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New β-Propellers Are Continuously Amplified From Single Blades in all Major Lineages of the β-Propeller Superfamily
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Abstract
β-Propellers are toroidal folds, in which consecutive supersecondary structure units of four anti-parallel β-strands–called blades–are arranged radially around a central axis. Uniquely among toroidal folds, blades span the full range of sequence symmetry, from near identity to complete divergence, indicating an ongoing process of amplification and differentiation. We have proposed that the major lineages of β-propellers arose through this mechanism and that therefore their last common ancestor was a single blade, not a fully formed β-propeller. Here we show that this process of amplification and differentiation is also widespread within individual lineages, yielding β-propellers with blades of more than 60% pairwise sequence identity in most major β-propeller families. In some cases, the blades are nearly identical, indicating a very recent amplification event, but even in cases where such recently amplified β-propellers have more than 80% overall sequence identity to each other, comparison of their DNA sequence shows that the amplification occurred independently.
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Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Research works printed but not linked: 61
- Afanasieva, 2019, Structural Diversity of Oligomeric β-propellers with Different Numbers of Identical Blades, eLife, 8, 10.7554/eLife.49853 · DOI
- Altschul, 1997, Gapped BLAST and PSI-BLAST: a New Generation of Protein Database Search Programs, Nucleic Acids Res., 25, 3389, 10.1093/nar/25.17.3389 · DOI · Paper page
- Alva, 2015, A Vocabulary of Ancient Peptides at the Origin of Folded Proteins, eLife, 4, e09410, 10.7554/eLife.09410.001 · DOI
- Amara, 2011, Macromolecular Inhibition of Quorum Sensing: Enzymes, Antibodies, and beyond, Chem. Rev., 111, 195, 10.1021/cr100101c · DOI
- Andrade, 2001, Protein Repeats: Structures, Functions, and Evolution, J. Struct. Biol., 134, 117, 10.1006/jsbi.2001.4392 · DOI
- Beisel, 1999, Tachylectin-2: Crystal Structure of a Specific GlcNAc/GalNAc-Binding Lectin Involved in the Innate Immunity Host Defense of the Japanese Horseshoe Crab Tachypleus Tridentatus, Embo J., 18, 2313, 10.1093/emboj/18.9.2313 · DOI
- Bezerra, 2015, Structure of Human Dipeptidyl Peptidase 10 (DPPY): A Modulator of Neuronal Kv4 Channels, Sci. Rep., 5, 10.1038/srep08769 · DOI
- Biegert, 2008, De Novo identification of Highly Diverged Protein Repeats by Probabilistic Consistency, Oxf. Univ. Press, 24, 807, 10.1093/bioinformatics/btn039 · DOI
- Blatch, 1999, The Tetratricopeptide Repeat: A Structural Motif Mediating Protein-Protein Interactions, BioEssays, 21, 932, 10.1002/(sici)1521-1878(199911)21:11<932::aid-bies5>3.0.co;2-n · DOI
- Bliven, 2019, Analyzing the Symmetrical Arrangement of Structural Repeats in Proteins with CE-Symm, PLoS Comput. Biol., 15, e1006842, 10.1371/journal.pcbi.1006842 · DOI
- Brown, 2013, Identification of the β-Lactamase Inhibitor Protein-II (BLIP-II) Interface Residues Essential for Binding Affinity and Specificity for Class A β-Lactamases, J. Biol. Chem., 288, 17156, 10.1074/jbc.M113.463521 · DOI
- Capella-Gutierrez, 2009, trimAl: a Tool for Automated Alignment Trimming in Large-Scale Phylogenetic Analyses, Bioinformatics, 25, 1972, 10.1093/bioinformatics/btp348 · DOI
- Chaudhuri, 2008, Evolution of the β-propeller Fold, Proteins, 71, 795, 10.1002/prot.21764 · DOI
- Chen, 2011, The Many Blades of the β-propeller Proteins: Conserved but Versatile, Trends Biochem. Sci., 36, 553, 10.1016/j.tibs.2011.07.004 · DOI
- Cock, 2009, Biopython: Freely Available Python Tools for Computational Molecular Biology and Bioinformatics, Bioinformatics, 25, 1422, 10.1093/bioinformatics/btp163 · DOI · Paper page
- Corbett, 2004, The C-Terminal Domain of DNA Gyrase A Adopts a DNA-Bending β-pinwheel Fold, Proc. Natl. Acad. Sci. U.S.A., 101, 7293, 10.1073/pnas.0401595101 · DOI
- Das, 2003, Structure and Evolutionary Aspects of Matrix Metalloproteinases: A Brief Overview, Mol. Cell. Biochem., 253, 31, 10.1023/A:1026093016148 · DOI
- Dunin-Horkawicz, 2014, Prokaryotic Ancestry of Eukaryotic Protein Networks Mediating Innate Immunity and Apoptosis, J. Mol. Biol., 426, 1568, 10.1016/j.jmb.2013.11.030 · DOI
- Edgar, 2004, MUSCLE: Multiple Sequence Alignment with High Accuracy and High Throughput, Nucleic acids Res., 32, 1792, 10.1093/nar/gkh340 · DOI · Paper page
- Frickey, 2004, CLANS: A Java Application for Visualizing Protein Families Based on Pairwise Similarity, Bioinformatics, 20, 3702, 10.1093/bioinformatics/bth444 · DOI
- Fülöp, 1998, Prolyl Oligopeptidase: an Unusual Beta-Propeller Domain Regulates Proteolysis, Cell, 94, 161, 10.1016/S0092-8674(00)81416-6 · DOI
- Fülöp, 1999, β Propellers: Structural Rigidity and Functional Diversity, Curr. Opin. Struct. Biol., 9, 715, 10.1016/S0959-440X(99)00035-4 · DOI
- Ghosh, 1995, The Refined Structure of the Quinoprotein Methanol Dehydrogenase from Methylobacterium Extorquens at 1.94 Å, Structure, 3, 177, 10.1016/S0969-2126(01)00148-4 · DOI
- Giuseppe, 2008, The Leptospiral Antigen Lp49 Is a Two-Domain Protein with Putative Protein Binding Function, J. Struct. Biol., 163, 53, 10.1016/j.jsb.2008.04.003 · DOI
- Gupta, 2014, Kelch Proteins: Emerging Roles in Skeletal Muscle Development and Diseases, Skelet. Muscle, 4, 11, 10.1186/2044-5040-4-11 · DOI
- Guruprasad, 2004, Structural Plasticity Associated with the β-propeller Architecture, Int. J. Biol. Macromol., 34, 55, 10.1016/j.ijbiomac.2004.03.003 · DOI
- Hadjebi, 2008, The RCC1 Superfamily: From Genes, to Function, to Disease, Biochimica Biophysica Acta (BBA) - Mol. Cell Res., 1783, 1467, 10.1016/j.bbamcr.2008.03.015 · DOI
- Hernandez Alvarez, 2019, Structural Diversity of Coiled Coils in Protein Fibers of the Bacterial Cell Envelope, Int. J. Med. Microbiol., 309, 351, 10.1016/J.IJMM.2019.05.011 · DOI
- Hester, 1996, The Mannose-specific Bulb Lectin fromGalanthus nivalis(Snowdrop) Binds Mono- and Dimannosides at Distinct Sites. Structure Analysis of Refined Complexes at 2.3 Å and 3.0 Å Resolution, J. Mol. Biol., 262, 516, 10.1006/jmbi.1996.0532 · DOI
- Hiramatsu, 2003, The Structure and Function of Human Dipeptidyl Peptidase IV, Possessing a Unique Eight-Bladed β-propeller Fold, Biochem. Biophysical Res. Commun., 302, 849, 10.1016/S0006-291X(03)00258-4 · DOI
- Jawad, 2002, Novel Sequences Propel Familiar Folds, Structure, 10, 447, 10.1016/S0969-2126(02)00750-5 · DOI
- Kaus, 2019, The 1.9 Å Crystal Structure of the Extracellular Matrix Protein Bap1 from Vibrio cholerae Provides Insights into Bacterial Biofilm Adhesion, J. Biol. Chem., 294, 14499, 10.1074/jbc.RA119.008335 · DOI
- Kim, 2011, Crystal Structure of Escherichia coli BamB, a Lipoprotein Component of the β-Barrel Assembly Machinery Complex, J. Mol. Biol., 406, 667, 10.1016/j.jmb.2010.12.020 · DOI
- Kopec, 2013, β-Propeller Blades as Ancestral Peptides in Protein Evolution, PLoS ONE, 8, e77074, 10.1371/journal.pone.0077074 · DOI
- Levasseur, 2011, The Role of Duplications in the Evolution of Genomes Highlights the Need for Evolutionary-Based Approaches in Comparative Genomics, Biol. Direct, 6, 11, 10.1186/1745-6150-6-11 · DOI
- Makarova, 2019, Antimicrobial Peptides, Polymorphic Toxins, and Self-Nonself Recognition Systems in Archaea: an Untapped Armory for Intermicrobial Conflicts, mBio, 10, e00715, 10.1128/mBio.00715-19 · DOI
- Matsushima, 2005, Leucine-Rich Repeats (LRRs): Structure, Function, Evolution and Interaction with Ligands, Ddro, 2, 305, 10.2174/1567269054087613 · DOI
- Mirdita, 2021, ColabFold - Making Protein Folding Accessible to All, bioRxiv, 10.1101/2021.08.15.456425 · DOI · Paper page
- Ochiai, 2007, A Novel Structural Fold in Polysaccharide Lyases, J. Biol. Chem., 282, 37134, 10.1074/jbc.M704663200 · DOI
- Ochiai, 2009, Structural Determinants Responsible for Substrate Recognition and Mode of Action in Family 11 Polysaccharide Lyases, J. Biol. Chem., 284, 10181, 10.1074/jbc.M807799200 · DOI
- Oubrie, 1999, Structure and Mechanism of Soluble Quinoprotein Glucose Dehydrogenase, EMBO J., 18, 5187, 10.1093/emboj/18.19.5187 · DOI
- Park, 1998, Cloning and Heterologous Expression of the Gene for BLIP-II, a -Lactamase-Inhibitory Protein from Streptomyces Exfoliatus SMF19, Microbiology, 144, 2161, 10.1099/00221287-144-8-2161 · DOI
- Pei, 2014, PROMALS3D: Multiple Protein Sequence Alignment Enhanced with Evolutionary and Three-Dimensional Structural Information, Methods Mol. Biol., 1079, 263, 10.1007/978-1-62703-646-7_17 · DOI
- Pereira, 2021, The VCBS Superfamily Forms a Third Supercluster of β-propellers that Includes Tachylectin and Integrins, Bioinformatics, 36, 5618, 10.1093/bioinformatics/btaa1085 · DOI
- Polgár, 2002, The Prolyl Oligopeptidase Family, Cell. Mol. Life Sci., 59, 349, 10.1007/s00018-002-8427-5 · DOI
- Pons, 2003, Beta-propellers: Associated Functions and Their Role in Human Diseases, Cmc, 10, 505, 10.2174/0929867033368204 · DOI
- Quistgaard, 2009, Sequence and Structural Analysis of the Asp-Box Motif and Asp-Box Beta-Propellers; a Widespread Propeller-type Characteristic of the Vps10 Domain Family and Several Glycoside Hydrolase Families, BMC Struct. Biol., 9, 46, 10.1186/1472-6807-9-46 · DOI
- Rigden, 2004, The DxDxDG Motif for Calcium Binding: Multiple Structural Contexts and Implications for Evolution, J. Mol. Biol., 343, 971, 10.1016/j.jmb.2004.08.077 · DOI
- Rigden, 2011, New Structural and Functional Contexts of the Dx[DN]xDG Linear Motif: Insights into Evolution of Calcium-Binding Proteins, PLoS ONE, 6, e21507, 10.1371/journal.pone.0021507 · DOI
- Smock, 2016, De Novo Evolutionary Emergence of a Symmetrical Protein Is Shaped by Folding Constraints, Cell, 164, 476, 10.1016/j.cell.2015.12.024 · DOI
- Söding, 2003, More Than the Sum of Their Parts: on the Evolution of Proteins from Peptides, BioEssays, 25, 837, 10.1002/bies.10321 · DOI · Paper page
- Söding, 2005, Protein Homology Detection by HMM-HMM Comparison, Bioinformatics, 21, 951, 10.1093/bioinformatics/bti125 · DOI
- Stevens, 2008, RCC1-like Repeat Proteins: A Pangenomic, Structurally Diverse New Superfamily of β-propeller Domains, Proteins, 70, 378, 10.1002/prot.21521 · DOI
- Studer, 2020, QMEANDisCo-Distance Constraints Applied on Model Quality Estimation, Bioinformatics, 36, 1765, 10.1093/bioinformatics/btz828 · DOI
- Varnay, 2009, Investigations on the 100 kDa Homohexameric Protein Ph1500 by NMR Spectroscopy
- Vrancken, 2020, Molecular Assemblies Built with the Artificial Protein Pizza, J. Struct. Biol. X, 4, 100027, 10.1016/j.yjsbx.2020.100027 · DOI
- Waterhouse, 2018, SWISS-MODEL: Homology Modelling of Protein Structures and Complexes, Nucleic Acids Res., 46, W296, 10.1093/nar/gky427 · DOI
- Yadid, 2011, Functional β-propeller Lectins by Tandem Duplications of Repetitive Units, Narnia, 24, 185, 10.1093/protein/gzq053 · DOI
- Yadid, 2007, Reconstruction of Functional β-Propeller Lectins via Homo-Oligomeric Assembly of Shorter Fragments, J. Mol. Biol., 365, 10, 10.1016/j.jmb.2006.09.055 · DOI
- Zhu, 2016, Origin of a Folded Repeat Protein from an Intrinsically Disordered Ancestor, eLife, 5, 551, 10.7554/eLife.16761 · DOI
- Zimmermann, 2018, A Completely Reimplemented MPI Bioinformatics Toolkit with a New HHpred Server at its Core, J. Mol. Biol., 430, 2237, 10.1016/j.jmb.2017.12.007 · DOI · Paper page
Metadata
- Authors
- Pereira, J., & Lupas, A. N.
- Affiliations
- Max Planck Institute for Biology (DE)
- Corresponding author
- Pereira, Joana
- Lupas, Andrei N.
- Venue
- Frontiers in Molecular Biosciences
- Publisher
- Frontiers Media SA
- Published
- 2022-06-09
- Volume
- 9
- Pages
- 895496-895496
- ISSN
- 2296-889X (ISSN-L)
- PMC
- PMC9218822
- OpenAlex
- W4281991817
- Cited by
- 8
- References
- 2
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 4
- FWCI
- 0.49
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Frontiers in Molecular Biosciences (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
- Funders
- Max-Planck-Gesellschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
- Keywords
- beta-propeller, protein evolution, sequence divergence, supersecondary structure, common ancestor, DNA sequence comparison
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