor, F420, which is not present in mammals, as a bioorthogonal monomerization switch. Using X-ray crystallography, we found that in the absence of F420 MSMEG_2027 forms a unique domain-swapped dimer that occludes the cofactor binding site. Rearrangement of the N-terminal helix upon F420 binding results in the dissolution of the dimer. We then showed that MSMEG_2027 can be fused to proteins of interest in human cells and applied it as a tool to induce and release MAPK/ERK signalling downstream of a chimeric fibroblast growth factor receptor 1 (FGFR1) tyrosine kinase. This F420-dependent chemogenetic de-homodimerization tool is stoichiometric and based on a single domain and thus represents a novel mechanism to investigate protein complexes in situ."}],"article_number":"169184","has_accepted_license":"1","project":[{"_id":"255A6082-B435-11E9-9278-68D0E5697425","grant_number":"W1232-B24","call_identifier":"FWF","name":"Molecular Drug Targets"}],"date_published":"2025-09-01T00:00:00Z","oa_version":"Published Version","year":"2025","date_updated":"2025-12-30T08:18:25Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","status":"public","tmp":{"short":"CC BY (4.0)","legal_code_url":"https://creativecommons.org/licenses/by/4.0/legalcode","image":"/images/cc_by.png","name":"Creative Commons Attribution 4.0 International Public License (CC-BY 4.0)"},"publisher":"Elsevier","type":"journal_article","day":"01","issue":"17","ddc":["570"],"OA_place":"publisher","doi":"10.1016/j.jmb.2025.169184","OA_type":"hybrid","article_type":"original","_id":"19725","title":"A F420-dependent single domain chemogenetic tool for protein de-dimerization","month":"09","article_processing_charge":"Yes (in subscription journal)","citation":{"ieee":"J. Antoney <i>et al.</i>, “A F420-dependent single domain chemogenetic tool for protein de-dimerization,” <i>Journal of Molecular Biology</i>, vol. 437, no. 17. Elsevier, 2025.","short":"J. Antoney, S. Kainrath, J.G. Dubowsky, F.H. Ahmed, S.W. Kang, E.R.R. Mackie, G. Bracho Granado, T.P. Soares Da Costa, C.J. Jackson, H.L. Janovjak, Journal of Molecular Biology 437 (2025).","mla":"Antoney, James, et al. “A F420-Dependent Single Domain Chemogenetic Tool for Protein de-Dimerization.” <i>Journal of Molecular Biology</i>, vol. 437, no. 17, 169184, Elsevier, 2025, doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169184\">10.1016/j.jmb.2025.169184</a>.","chicago":"Antoney, James, Stephanie Kainrath, Joshua G. Dubowsky, F. Hafna Ahmed, Suk Woo Kang, Emily R.R. Mackie, Gustavo Bracho Granado, Tatiana P. Soares Da Costa, Colin J. Jackson, and Harald L Janovjak. “A F420-Dependent Single Domain Chemogenetic Tool for Protein de-Dimerization.” <i>Journal of Molecular Biology</i>. Elsevier, 2025. <a href=\"https://doi.org/10.1016/j.jmb.2025.169184\">https://doi.org/10.1016/j.jmb.2025.169184</a>.","ista":"Antoney J, Kainrath S, Dubowsky JG, Ahmed FH, Kang SW, Mackie ERR, Bracho Granado G, Soares Da Costa TP, Jackson CJ, Janovjak HL. 2025. A F420-dependent single domain chemogenetic tool for protein de-dimerization. Journal of Molecular Biology. 437(17), 169184.","ama":"Antoney J, Kainrath S, Dubowsky JG, et al. A F420-dependent single domain chemogenetic tool for protein de-dimerization. <i>Journal of Molecular Biology</i>. 2025;437(17). doi:<a href=\"https://doi.org/10.1016/j.jmb.2025.169184\">10.1016/j.jmb.2025.169184</a>","apa":"Antoney, J., Kainrath, S., Dubowsky, J. G., Ahmed, F. H., Kang, S. W., Mackie, E. R. R., … Janovjak, H. L. (2025). A F420-dependent single domain chemogenetic tool for protein de-dimerization. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2025.169184\">https://doi.org/10.1016/j.jmb.2025.169184</a>"},"PlanS_conform":"1"},{"oa":1,"publication_identifier":{"eissn":["1089-8638"],"issn":["0022-2836"]},"main_file_link":[{"open_access":"1","url":"http://www.biorxiv.org/content/10.1101/583369v1"}],"author":[{"full_name":"Tichy, Alexandra-Madelaine","last_name":"Tichy","first_name":"Alexandra-Madelaine","id":"29D8BB2C-F248-11E8-B48F-1D18A9856A87"},{"first_name":"Elliot J.","full_name":"Gerrard, Elliot J.","last_name":"Gerrard"},{"first_name":"Julien M.D.","full_name":"Legrand, Julien M.D.","last_name":"Legrand"},{"full_name":"Hobbs, Robin M.","last_name":"Hobbs","first_name":"Robin M."},{"last_name":"Janovjak","full_name":"Janovjak, Harald L","first_name":"Harald L","id":"33BA6C30-F248-11E8-B48F-1D18A9856A87","orcid":"0000-0002-8023-9315"}],"publication":"Journal of Molecular Biology","scopus_import":"1","isi":1,"intvolume":"       431","volume":431,"quality_controlled":"1","abstract":[{"lang":"eng","text":"Optogenetics enables the spatio-temporally precise control of cell and animal behavior. Many optogenetic tools are driven by light-controlled protein–protein interactions (PPIs) that are repurposed from natural light-sensitive domains (LSDs). Applying light-controlled PPIs to new target proteins is challenging because it is difficult to predict which of the many available LSDs, if any, will yield robust light regulation. As a consequence, fusion protein libraries need to be prepared and tested, but methods and platforms to facilitate this process are currently not available. Here, we developed a genetic engineering strategy and vector library for the rapid generation of light-controlled PPIs. The strategy permits fusing a target protein to multiple LSDs efficiently and in two orientations. The public and expandable library contains 29 vectors with blue, green or red light-responsive LSDs, many of which have been previously applied ex vivo and in vivo. We demonstrate the versatility of the approach and the necessity for sampling LSDs by generating light-activated caspase-9 (casp9) enzymes. Collectively, this work provides a new resource for optical regulation of a broad range of target proteins in cell and developmental biology."}],"publication_status":"published","department":[{"_id":"HaJa"}],"external_id":{"isi":["000482872100002"]},"date_created":"2019-06-16T21:59:14Z","language":[{"iso":"eng"}],"status":"public","type":"journal_article","day":"09","publisher":"Elsevier","issue":"17","date_published":"2019-08-09T00:00:00Z","oa_version":"Preprint","year":"2019","date_updated":"2025-07-10T11:53:33Z","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","page":"3046-3055","_id":"6564","title":"Engineering strategy and vector library for the rapid generation of modular light-controlled protein–protein interactions","month":"08","article_processing_charge":"No","citation":{"ieee":"A.-M. Tichy, E. J. Gerrard, J. M. D. Legrand, R. M. Hobbs, and H. L. Janovjak, “Engineering strategy and vector library for the rapid generation of modular light-controlled protein–protein interactions,” <i>Journal of Molecular Biology</i>, vol. 431, no. 17. Elsevier, pp. 3046–3055, 2019.","short":"A.-M. Tichy, E.J. Gerrard, J.M.D. Legrand, R.M. Hobbs, H.L. Janovjak, Journal of Molecular Biology 431 (2019) 3046–3055.","mla":"Tichy, Alexandra-Madelaine, et al. “Engineering Strategy and Vector Library for the Rapid Generation of Modular Light-Controlled Protein–Protein Interactions.” <i>Journal of Molecular Biology</i>, vol. 431, no. 17, Elsevier, 2019, pp. 3046–55, doi:<a href=\"https://doi.org/10.1016/j.jmb.2019.05.033\">10.1016/j.jmb.2019.05.033</a>.","ista":"Tichy A-M, Gerrard EJ, Legrand JMD, Hobbs RM, Janovjak HL. 2019. Engineering strategy and vector library for the rapid generation of modular light-controlled protein–protein interactions. Journal of Molecular Biology. 431(17), 3046–3055.","chicago":"Tichy, Alexandra-Madelaine, Elliot J. Gerrard, Julien M.D. Legrand, Robin M. Hobbs, and Harald L Janovjak. “Engineering Strategy and Vector Library for the Rapid Generation of Modular Light-Controlled Protein–Protein Interactions.” <i>Journal of Molecular Biology</i>. Elsevier, 2019. <a href=\"https://doi.org/10.1016/j.jmb.2019.05.033\">https://doi.org/10.1016/j.jmb.2019.05.033</a>.","apa":"Tichy, A.-M., Gerrard, E. J., Legrand, J. M. D., Hobbs, R. M., &#38; Janovjak, H. L. (2019). Engineering strategy and vector library for the rapid generation of modular light-controlled protein–protein interactions. <i>Journal of Molecular Biology</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.jmb.2019.05.033\">https://doi.org/10.1016/j.jmb.2019.05.033</a>","ama":"Tichy A-M, Gerrard EJ, Legrand JMD, Hobbs RM, Janovjak HL. Engineering strategy and vector library for the rapid generation of modular light-controlled protein–protein interactions. <i>Journal of Molecular Biology</i>. 2019;431(17):3046-3055. doi:<a href=\"https://doi.org/10.1016/j.jmb.2019.05.033\">10.1016/j.jmb.2019.05.033</a>"},"doi":"10.1016/j.jmb.2019.05.033","article_type":"original"}]