Results
- Showing results for:
- Reset all filters
Search results
-
Journal articleLiu B, Shadrin A, Sheppard C, et al., 2014, , Bacteriophage, Vol: 4, ISSN: 2159-7073
Many bacteriophages produce small proteins that specifically interfere with the bacterial host transcription machinery and thus contribute to the acquisition of the bacterial cell by the bacteriophage. We recently described how a small protein, called P7, produced by the Xp10 bacteriophage inhibits bacterial transcription initiation by causing the dissociation of the promoter specificity sigma factor subunit from the host RNA polymerase holoenzyme. In this addendum to the original publication, we present the highlights of that research.
-
Journal articleHamilton ML, Franco E, De谩k Z, et al., 2014, , Plant and Cell Physiology, Vol: 55, Pages: 1276-1285, ISSN: 0032-0781
Despite many years of study, the physiological role of cytochrome b-559 (Cyt b-559) within the photosystem II (PSII) complex still remains unclear. Here we describe the analysis of a mutant of the green alga Chlamydomonas reinhardtii in which the His ligand to the haem, provided by the alpha subunit, has been replaced by a Cys residue. The mutant is unable to grow photoautotrophically but can assemble oxygen-evolving PSII supercomplexes to 15-20% of the levels found in the wild-type control. Haem is still detected in the isolated PSII supercomplexes but at sub-stoichiometric levels consistent with weaker binding to the mutated cytochrome. Analysis of PSII activity in cells indicates slowed electron transfer in the mutant between plastoquinones Q<inf>A</inf> and Q<inf>B</inf>. We show that PSII activity in the mutant is more sensitive to chronic photoinhibition than the WT control because of two effects: a faster rate of damage and an impaired PSII repair cycle at the level of synthesis and/or incorporation of D1 into PSII. We also demonstrate that Cyt b-559 plays a role during the critical stage of assembling the Mn <inf>4</inf>CaO<inf>5</inf> cluster. Overall we conclude that Cyt b-559 optimises electron transfer on the acceptor side of PSII and plays physiologically important roles in the assembly, repair and maintenance of the complex. © 2014 The Author 2014.
-
Journal articleSugiura M, Azami C, Koyama K, et al., 2014, , BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, Vol: 1837, Pages: 139-148, ISSN: 0005-2728
- Cite
- Citations: 34
-
Journal articleMickleburgh I, Kafasla P, Cherny D, et al., 2014, , NUCLEIC ACIDS RESEARCH, Vol: 42, Pages: 8605-8620, ISSN: 0305-1048
- Cite
- Citations: 18
-
Journal articleMuhl D, Filloux A, 2014, , PSEUDOMONAS: METHODS AND PROTOCOLS, Vol: 1149, Pages: 521-539, ISSN: 1064-3745
- Cite
- Citations: 13
-
Journal articleBarraud N, Moscoso JA, Ghigo J-M, et al., 2014, , PSEUDOMONAS: METHODS AND PROTOCOLS, Vol: 1149, Pages: 643-651, ISSN: 1064-3745
- Cite
- Citations: 26
-
Journal articlePercy MG, Gruendling A, 2014, , ANNUAL REVIEW OF MICROBIOLOGY, VOL 68, Vol: 68, Pages: 81-100, ISSN: 0066-4227
- Cite
- Citations: 325
-
Journal articleDarbari VC, Lawton E, Lu D, et al., 2014, , NUCLEIC ACIDS RESEARCH, Vol: 42, Pages: 9249-9261, ISSN: 0305-1048
- Cite
- Citations: 3
-
Journal articleJones C, Filloux A, 2014, , PSEUDOMONAS: METHODS AND PROTOCOLS, Vol: 1149, Pages: 457-468, ISSN: 1064-3745
- Cite
- Citations: 1
-
Journal articlevan Thor JJ, Warren MM, Lincoln CN, et al., 2014, , FARADAY DISCUSSIONS, Vol: 171, Pages: 439-455, ISSN: 1359-6640
- Cite
- Citations: 18
-
Journal articleFilloux A, Ramos J-L, 2014,
Pseudomonas Methods and Protocols Preface
, PSEUDOMONAS: METHODS AND PROTOCOLS, Vol: 1149, Pages: V-V, ISSN: 1064-3745- Cite
- Citations: 5
-
Journal articleWang H, Shun M-C, Li X, et al., 2014, , MOLECULAR THERAPY-METHODS & CLINICAL DEVELOPMENT, Vol: 1
- Cite
- Citations: 25
-
Journal articleEngelman A, Cherepanov P, 2014, , Microbiol Spectr, Vol: 2, Pages: 1-22
Due to the importance of human immunodeficiency virus type 1 (HIV-1) integrase as a drug target, the biochemistry and structural aspects of retroviral DNA integration have been the focus of intensive research during the past three decades. The retroviral integrase enzyme acts on the linear double-stranded viral DNA product of reverse transcription. Integrase cleaves specific phosphodiester bonds near the viral DNA ends during the 3' processing reaction. The enzyme then uses the resulting viral DNA 3'-OH groups during strand transfer to cut chromosomal target DNA, which simultaneously joins both viral DNA ends to target DNA 5'-phosphates. Both reactions proceed via direct transesterification of scissile phosphodiester bonds by attacking nucleophiles: a water molecule for 3' processing, and the viral DNA 3'-OH for strand transfer. X-ray crystal structures of prototype foamy virus integrase-DNA complexes revealed the architectures of the key nucleoprotein complexes that form sequentially during the integration process and explained the roles of active site metal ions in catalysis. X-ray crystallography furthermore elucidated the mechanism of action of HIV-1 integrase strand transfer inhibitors, which are currently used to treat AIDS patients, and provided valuable insights into the mechanisms of viral drug resistance.
-
Journal articleReeve B, Sanderson T, Ellis T, et al., 2014, , BIOLUMINESCENCE: FUNDAMENTALS AND APPLICATIONS IN BIOTECHNOLOGY, VOL 2, Vol: 145, Pages: 3-30, ISSN: 0724-6145
- Cite
- Citations: 12
-
Journal articleFilloux A, 2013, , PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 110, Pages: 20360-20361, ISSN: 0027-8424
- Cite
- Citations: 1
-
Journal articleHa K, Buchan JG, Alvarado DM, et al., 2013, , HUMAN MOLECULAR GENETICS, Vol: 22, Pages: 4967-4977, ISSN: 0964-6906
- Cite
- Citations: 50
-
Journal articleJones C, Hachani A, Manoli E, et al., 2013, , Journal of Bacteriology, Vol: 196, Pages: 800-810, ISSN: 1098-5530
The type VI secretion system (T6SS) of Gram-negative bacteria has been involved in various processes, notably bacterial competition and eukaryotic cell subversion. Most Pseudomonas aeruginosa strains possess three T6SS gene clusters, but only the function of the first T6SS (H1-T6SS) has been clearly elucidated. It is involved in the secretion of three toxins (Tse1 to -3) that target bacterial competitors. In the case of the H2- and H3-T6SS, no clear function has been assigned, and only one effector has been associated with these systems. Yet the H2-T6SS was proposed to promote P. aeruginosa internalization in nonphagocytic epithelial cells. Although the H2-T6SS genetic organization is conserved across P. aeruginosa isolates, one feature is the presence of an additional transcriptional unit in the PA14 strain H2-T6SS cluster, which is divergent from the core H2-T6SS genes. A specific set of four genes encodes an Hcp protein (Hcp2), a VgrG protein (VgrG14), an Rhs element (PA14_43100 or RhsP2), and a protein with no homologies with previously characterized proteins (PA14_43090). In this study, we engineered a P. aeruginosa PA14 strain carrying an arabinose-inducible H2-T6SS on the chromosome. We showed that arabinose induction readily promotes assembly of the H2-T6SS, as seen by monitoring Hcp2 secretion. We further studied the secretion fate of VgrG14 and RhsP2, but these were not detectable in the extracellular medium. We finally investigated whether activation of the PA14 H2-T6SS gene cluster could influence phenotypic traits such as internalization in eukaryotic cells, and we reported noteworthy differences compared to strain PAO1, which may be accounted for by the described genetic differences.
-
Journal articleIslam M, Gor J, Perkins SJ, et al., 2013, , JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 288, Pages: 35526-35533
- Cite
- Citations: 30
-
Journal articleGlassford SE, Byrne B, Kazarian SG, 2013, , BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, Vol: 1834, Pages: 2849-2858, ISSN: 1570-9639
- Cite
- Citations: 265
-
Conference paperCarlsson E, Zhang M, Ding JL, et al., 2013,
Gly601 residue of human SARM is critical for interaction with other TLR adaptor proteins
, Annual Congress of the British-Society-for-Immunology, Publisher: WILEY-BLACKWELL, Pages: 180-180, ISSN: 0019-2805 -
Journal articleMuniz-Feliciano L, Van Grol J, Portillo J-AC, et al., 2013, , PLOS PATHOGENS, Vol: 9, ISSN: 1553-7366
- Cite
- Citations: 105
-
Journal articleDevi S, Williams D, 2013, , JOURNAL OF PHARMACEUTICAL SCIENCES, Vol: 102, Pages: 4246-4255, ISSN: 0022-3549
- Cite
- Citations: 20
-
Journal articleRunti G, Ruiz MDCL, Stoilova T, et al., 2013, , JOURNAL OF BACTERIOLOGY, Vol: 195, Pages: 5343-5351, ISSN: 0021-9193
- Cite
- Citations: 82
-
Journal articleCorbalan N, Runti G, Adler C, et al., 2013, , JOURNAL OF BACTERIOLOGY, Vol: 195, Pages: 5352-5361, ISSN: 0021-9193
- Cite
- Citations: 31
-
Journal articleGupta SS, Maetzig T, Maertens GN, et al., 2013, , JOURNAL OF VIROLOGY, Vol: 87, Pages: 12721-12736, ISSN: 0022-538X
- Cite
- Citations: 111
-
Journal articleChae PS, Kruse AC, Gotfryd K, et al., 2013, , CHEMISTRY-A EUROPEAN JOURNAL, Vol: 19, Pages: 15645-15651, ISSN: 0947-6539
- Cite
- Citations: 50
-
Journal articlevan Heel M, 2013, , PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, Vol: 110, Pages: E4175-E4177, ISSN: 0027-8424
- Cite
- Citations: 54
-
Journal articleLu Z, Bergeron JRC, Atkinson RA, et al., 2013, , Open Biology, Vol: 3, Pages: 1-11, ISSN: 2046-2441
The HIV-1 viral infectivity factor (Vif) neutralizes cell-encoded antiviral APOBEC3 proteins by recruiting a cellular ElonginB (EloB)/ElonginC (EloC)/Cullin5-containing ubiquitin ligase complex, resulting in APOBEC3 ubiquitination and proteolysis. The suppressors-of-cytokine-signalling-like domain (SOCS-box) of HIV-1 Vif is essential for E3 ligase engagement, and contains a BC box as well as an unusual proline-rich motif. Here, we report the NMR solution structure of the Vif SOCS–ElonginBC (EloBC) complex. In contrast to SOCS-boxes described in other proteins, the HIV-1 Vif SOCS-box contains only one α-helical domain followed by a β-sheet fold. The SOCS-box of Vif binds primarily to EloC by hydrophobic interactions. The functionally essential proline-rich motif mediates a direct but weak interaction with residues 101–104 of EloB, inducing a conformational change from an unstructured state to a structured state. The structure of the complex and biophysical studies provide detailed insight into the function of Vif's proline-rich motif and reveal novel dynamic information on the Vif–EloBC interaction.
-
Journal articleLai Y, Rosenshine I, Leong JM, et al., 2013, , CELLULAR MICROBIOLOGY, Vol: 15, Pages: 1796-1808, ISSN: 1462-5814
- Cite
- Citations: 94
-
Journal articleHarding CR, Mattheis C, Mousnier A, et al., 2013, , INFECTION AND IMMUNITY, Vol: 81, Pages: 4261-4270, ISSN: 0019-9567
- Cite
- Citations: 30
This data is extracted from the Web of Science and reproduced under a licence from Thomson Reuters. You may not copy or re-distribute this data in whole or in part without the written consent of the Science business of Thomson Reuters.