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• Journal article
  Briggs LC, Baldwin GS, Miyata N, Kondo H, Zhang X, Freemont PSet al., 2008,
  , JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 283, Pages: 13745-13752
  • Cite
  • Citations: 68
• Journal article
  Ishida N, Sugiura M, Rappaport F, Lai TL, Rutherford AW, Boussac Aet al., 2008,
  , J Biol Chem, Vol: 283, Pages: 13330-13340, ISSN: 0021-9258

  The active site for water oxidation in photosystem II goes through five sequential oxidation states (S(0) to S(4)) before O(2) is evolved. It consists of a Mn(4)Ca cluster close to a redox-active tyrosine residue (Tyr(Z)). Cl(-) is also required for enzyme activity. To study the role of Ca(2+) and Cl(-) in PSII, these ions were biosynthetically substituted by Sr(2+) and Br(-), respectively, in the thermophilic cyanobacterium Thermosynechococcus elongatus. Irrespective of the combination of the non-native ions used (Ca/Br, Sr/Cl, Sr/Br), the enzyme could be isolated in a state that was fully intact but kinetically limited. The electron transfer steps affected by the exchanges were identified and then investigated by using time-resolved UV-visible absorption spectroscopy, time-resolved O(2) polarography, and thermoluminescence spectroscopy. The effect of the Ca(2+)/Sr(2+) and Cl(-)/Br(-) exchanges was additive, and the magnitude of the effect varied in the following order: Ca/Cl < Ca/Br < Sr/Cl < Sr/Br. In all cases, the rate of O(2) release was similar to that of the S(3)Tyr(Z)(.) to S(0)Tyr(Z) transition, with the slowest kinetics (i.e. the Sr/Br enzyme) being approximately 6-7 slower than in the native Ca/Cl enzyme. This slowdown in the kinetics was reflected in a decrease in the free energy level of the S(3) state as manifest by thermoluminescence. These observations indicate that Cl(-) is involved in the water oxidation mechanism. The possibility that Cl(-) is close to the active site is discussed in terms of recent structural models.

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• Journal article
  Wigneshweraraj S, Bose D, Burrows PC, Joly N, Schumacher J, Rappas M, Pape T, Zhang X, Stockley P, Severinov K, Buck Met al., 2008,
  , MOLECULAR MICROBIOLOGY, Vol: 68, Pages: 538-546, ISSN: 0950-382X
  • Cite
  • Citations: 104
• Journal article
  Squire JM, Knupp C, Luther PK, 2008,
  , JOURNAL OF GENERAL PHYSIOLOGY, Vol: 131, Pages: 439-443, ISSN: 0022-1295
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  • Citations: 4
• Journal article
  Hohenester E, 2008,
  , BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 36, Pages: 251-256, ISSN: 0300-5127
  • Cite
  • Citations: 78
• Journal article
  Barber J, Murray JW, 2008,
  , PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES, Vol: 363, Pages: 1129-1137, ISSN: 0962-8436
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  • Citations: 47
• Journal article
  Boussac A, Sugiura M, Lai T-L, Rutherford AWet al., 2008,
  , PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES, Vol: 363, Pages: 1203-1210, ISSN: 0962-8436
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  • Citations: 35
• Journal article
  Barber J, Rutherford AW, 2008,
  , PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES, Vol: 363, Pages: 1125-1128, ISSN: 0962-8436
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  • Citations: 4
• Journal article
  Carafoli F, Saffell JL, Hohenester E, 2008,
  , JOURNAL OF MOLECULAR BIOLOGY, Vol: 377, Pages: 524-534, ISSN: 0022-2836
  • Cite
  • Citations: 32
• Journal article
  Adams JC, Bentley AA, Kvansakul M, Hatherley D, Hohenester Eet al., 2008,
  , JOURNAL OF CELL SCIENCE, Vol: 121, Pages: 784-795, ISSN: 0021-9533
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  • Citations: 42
• Journal article
  Konitsiotis AD, Raynal N, Bihan D, Hohenester E, Farndale RW, Leitinger Bet al., 2008,
  , JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 283, Pages: 6861-6868, ISSN: 0021-9258
  • Cite
  • Citations: 169
• Journal article
  Engelman A, Cherepanov P, 2008,
  , PLOS PATHOGENS, Vol: 4, ISSN: 1553-7366
  • Cite
  • Citations: 188
• Journal article
  Frankel G, Phillips AD, 2008,
  , CELLULAR MICROBIOLOGY, Vol: 10, Pages: 549-556, ISSN: 1462-5814
  • Cite
  • Citations: 133
• Journal article
  De Simone A, Pedone C, Vitagliano L, 2008,
  , BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol: 366, Pages: 800-806, ISSN: 0006-291X
  • Cite
  • Citations: 15
• Journal article
  Colombo G, Meli M, De Simone A, 2008,
  , PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, Vol: 70, Pages: 863-872, ISSN: 0887-3585
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  • Citations: 17
• Journal article
  Mazurkiewicz P, Thomas J, Thompson JA, Liu M, Arbibe L, Sansonetti P, Holden DWet al., 2008,
  , Molecular Microbiology, Vol: 67, Pages: 1371-1383, ISSN: 1365-2958

  SpvC is encoded by the Salmonella virulence plasmid. We have investigated the biochemical function of SpvC and the mechanism by which it is secreted by bacteria and translocated into infected macrophages. We constructed a strain carrying a deletion in spvC and showed that the strain is attenuated for systemic virulence in mice. SpvC can be secreted in vitro by either the SPI-1 or SPI-2 type III secretion systems. Cell biological and genetic experiments showed that translocation of the protein into the cytosol of macrophages by intracellular bacteria is dependent on the SPI-2 T3SS. Using antibodies specific to phospho-amino acids and mass spectrometry we demonstrate that SpvC has phosphothreonine lyase activity on full-length phospho-Erk (pErk) and a synthetic 13-amino-acid phospho-peptide containing the TXY motif. A Salmonella strain expressing spvC from a plasmid downregulated cytokine release from infected cells.

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• Journal article
  Vardakou M, Dumon C, Murray JW, Christakopoulos P, Weiner DP, Juge N, Lewis RJ, Gilbert HJ, Flint JEet al., 2008,
  , JOURNAL OF MOLECULAR BIOLOGY, Vol: 375, Pages: 1293-1305, ISSN: 0022-2836
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  • Citations: 106
• Journal article
  Herrero C, Lassalle-Kaiser B, Leibl W, Rutherford AW, Aukauloo Aet al., 2008,
  , COORDINATION CHEMISTRY REVIEWS, Vol: 252, Pages: 456-468, ISSN: 0010-8545
  • Cite
  • Citations: 92
• Journal article
  Barber J, Murray JW, 2008,
  , COORDINATION CHEMISTRY REVIEWS, Vol: 252, Pages: 233-243, ISSN: 0010-8545
  • Cite
  • Citations: 65
• Journal article
  Yeung HO, Kloppsteck P, Niwa H, Isaacson RL, Matthews S, Zhang X, Freemont PSet al., 2008,
  , BIOCHEMICAL SOCIETY TRANSACTIONS, Vol: 36, Pages: 62-67, ISSN: 0300-5127
  • Cite
  • Citations: 114
• Journal article
  Burgoyne T, Muhamed F, Luther PK, 2008,
  , Cardiovascular Research
  • Cite
• Journal article
  Bai L, Schuller S, Whale A, Mousnier A, Marches O, Wang L, Ooka T, Heuschkel R, Torrente F, Kaper JB, Gomes TAT, Xu J, Phillips AD, Frankel Get al., 2008,
  , INFECTION AND IMMUNITY, Vol: 76, Pages: 361-368, ISSN: 0019-9567
  • Cite
  • Citations: 32
• Journal article
  Baldwin GS, Brooks NJ, Robson RE, Wynveen A, Goldar A, Leikin S, Seddon JM, Kornyshev AAet al., 2008,

  DNA double helices recognize mutual sequence homology in a protein free environment

  , J. Phys. Chem. B, Vol: 112, Pages: 1060-1064
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• Journal article
  van Thor JJ, Ronayne KL, Towrie M, Sage JTet al., 2008,

  Balance between parallel ultrafast excited state proton transfer reactions in GFP has a structural origin.

  , Biophys J, Vol: 95, Pages: 1902-1912

  The fluorescence photocycle of the green fluorescent protein is functionally dependent on the specific structural protein environment. A direct relationship between equilibrium protein side-chain conformation of glutamate 222 and reactivity is established, particularly the rate of ultrafast proton transfer reactions in the fluorescence photocycle. We show that parallel transformations in the photocycle have a structural origin, and we report on the vibrational properties of responsive amino acids on an ultrafast timescale. Blue excitation of GFP drives two parallel, excited-state deuteron transfer reactions with 10 ps and 75 ps time constants to the buried carboxylic acid side chain of glutamate 222 via a hydrogen-bonding network. Assignment of 1456 cm(-1) and 1441 cm(-1) modes to nu(sym) and assignment of 1564 cm(-1) and 1570 cm(-1) features to nu(asym) of E222 in the 10 ps and 75 ps components, respectively, was possible from the analysis of the transient absorption data of an E222D mutant and was consistent with photoselection measurements. In contrast to the wild-type, measurements of E222D can be described with only one difference spectrum, with the nu(sym) mode at 1435 cm(-1) and the nu(asym) mode at 1567 cm(-1), also correlating a large Deltanu(asym-sym) with slow excited-state proton transfer kinetics. Density Functional Theory calculations and published model compound and theoretical studies relate differences in Deltanu(asym-sym) to the strength and number of hydrogen-bonding interactions that are detected via equilibrium geometry and COO- stretching frequency differences of the carboxylate. The correlation of photocycle kinetics with side-chain conformation of the acceptor suggests that proton transfer from S205 to E222 controls the rate of the overall excited-state proton transfer process, which is consistent with recent theoretical predictions. Photoselection measurements show agreement for localized C=O vibrations of chromophore, Q69, and E222 with Den

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• Journal article
  Millson SH, Vaughan CK, Zhai C, Ali MM, Panaretou B, Piper PW, Pearl LH, Prodromou Cet al., 2008,

  Chaperone ligand-discrimination by the TPR-domain protein Tah1

  , Biochem J, Pages: 261-268
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