203 results found
Darvill N, Dubois DJ, Rouse SL, et al., 2018, Structural Basis of Phosphatidic Acid Sensing by APH in Apicomplexan Parasites, STRUCTURE, Vol: 26, Pages: 1059-+, ISSN: 0969-2126
Gatta AT, Sauerwein AC, Zhuravleva A, et al., 2018, Structural insights into a StART-like domain in Lam4 and its interaction with sterol ligands, BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol: 495, Pages: 2270-2274, ISSN: 0006-291X
Liu B, Wang Z, Lan L, et al., 2018, A Rapid Colorimetric Method to Visualize Protein Interactions, CHEMISTRY-A EUROPEAN JOURNAL, Vol: 24, Pages: 6727-6731, ISSN: 0947-6539
Pakharukova N, McKenna S, Tuittila M, et al., 2018, Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information., J Biol Chem
Adhesive pili are external component of fibrous adhesive organelles and help bacteria attach to biotic or abiotic surfaces. The biogenesis of adhesive pili via the chaperone-usher pathway (CUP) is independent of external energy sources. In the classical CUP, chaperones transport assembly-competent pilins in a folded but expanded conformation. During donor-strand exchange, pilins subsequently collapse, producing a tightly-packed hydrophobic core and releasing the necessary free energy to drive fiber formation. Here, we show that pilus biogenesis in non-classical, archaic, and alternative CUPs uses a different source of conformational energy. High-resolution structures of the archaic Csu-pili system from Acinetobacter baumannii revealed that non-classical chaperones employ a short donor-strand motif that is insufficient to fully complement the pilin fold. This results in chaperone-bound pilins being trapped in a substantially unfolded intermediate. The exchange of this short motif with the longer donor strand from adjacent pilin provides the full steric information essential for folding, and thereby induces a large unfolded-to-folded conformational transition to drive assembly. Our findings may inform the development of anti-adhesion drugs (pilicides) to combat bacterial infections.
Rouse SL, Matthews SJ, Dueholm MS, 2018, Ecology and Biogenesis of Functional Amyloids in Pseudomonas., J Mol Biol, Vol: 430, Pages: 3685-3695
Functional amyloids can be found in the extracellular matrix produced by many bacteria during biofilm growth. They mediate the initial attachment of bacteria to surfaces and provide stability and functionality to mature biofilms. Efficient amyloid biogenesis requires a highly coordinated system of amyloid subunits, molecular chaperones and transport systems. The functional amyloid of Pseudomonas (Fap) represents such a system. Here, we review the phylogenetic diversification of the Fap system, its potential ecological role and the dedicated machinery required for Fap biogenesis, with a particular focus on the amyloid exporter FapF, the structure of which has been recently resolved. We also present a sequence covariance-based in silico model of the FapC fiber-forming subunit. Finally, we highlight key questions that remain unanswered and we believe deserve further attention by the scientific community.
Rouse SL, Stylianou F, Wu HYG, et al., 2018, The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil., J Mol Biol, Vol: 430, Pages: 3863-3871
Gram-negative bacteria possess specialized biogenesis machineries that facilitate the export of amyloid subunits, the fibers of which are key components of their biofilm matrix. The secretion of bacterial functional amyloid requires a specialized outer-membrane protein channel through which unfolded amyloid substrates are translocated. We previously reported the crystal structure of the membrane-spanning domain of the amyloid subunit transporter FapF from Pseudomonas. However, the structure of the periplasmic domain, which is essential for amyloid transport, is yet to be determined. Here, we present the crystal structure of the N-terminal periplasmic domain at 1.8-Å resolution. This domain forms a novel asymmetric trimeric coiled coil that possesses a single buried tyrosine residue as well as an extensive hydrogen-bonding network within a glutamine layer. This new structural insight allows us to understand this newly described functional amyloid secretion system in greater detail.
Tabib-Salazar A, Liu B, Barker D, et al., 2018, T7 phage factor required for managing RpoS in Escherichia coli, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 115, Pages: E5353-E5362, ISSN: 0027-8424
Jia Y, Benjamin S, Liu Q, et al., 2017, Toxoplasma gondii immune mapped protein 1 is anchored to the inner leaflet of the plasma membrane and adopts a novel protein fold, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, Vol: 1865, Pages: 208-219, ISSN: 1570-9639
Jia Y, Benjamin S, Liu Q, et al., 2017, "Toxoplasma gondii immune mapped protein 1 is anchored to the inner leaflet of the plasma membrane and adopts a novel protein fold" (vol 1865, pg 208, 2017), BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, Vol: 1865, Pages: 631-631, ISSN: 1570-9639
Jonsson R, Liu B, Struve C, et al., 2017, Structural and functional studies of Escherichia coli aggregative adherence fimbriae (AAF/V) reveal a deficiency in extracellular matrix binding, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, Vol: 1865, Pages: 304-311, ISSN: 1570-9639
Otzen DE, Vad BS, Dueholm MS, et al., 2017, Self-organizing amyloid in bacteria, 19th IUPAB Congress / 11th EBSA Congress, Publisher: SPRINGER, Pages: S98-S98, ISSN: 0175-7571
Otzen DE, Vad BS, Dueholm MS, et al., 2017, Self-organizing amyloid in bacteria, 19th IUPAB Congress / 11th EBSA Congress, Publisher: SPRINGER, Pages: S341-S341, ISSN: 0175-7571
Rouse SL, Hawthorne W, Berry J, et al., 2017, Structural and Mechanistic Insights into Transport of Functional Amyloid Subunits across the Pseudomonas Outer Membrane, 61st Annual Meeting of the Biophysical-Society, Publisher: CELL PRESS, Pages: 188A-188A, ISSN: 0006-3495
Rouse SL, Hawthorne WJ, Berry J-L, et al., 2017, A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis, NATURE COMMUNICATIONS, Vol: 8, ISSN: 2041-1723
Tabib-Salazar A, Liu B, Shadrin A, et al., 2017, Full shut-off of Escherichia coli RNA-polymerase by T7 phage requires a small phage-encoded DNA-binding protein, NUCLEIC ACIDS RESEARCH, Vol: 45, Pages: 7697-7707, ISSN: 0305-1048
Wang S-T, Lin Y, Todorova N, et al., 2017, Facet-Dependent Interactions of Islet Amyloid Polypeptide with Gold Nanoparticles: Implications for Fibril Formation and Peptide-Induced Lipid Membrane Disruption, CHEMISTRY OF MATERIALS, Vol: 29, Pages: 1550-1560, ISSN: 0897-4756
Berry J-L, Xu Y, Ward PN, et al., 2016, A Comparative Structure/Function Analysis of Two Type IV Pilin DNA Receptors Defines a Novel Mode of DNA Binding, STRUCTURE, Vol: 24, Pages: 926-934, ISSN: 0969-2126
Brown DR, Sheppard CM, Burchell L, et al., 2016, The Xp10 Bacteriophage Protein P7 Inhibits Transcription by the Major and Major Variant Forms of the Host RNA Polymerase via a Common Mechanism, JOURNAL OF MOLECULAR BIOLOGY, Vol: 428, Pages: 3911-3919, ISSN: 0022-2836
Grundy GJ, Polo LM, Zeng Z, et al., 2016, PARP3 is a sensor of nicked nucleosomes and monoribosylates histone H2B(Glu2), NATURE COMMUNICATIONS, Vol: 7, ISSN: 2041-1723
Hawthorne W, Rouse S, Sewell L, et al., 2016, Structural insights into functional amyloid inhibition in Gram -ve bacteria, BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 44, Pages: 1643-1649, ISSN: 0300-5127
Lee W-C, Matthews S, Garnett JA, 2016, Crystal structure and analysis of HdaB: The enteroaggregative Escherichia coli AAF/IV pilus tip protein, PROTEIN SCIENCE, Vol: 25, Pages: 1898-1905, ISSN: 0961-8368
Leen EN, Sorgeloos F, Correia S, et al., 2016, A Conserved Interaction between a C-Terminal Motif in Norovirus VPg and the HEAT-1 Domain of eIF4G Is Essential for Translation Initiation., PLOS Pathogens, Vol: 12, ISSN: 1553-7366
Translation initiation is a critical early step in the replication cycle of the positive-sense, single-stranded RNA genome of noroviruses, a major cause of gastroenteritis in humans. Norovirus RNA, which has neither a 5´ m7G cap nor an internal ribosome entry site (IRES), adopts an unusual mechanism to initiate protein synthesis that relies on interactions between the VPg protein covalently attached to the 5´-end of the viral RNA and eukaryotic initiation factors (eIFs) in the host cell. For murine norovirus (MNV) we previously showed that VPg binds to the middle fragment of eIF4G (4GM; residues 652-1132). Here we have used pull-down assays, fluorescence anisotropy, and isothermal titration calorimetry (ITC) to demonstrate that a stretch of ~20 amino acids at the C terminus of MNV VPg mediates direct and specific binding to the HEAT-1 domain within the 4GM fragment of eIF4G. Our analysis further reveals that the MNV C terminus binds to eIF4G HEAT-1 via a motif that is conserved in all known noroviruses. Fine mutagenic mapping suggests that the MNV VPg C terminus may interact with eIF4G in a helical conformation. NMR spectroscopy was used to define the VPg binding site on eIF4G HEAT-1, which was confirmed by mutagenesis and binding assays. We have found that this site is non-overlapping with the binding site for eIF4A on eIF4G HEAT-1 by demonstrating that norovirus VPg can form ternary VPg-eIF4G-eIF4A complexes. The functional significance of the VPg-eIF4G interaction was shown by the ability of fusion proteins containing the C-terminal peptide of MNV VPg to inhibit in vitro translation of norovirus RNA but not cap- or IRES-dependent translation. These observations define important structural details of a functional interaction between norovirus VPg and eIF4G and reveal a binding interface that might be exploited as a target for antiviral therapy.
Liang X, Liu B, Zhu F, et al., 2016, A distinct sortase SrtB anchors and processes a streptococcal adhesin AbpA with a novel structural property, SCIENTIFIC REPORTS, Vol: 6, ISSN: 2045-2322
Miliara X, Matthews S, 2016, Structural comparison of yeast and human intra-mitochondrial lipid transport systems, BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 44, Pages: 479-485, ISSN: 0300-5127
Rasheed M, Garnett J, Perez-Dorado I, et al., 2016, Crystal structure of the CupB6 adhesive tip from the chaperone-usher family of pili from Pseudomonas aeruginosa, BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, Vol: 1864, Pages: 1500-1505, ISSN: 1570-9639
Rouse SL, Hawthorne WJ, Lambert S, et al., 2016, Purification, crystallization and characterization of the Pseudomonas outer membrane protein FapF, a functional amyloid transporter, ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS, Vol: 72, Pages: 892-896, ISSN: 2053-230X
Taglialegna A, Navarro S, Ventura S, et al., 2016, Staphylococcal Bap Proteins Build Amyloid Scaffold Biofilm Matrices in Response to Environmental Signals, PLOS PATHOGENS, Vol: 12, ISSN: 1553-7366
Taylor JD, Hawthorne WJ, Lo J, et al., 2016, Electrostatically-guided inhibition of Curli amyloid nucleation by the CsgC-like family of chaperones, SCIENTIFIC REPORTS, Vol: 6, ISSN: 2045-2322
Taylor JD, Taylor G, Hare SA, et al., 2016, Structures of the DfsB Protein Family Suggest a Cationic, Helical Sibling Lethal Factor Peptide, JOURNAL OF MOLECULAR BIOLOGY, Vol: 428, Pages: 554-560, ISSN: 0022-2836
Benjamin S, Williams F, Kerry L, et al., 2015, NMR assignment of the immune mapped protein 1 (IMP1) homologue from Plasmodium falciparum, BIOMOLECULAR NMR ASSIGNMENTS, Vol: 9, Pages: 393-395, ISSN: 1874-2718
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