caa a22 4500 606177329 CHVBK 20210128100751.0 cr unu---uuuuu 210128e20151101xx s 000 0 eng 10.1007/s00018-015-1932-0 doi (NATIONALLICENCE)springer-10.1007/s00018-015-1932-0 Two independently folding units of Plasmodium profilin suggest evolution via gene fusion [Elektronische Daten] [Saligram Bhargav, Juha Vahokoski, Juha Kallio, Andrew Torda, Petri Kursula, Inari Kursula] Gene fusion is a common mechanism of protein evolution that has mainly been discussed in the context of multidomain or symmetric proteins. Less is known about fusion of ancestral genes to produce small single-domain proteins. Here, we show with a domain-swapped mutant Plasmodium profilin that this small, globular, apparently single-domain protein consists of two foldons. The separation of binding sites for different protein ligands in the two halves suggests evolution via an ancient gene fusion event, analogous to the formation of multidomain proteins. Finally, the two fragments can be assembled together after expression as two separate gene products. The possibility to engineer both domain-swapped dimers and half-profilins that can be assembled back to a full profilin provides perspectives for engineering of novel protein folds, e.g., with different scaffolding functions. Springer Basel, 2015 Actin-binding protein nationallicence Crystal structure nationallicence β-Hairpin nationallicence Modular nationallicence Protein interaction nationallicence Sequence analysis nationallicence Small-angle X-ray scattering nationallicence Tris : 2-amino-2-hydroxymethyl-propane-1,3-diol nationallicence CD : Circular dichroism nationallicence DTT : Dithiothreitol nationallicence SEC : Size-exclusion chromatography nationallicence SAXS : Small-angle X-ray scattering nationallicence SR : Synchrotron radiation nationallicence TEV : Tobacco etch virus nationallicence TIM : Triosephosphate isomerase nationallicence Bhargav Saligram Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland aut Vahokoski Juha Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland aut Kallio Juha Helmholtz Centre for Infection Research, Notkestrasse 85, 22607, Hamburg, Germany aut Torda Andrew Centre for Bioinformatics, University of Hamburg, Bundesstrasse 43, 20146, Hamburg, Germany aut Kursula Petri Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland aut Kursula Inari Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland aut Cellular and Molecular Life Sciences Springer Basel 72/21(2015-11-01), 4193-4203 1420-682X 72:21<4193 2015 72 18 https://doi.org/10.1007/s00018-015-1932-0 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00018-015-1932-0 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Bhargav Saligram Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland aut NATIONALLICENCE 700 1- Vahokoski Juha Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland aut NATIONALLICENCE 700 1- Kallio Juha Helmholtz Centre for Infection Research, Notkestrasse 85, 22607, Hamburg, Germany aut NATIONALLICENCE 700 1- Torda Andrew Centre for Bioinformatics, University of Hamburg, Bundesstrasse 43, 20146, Hamburg, Germany aut NATIONALLICENCE 700 1- Kursula Petri Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland aut NATIONALLICENCE 700 1- Kursula Inari Faculty of Biochemistry and Molecular Medicine, University of Oulu, P.O. Box 5400, 90014, Oulu, Finland aut NATIONALLICENCE 773 0- Cellular and Molecular Life Sciences Springer Basel 72/21(2015-11-01), 4193-4203 1420-682X 72:21<4193 2015 72 18