{"entity": "researcher", "timestamp": "2026-08-08T16:48:36.204Z", "family": "Eriksson", "given": "Leif A", "initials": "LA", "orcid": "0000-0001-5654-3109", "affiliations": ["Department of Chemistry and Molecular Biology, Lundberg Laboratory, University of Gothenburg, 405 30 G\u00f6teborg, Sweden."], "links": {"self": {"href": "https://publications.scilifelab.se/researcher/53b168b3ab17495783f874c427edd0c3.json"}, "display": {"href": "https://publications.scilifelab.se/researcher/53b168b3ab17495783f874c427edd0c3"}}, "publications": [{"entity": "publication", "iuid": "f89fbf236c224156aa48e89c92a6a48f", "links": {"self": {"href": "https://publications.scilifelab.se/publication/f89fbf236c224156aa48e89c92a6a48f.json"}, "display": {"href": "https://publications.scilifelab.se/publication/f89fbf236c224156aa48e89c92a6a48f"}}, "title": "Footprints of natural selection at the mannose-6-phosphate isomerase locus in barnacles.", "authors": [{"family": "Nunez", "given": "Joaquin C B", "initials": "JCB", "orcid": "0000-0002-3171-8918", "researcher": {"href": "https://publications.scilifelab.se/researcher/17eb1fe919d7471ebd0892307c72bea4.json"}}, {"family": "Flight", "given": "Patrick A", "initials": "PA"}, {"family": "Neil", "given": "Kimberly B", "initials": "KB"}, {"family": "Rong", "given": "Stephen", "initials": "S", "orcid": "0000-0002-6584-1391", "researcher": {"href": "https://publications.scilifelab.se/researcher/3944f25fb7a04a9b970260754505a28f.json"}}, {"family": "Eriksson", "given": "Leif A", "initials": "LA", "orcid": "0000-0001-5654-3109", "researcher": {"href": "https://publications.scilifelab.se/researcher/53b168b3ab17495783f874c427edd0c3.json"}}, {"family": "Ferranti", "given": "David A", "initials": "DA"}, {"family": "Rosenblad", "given": "Magnus Alm", "initials": "MA"}, {"family": "Blomberg", "given": "Anders", "initials": "A"}, {"family": "Rand", "given": "David M", "initials": "DM", "orcid": "0000-0001-6817-3459", "researcher": {"href": "https://publications.scilifelab.se/researcher/668b164c47974d5d8f733551d4d2dc2f.json"}}], "type": "journal article", "published": "2020-03-10", "journal": {"title": "Proc. Natl. Acad. Sci. U.S.A.", "issn": "1091-6490", "volume": "117", "issue": "10", "pages": "5376-5385", "issn-l": "0027-8424"}, "abstract": "The mannose-6-phosphate isomerase (Mpi) locus in Semibalanus balanoides has been studied as a candidate gene for balancing selection for more than two decades. Previous work has shown that Mpi allozyme genotypes (fast and slow) have different frequencies across Atlantic intertidal zones due to selection on postsettlement survival (i.e., allele zonation). We present the complete gene sequence of the Mpi locus and quantify nucleotide polymorphism in S. balanoides, as well as divergence to its sister taxon Semibalanus cariosus We show that the slow allozyme contains a derived charge-altering amino acid polymorphism, and both allozyme classes correspond to two haplogroups with multiple internal haplotypes. The locus shows several footprints of balancing selection around the fast/slow site: an enrichment of positive Tajima's D for nonsynonymous mutations, an excess of polymorphism, and a spike in the levels of silent polymorphism relative to silent divergence, as well as a site frequency spectrum enriched for midfrequency mutations. We observe other departures from neutrality across the locus in both coding and noncoding regions. These include a nonsynonymous trans-species polymorphism and a recent mutation under selection within the fast haplogroup. The latter suggests ongoing allelic replacement of functionally relevant amino acid variants. Moreover, predicted models of Mpi protein structure provide insight into the functional significance of the putatively selected amino acid polymorphisms. While footprints of selection are widespread across the range of S. balanoides, our data show that intertidal zonation patterns are variable across both spatial and temporal scales. These data provide further evidence for heterogeneous selection on Mpi.", "doi": "10.1073/pnas.1918232117", "pmid": "32098846", "labels": {"Bioinformatics Support, Infrastructure and Training": "Collaborative", "Bioinformatics Support and Infrastructure": "Collaborative", "Bioinformatics Support for Computational Resources": "Service", "Bioinformatics (NBIS)": "Collaborative"}, "xrefs": [{"db": "pii", "key": "1918232117"}, {"db": "pmc", "key": "PMC7071928"}, {"db": "GENBANK", "key": "MK955540"}, {"db": "GENBANK", "key": "MK955547"}, {"db": "GENBANK", "key": "MK955548"}, {"db": "GENBANK", "key": "MK955609"}, {"db": "GENBANK", "key": "MK955610"}, {"db": "GENBANK", "key": "MK955671"}, {"db": "GENBANK", "key": "MK953001"}, {"db": "GENBANK", "key": "MK953005"}], "notes": [], "created": "2020-02-27T12:43:12.731Z", "modified": "2024-01-16T13:48:42.795Z"}, {"entity": "publication", "iuid": "d1a4105876624a43a0384572921bc580", "links": {"self": {"href": "https://publications.scilifelab.se/publication/d1a4105876624a43a0384572921bc580.json"}, "display": {"href": "https://publications.scilifelab.se/publication/d1a4105876624a43a0384572921bc580"}}, "title": "Proline 411 biases the conformation of the intrinsically disordered plant UVR8 photoreceptor C27 domain altering the functional properties of the peptide.", "authors": [{"family": "Wu", "given": "Min", "initials": "M"}, {"family": "Farkas", "given": "Daniel", "initials": "D"}, {"family": "Eriksson", "given": "Leif A", "initials": "LA", "orcid": "0000-0001-5654-3109", "researcher": {"href": "https://publications.scilifelab.se/researcher/53b168b3ab17495783f874c427edd0c3.json"}}, {"family": "Strid", "given": "\u00c5ke", "initials": "\u00c5", "orcid": "0000-0003-3315-8835", "researcher": {"href": "https://publications.scilifelab.se/researcher/da80ca55a0d54cd082fe18a56d025830.json"}}], "type": "journal article", "published": "2019-01-28", "journal": {"title": "Sci Rep", "issn": "2045-2322", "volume": "9", "issue": "1", "pages": "818", "issn-l": "2045-2322"}, "abstract": "UVR8 (UV RESISTANCE LOCUS 8) is a UV-B photoreceptor responsible for initiating UV-B signalling in plants. UVR8 is a homodimer in its signalling inactive form. Upon absorption of UV radiation, the protein monomerizes into its photoactivated state. In the monomeric form, UVR8 binds the E3 ubiquitin ligase COP1 (CONSTITUTIVELY PHOTOMORPHOGENIC 1), triggering subsequent UV-B-dependent photomorphogenic development in plants. Recent in vivo experiments have shown that the UVR8 C-terminal region (aa 397-423; UVR8C27) alone is sufficient to regulate the activity of COP1. In this work, CD spectroscopy and NMR experiments showed that the UVR8C27 domain was non-structured but gained secondary structure at higher temperatures leading to increased order. Bias-exchange metadynamics simulations were also performed to evaluate the free energy landscape of UVR8C27. An inverted free energy landscape was revealed, with a disordered structure in the global energy minimum. Flanking the global energy minimum, more structured states were found at higher energies. Furthermore, stabilization of the low energy disordered state was attributed to a proline residue, P411, as evident from P411A mutant data. P411 is also a key residue in UVR8 binding to COP1. UVR8C27 is therefore structurally competent to function as a molecular switch for interaction of UVR8 with different binding partners since at higher free energies different structural conformations are being induced in this peptide. P411 has a key role for this function.", "doi": "10.1038/s41598-018-37005-8", "pmid": "30692548", "labels": {"Swedish NMR Centre": "Service"}, "xrefs": [{"db": "pii", "key": "10.1038/s41598-018-37005-8"}, {"db": "pmc", "key": "PMC6349876"}], "notes": [], "created": "2020-01-07T11:39:43.195Z", "modified": "2025-10-17T13:03:58.226Z"}]}