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https://www.readbyqxmd.com/read/28821406/structural-insight-into-lipopolysaccharide-transport-from-the-gram-negative-bacterial-inner-membrane-to-the-outer-membrane
#1
REVIEW
Haohao Dong, Xiaodi Tang, Zhengyu Zhang, Changjiang Dong
Lipopolysaccharide (LPS) is an important component of the outer membrane (OM) of Gram-negative bacteria, playing essential roles in protecting bacteria from harsh environments, in drug resistance and in pathogenesis. LPS is synthesized in the cytoplasm and translocated to the periplasmic side of the inner membrane (IM), where it matures. Seven lipopolysaccharide transport proteins, LptA-G, form a trans‑envelope complex that is responsible for LPS extraction from the IM and transporting it across the periplasm to the OM...
August 15, 2017: Biochimica et Biophysica Acta
https://www.readbyqxmd.com/read/28816463/signaling-related-mobility-changes-in-bacterial-chemotaxis-receptors-revealed-by-solid-state-nmr
#2
Maryam Kashefi, Lynmarie K Thompson
Bacteria employ remarkable membrane-bound nanoarrays to sense their environment and direct their swimming. Arrays consist of chemotaxis receptor trimers of dimers that are bridged at their membrane-distal tips by rings of two cytoplasmic proteins, a kinase CheA and a coupling protein CheW. It is not clear how ligand binding to the periplasmic domain of the receptor deactivates the CheA kinase bound to the cytoplasmic tip ~300 Å away, but the mechanism is thought to involve changes in dynamics within the cytoplasmic domain...
August 17, 2017: Journal of Physical Chemistry. B
https://www.readbyqxmd.com/read/28814504/osm1-facilitates-the-transfer-of-electrons-from-erv1-to-fumarate-in-the-redox-regulated-import-pathway-in-the-mitochondrial-intermembrane-space
#3
Sonya E Neal, Deepa V Dabir, Juwina Wijaya, Cennyana Boon, Carla M Koehler
Prokaryotes have aerobic and anaerobic electron acceptors for oxidative folding of periplasmic proteins. The mitochondrial intermembrane space has an analogous pathway with the oxidoreductase Mia40 and sulfhydryl oxidase Erv1, termed the MIA pathway. The aerobic electron acceptors include oxygen and cytochrome c, but an acceptor that can function under anaerobic conditions has not been identified. Here we show that the fumarate reductase Osm1, which facilitates electron transfer from fumarate to succinate, fills this gap as a new electron acceptor...
August 16, 2017: Molecular Biology of the Cell
https://www.readbyqxmd.com/read/28811596/complete-alanine-scanning-of-the-escherichia-coli-rbsb-ribose-binding-protein-reveals-residues-important-for-chemoreceptor-signaling-and-periplasmic-abundance
#4
Artur Reimer, Vitali Maffenbeier, Manupriyam Dubey, Vladimir Sentchilo, Diogo Tavares, Manuel Hernandez Gil, Siham Beggah, Jan Roelof van der Meer
The Escherichia coli RbsB ribose binding protein has been used as a scaffold for predicting new ligand binding functions through in silico modeling, yet with limited success and reproducibility. In order to possibly improve the success of predictive modeling on RbsB, we study here the influence of individual residues on RbsB-mediated signaling in a near complete library of alanine-substituted RbsB mutants. Among a total of 232 tested mutants, we found 10 which no longer activated GFPmut2 reporter expression in E...
August 15, 2017: Scientific Reports
https://www.readbyqxmd.com/read/28811582/a-new-class-of-hybrid-secretion-system-is-employed-in-pseudomonas-amyloid-biogenesis
#5
Sarah L Rouse, William J Hawthorne, Jamie-Lee Berry, Dror S Chorev, Sandra A Ionescu, Sebastian Lambert, Fisentzos Stylianou, Wiebke Ewert, Uma Mackie, R Marc L Morgan, Daniel Otzen, Florian-Alexander Herbst, Per H Nielsen, Morten Dueholm, Hagan Bayley, Carol V Robinson, Stephen Hare, Stephen Matthews
Gram-negative bacteria possess specialised biogenesis machineries that facilitate the export of amyloid subunits for construction of a biofilm matrix. The secretion of bacterial functional amyloid requires a bespoke outer-membrane protein channel through which unfolded amyloid substrates are translocated. Here, we combine X-ray crystallography, native mass spectrometry, single-channel electrical recording, molecular simulations and circular dichroism measurements to provide high-resolution structural insight into the functional amyloid transporter from Pseudomonas, FapF...
August 15, 2017: Nature Communications
https://www.readbyqxmd.com/read/28808685/structure-of-a-1-5-mda-adhesin-that-binds-its-antarctic-bacterium-to-diatoms-and-ice
#6
Shuaiqi Guo, Corey A Stevens, Tyler D R Vance, Luuk L C Olijve, Laurie A Graham, Robert L Campbell, Saeed R Yazdi, Carlos Escobedo, Maya Bar-Dolev, Victor Yashunsky, Ido Braslavsky, David N Langelaan, Steven P Smith, John S Allingham, Ilja K Voets, Peter L Davies
Bacterial adhesins are modular cell-surface proteins that mediate adherence to other cells, surfaces, and ligands. The Antarctic bacterium Marinomonas primoryensis uses a 1.5-MDa adhesin comprising over 130 domains to position it on ice at the top of the water column for better access to oxygen and nutrients. We have reconstructed this 0.6-μm-long adhesin using a "dissect and build" structural biology approach and have established complementary roles for its five distinct regions. Domains in region I (RI) tether the adhesin to the type I secretion machinery in the periplasm of the bacterium and pass it through the outer membrane...
August 2017: Science Advances
https://www.readbyqxmd.com/read/28808127/the-components-of-the-unique-zur-regulon-of-cupriavidus-metallidurans-mediate-cytoplasmic-zinc-handling
#7
Lucy Bütof, Christopher Schmidt-Vogler, Martin Herzberg, Cornelia Große, Dietrich H Nies
Zinc is an essential trace element and at the same time it is toxic at high concentrations. In the beta-proteobacterium Cupriavidus metallidurans the highly efficient removal of surplus zinc from the periplasm is responsible for its outstanding metal resistance. Rather than having a typical Zur-dependent, high-affinity ATP-binding cassette transporter of the ABC protein superfamily for zinc uptake at low concentrations, C. metallidurans instead has the secondary zinc importer ZupT of the ZRT/IRT (ZIP) family...
August 14, 2017: Journal of Bacteriology
https://www.readbyqxmd.com/read/28808000/vibrio-cholerae-type-6-secretion-system-effector-trafficking-in-target-bacterial-cells
#8
Brian T Ho, Yang Fu, Tao G Dong, John J Mekalanos
The type 6 secretion system (T6SS) is used by many Gram-negative bacterial species to deliver toxic effector proteins into nearby bacteria prey cells to kill or inhibit their growth. VgrG proteins are core conserved secretion substrates of the T6SS and one subset of T6SS effectors consists of VgrG proteins with C-terminal extension domains carrying various enzymatic activities. In Vibrio cholerae, VgrG3 has a hydrolase extension domain and degrades peptidoglycan in the periplasm of target bacteria. In this study, we replaced this domain with a nuclease domain from Salmonella enterica subsp...
August 14, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28807152/structure-of-thrombospondin-type-3-repeats-in-bacterial-outer-membrane-protein-a-reveals-its-intra-repeat-disulfide-bond-dependent-calcium-binding-capability
#9
Shuyan Dai, Cancan Sun, Kemin Tan, Sheng Ye, Rongguang Zhang
Eukaryotic thrombospondin type 3 repeat (TT3R) is an efficient calcium ion (Ca(2+)) binding motif only found in mammalian thrombospondin family. TT3R has also been found in prokaryotic cellulase Cel5G, which was thought to forfeit the Ca(2+)-binding capability due to the formation of intra-repeat disulfide bonds, instead of the inter-repeat ones possessed by eukaryotic TT3Rs. In this study, we have identified an enormous number of prokaryotic TT3R-containing proteins belonging to several different protein families, including outer membrane protein A (OmpA), an important structural protein connecting the outer membrane and the periplasmic peptidoglycan layer in gram-negative bacteria...
September 2017: Cell Calcium
https://www.readbyqxmd.com/read/28794281/lethality-of-male-lacz-hybrid-protein-shares-mechanistic-attributes-with-oxidative-component-of-antibiotic-lethality
#10
Noriko Takahashi, Charley C Gruber, Jason H Yang, Xiaobo Liu, Dana Braff, Chittampalli N Yashaswini, Sakkarin Bhubhanil, Yoshikazu Furuta, Silvana Andreescu, James J Collins, Graham C Walker
Downstream metabolic events can contribute to the lethality of drugs or agents that interact with a primary cellular target. In bacteria, the production of reactive oxygen species (ROS) has been associated with the lethal effects of a variety of stresses including bactericidal antibiotics, but the relative contribution of this oxidative component to cell death depends on a variety of factors. Experimental evidence has suggested that unresolvable DNA problems caused by incorporation of oxidized nucleotides into nascent DNA followed by incomplete base excision repair contribute to the ROS-dependent component of antibiotic lethality...
August 9, 2017: Proceedings of the National Academy of Sciences of the United States of America
https://www.readbyqxmd.com/read/28791880/reexamining-the-function-of-glutathione-in-oxidative-protein-folding-and-secretion
#11
Agnès Delaunay-Moisan, Alise Ponsero, Michel Toledano
SIGNIFICANCE: Disturbance of glutathione metabolism is a hallmark of numerous diseases, yet glutathione functions are poorly understood. One key to this question is to consider its functional compartmentation. In the endoplasmic reticulum (ER), protein folding involves disulfide bond formation catalyzed by the thiol oxidase Ero1 and proteins from the disulfide isomerase family (PDI). GSH competes with substrates for oxidation by Ero1, but its requirement for ER oxidative protein folding is questioned...
August 9, 2017: Antioxidants & Redox Signaling
https://www.readbyqxmd.com/read/28790314/structural-and-functional-insights-into-the-lipopolysaccharide-abc-transporter-lptb2fg
#12
Haohao Dong, Zhengyu Zhang, Xiaodi Tang, Neil G Paterson, Changjiang Dong
The cell surface of most Gram-negative bacteria contains lipopolysaccharide that is essential for their viability and drug resistance. A 134-kDa protein complex LptB2FG is unique among ATP-binding cassette transporters because it extracts lipopolysaccharide from the external leaflet of the inner membrane and propels it along a filament that extends across the periplasm to directly deliver lipopolysaccharide into the external leaflet of the outer membrane. Here we report the crystal structure of the lipopolysaccharide transporter LptB2FG from Klebsiella pneumoniae, in which both LptF and LptG are composed of a β-jellyroll-like periplasmic domain and six α-helical segments in the transmembrane domain...
August 9, 2017: Nature Communications
https://www.readbyqxmd.com/read/28789875/in%C3%A2-vitro-expression-of-sec-dependent-pathway-and-type-4b-secretion-system-in-piscirickettsia-salmonis
#13
Marcos Cortés, Patricio Sánchez, Pamela Ruiz, Ronie Haro, Jerson Sáez, Fabián Sánchez, Mauricio Hernández, Cristian Oliver, Alejandro J Yáñez
Piscirickettsia salmonis is an intracellular bacterium and the causative agent of Piscirickettsiosis, a disease responsible for considerable mortalities in the Chilean salmon farming industry. Currently, P. salmonis protein translocation across the membrane and the mechanisms by which virulence factors are delivered to host cells are poorly understood. However, it is known that Gram-negative bacteria possess several mechanisms that transport proteins to the periplasmic and extracellular compartments. The aim of this study was to evaluate the expressional changes of several genes in the P...
August 5, 2017: Microbial Pathogenesis
https://www.readbyqxmd.com/read/28780349/implications-of-coordinated-cell-body-rotations-for-leptospira-motility
#14
Kyosuke Takabe, Akihiro Kawamoto, Hajime Tahara, Seishi Kudo, Shuichi Nakamura
The spirochete Leptospira has a coiled cell body and two periplasmic flagella (PFs) that reside beneath the outer sheath. PFs extend from each end of the cell body and are attached to the right-handed spiral protoplasmic cylinder (PC) via a connection with the flagellar motor embedded in the inner membrane. PFs bend each end of the cell body into left-handed spiral (S) or planar hook (H) shapes, allowing leptospiral cells to swim using combined anterior S-end and posterior H-end gyrations with PC rotations...
August 2, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28777087/methylation-crystallization-and-sad-phasing-of-the-csu-pilus-csuc-csue-chaperone-adhesin-subunit-pre-assembly-complex-from-acinetobacter-baumannii
#15
Natalia Pakharukova, Minna Tuittila, Sari Paavilainen, Anton Zavialov
Acinetobacter baumannii is one of the most difficult Gram-negative bacteria to control and treat. This pathogen forms biofilms on hospital surfaces and medical devices using Csu pili assembled via the archaic chaperone-usher pathway. To uncover the mechanism of bacterial attachment to abiotic surfaces, it was aimed to determine the crystal structure of the pilus tip adhesin CsuE. The CsuC-CsuE chaperone-subunit pre-assembly complex was purified from the periplasm of Escherichia coli overexpressing CsuC and CsuE...
August 1, 2017: Acta Crystallographica. Section F, Structural Biology Communications
https://www.readbyqxmd.com/read/28771515/the-role-of-core-and-accessory-type-iv-pilus-genes-in-natural-transformation-and-twitching-motility-in-the-bacterium-acinetobacter-baylyi
#16
Colleen G Leong, Rebecca A Bloomfield, Caroline A Boyd, Amber J Dornbusch, Leah Lieber, Flora Liu, Amie Owen, Erin Slay, Kristine M Lang, C Phoebe Lostroh
Here we present an examination of type IV pilus genes associated with competence and twitching in the bacterium Acinetobacter baylyi (strain ADP1, BD413). We used bioinformatics to identify potential competence and twitching genes and their operons. We measured the competence and twitching phenotypes of the bioinformatically-identified genes. These results demonstrate that competence and twitching in A. baylyi both rely upon a core of the same type IV pilus proteins. The core includes the inner membrane assembly platform (PilC), a periplasmic assemblage connecting the inner membrane assembly platform to the secretin (ComM), a secretin (ComQ) and its associated pilotin (PilF) that assists with secretin assembly and localization, both cytoplasmic pilus retraction ATPases (PilU, PilT), and pilins (ComP, ComB, PilX)...
2017: PloS One
https://www.readbyqxmd.com/read/28771466/assembly-and-stoichiometry-of-the-core-structure-of-the-bacterial-flagellar-type-iii-export-gate-complex
#17
Takuma Fukumura, Fumiaki Makino, Tobias Dietsche, Miki Kinoshita, Takayuki Kato, Samuel Wagner, Keiichi Namba, Katsumi Imada, Tohru Minamino
The bacterial flagellar type III export apparatus, which is required for flagellar assembly beyond the cell membranes, consists of a transmembrane export gate complex and a cytoplasmic ATPase complex. FlhA, FlhB, FliP, FliQ, and FliR form the gate complex inside the basal body MS ring, although FliO is required for efficient export gate formation in Salmonella enterica. However, it remains unknown how they form the gate complex. Here we report that FliP forms a homohexameric ring with a diameter of 10 nm. Alanine substitutions of conserved Phe-137, Phe-150, and Glu-178 residues in the periplasmic domain of FliP (FliPP) inhibited FliP6 ring formation, suppressing flagellar protein export...
August 2017: PLoS Biology
https://www.readbyqxmd.com/read/28768763/a-solute-binding-protein-in-the-closed-conformation-induces-atp-hydrolysis-in-a-bacterial-atp-binding-cassette-transporter-involved-in-the-import-of-alginate
#18
Ai Kaneko, Kasumi Uenishi, Yukie Maruyama, Nobuhiro Mizuno, Seiki Baba, Takashi Kumasaka, Bunzo Mikami, Kousaku Murata, Wataru Hashimoto
The Gram-negative bacterium Sphingomonas sp. A1 incorporates alginate into cells via the cell-surface pit without prior depolymerization by extracellular enzymes. Alginate import across cytoplasmic membranes thereby depends on the ATP-binding cassette (ABC) transporter AlgM1M2SS (a heterotetramer of AlgM1, AlgM2, and AlgS), which cooperates with the periplasmic solute-binding protein AlgQ1 or AlgQ2; however, several details of AlgM1M2SS-mediated alginate import are not well understood. Herein, we analyzed ATPase and transport activities of AlgM1M2SS after reconstitution into liposomes with AlgQ2 and alginate oligosaccharide substrates having different polymerization degrees (PDs)...
August 2, 2017: Journal of Biological Chemistry
https://www.readbyqxmd.com/read/28765215/methane-fueled-syntrophy-through-extracellular-electron-transfer-uncovering-the-genomic-traits-conserved-within-diverse-bacterial-partners-of-anaerobic-methanotrophic-archaea
#19
Connor T Skennerton, Karuna Chourey, Ramsunder Iyer, Robert L Hettich, Gene W Tyson, Victoria J Orphan
The anaerobic oxidation of methane by anaerobic methanotrophic (ANME) archaea in syntrophic partnership with deltaproteobacterial sulfate-reducing bacteria (SRB) is the primary mechanism for methane removal in ocean sediments. The mechanism of their syntrophy has been the subject of much research as traditional intermediate compounds, such as hydrogen and formate, failed to decouple the partners. Recent findings have indicated the potential for extracellular electron transfer from ANME archaea to SRB, though it is unclear how extracellular electrons are integrated into the metabolism of the SRB partner...
August 1, 2017: MBio
https://www.readbyqxmd.com/read/28760846/conformational-changes-that-coordinate-the-activity-of-bama-and-bamd-allowing-%C3%AE-barrel-assembly
#20
Anne L McCabe, Dante Ricci, Modupe Adetunji, Thomas J Silhavy
Most integral outer membrane proteins (OMPs) of Gram-negative bacteria such as Escherichia coli assume a β-barrel structure. The β-barrel Assembly Machine (Bam)-a five-member complex composed of β-barrel OMP BamA and four associated lipoproteins, BamB,C,D, and E-folds and inserts OMPs into the outer membrane. The two essential proteins, BamA and BamD interact to stabilize two subcomplexes, BamAB and BamCDE and genetic and structural evidence suggests that interactions between BamA and BamD occur via an electrostatic interaction between a conserved aspartate residue in a periplasmic domain of BamA and a conserved arginine in BamD...
July 31, 2017: Journal of Bacteriology
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