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  • 1
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States of America, 30 April 2013, Vol.110(18), pp.7217-22
    Description: The (6-4) photolyases use blue light to reverse UV-induced (6-4) photoproducts in DNA. This (6-4) photorepair was thought to be restricted to eukaryotes. Here we report a prokaryotic (6-4) photolyase, PhrB from Agrobacterium tumefaciens, and propose that (6-4) photolyases are broadly distributed in prokaryotes. The crystal structure of photolyase related protein B (PhrB) at 1.45 Å resolution suggests a DNA binding mode different from that of the eukaryotic counterparts. A His-His-X-X-Arg motif is located within the proposed DNA lesion contact site of PhrB. This motif is structurally conserved in eukaryotic (6-4) photolyases for which the second His is essential for the (6-4) photolyase function. The PhrB structure contains 6,7-dimethyl-8-ribityllumazine as an antenna chromophore and a [4Fe-4S] cluster bound to the catalytic domain. A significant part of the Fe-S fold strikingly resembles that of the large subunit of eukaryotic and archaeal primases, suggesting that the PhrB-like photolyases branched at the base of the evolution of the cryptochrome/photolyase family. Our study presents a unique prokaryotic (6-4) photolyase and proposes that the prokaryotic (6-4) photolyases are the ancestors of the cryptochrome/photolyase family.
    Keywords: Agrobacterium Tumefaciens -- Enzymology ; Deoxyribodipyrimidine Photo-Lyase -- Chemistry ; Iron-Sulfur Proteins -- Chemistry ; Pteridines -- Metabolism
    ISSN: 00278424
    E-ISSN: 1091-6490
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  • 2
    In: PLoS ONE, 2014, Vol.9(10)
    Description: Bacteriophytochromes (BphPs) are light-sensing regulatory proteins encoded in photosynthetic and non-photosynthetic bacteria. This protein class incorporate bilin as their chromophore, with majority of them bearing a light- regulated His kinase or His kinase related module in the C-terminal. We studied the His kinase actives in the temperature range of 5°C to 40°C on two BphPs, Agp1 from Agrobacterium tumefaciens and Cph1 from cyanobacterium Synechocystis PCC 6803. As reported, the phosphorylation activities of the far red (FR) irradiated form of the holoprotein is stronger than that of the red (R) irradiated form in both phytochromes. We observed for the apoprotein and FR irradiated holoprotein of Agp1 an increase in the phosphorylation activities from 5°C to 25°C and a decrease from 25°C to 40°C. At 5°C the activities of the apoprotein were significantly lower than those of the FR irradiated holoprotein, which was opposite at 40°C. A similar temperature pattern was observed for Cph1, but the maximum of the apoprotein was at 20°C while the maximum of the FR irradiated holoprotein was at 10°C. At 40°C, prolonged R irradiation leads to an irreversible bleaching of Cph1, an effect which depends on the C-terminal His kinase module. A more prominent and reversible temperature effect on spectral properties of Agp1, mediated by the His kinase, has been reported before. His kinases in phytochromes could therefore share similar temperature characteristics. We also found that phytochrome B mutants of Arabidopsis have reduced hypocotyl growth at 37°C in darkness, suggesting that this phytochrome senses the temperature or mediates signal transduction of temperature effects.
    Keywords: Research Article ; Biology And Life Sciences
    E-ISSN: 1932-6203
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  • 3
    Article
    Article
    Language: English
    In: Forum der Psychoanalyse, Sept, 2011, Vol.27(3), p.219(4)
    Description: Byline: Ulrich Lamparter (1) Author Affiliation: (1) Institut und Poliklinik fur Psychosomatische Medizin und Psychotherapie, Universitatsklinikum Hamburg-Eppendorf, Martinistr. 52, 20246, Hamburg, Deutschland Article History: Registration Date: 15/07/2011 Online Date: 10/08/2011
    ISSN: 0178-7667
    Source: Cengage Learning, Inc.
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  • 4
    Language: English
    In: PLoS ONE, 2011, Vol.6(10), p.e25977
    Description: Phytochromes are widely distributed biliprotein photoreceptors with a conserved N-terminal chromophore-binding domain. Most phytochromes bear a light-regulated C-terminal His kinase or His kinase-like region. We investigated the effects of light and temperature on the His kinase activity of the phytochrome Agp1 from Agrobacterium tumefaciens . As in earlier studies, the phosphorylation activity of the holoprotein after far-red irradiation (where the red-light absorbing Pr form dominates) was stronger than that of the holoprotein after red irradiation (where the far red-absorbing Pfr form dominates). Phosphorylation activities of the apoprotein, far red-irradiated holoprotein, and red-irradiated holoprotein decreased when the temperature increased from 25°C to 35°C; at 40°C, almost no kinase activity was detected. The activity of a holoprotein sample incubated at 40°C was nearly completely restored when the temperature returned to 25°C. UV/visible spectroscopy indicated that the protein was not denatured up to 45°C. At 50°C, however, Pfr denatured faster than the dark-adapted sample containing the Pr form of Agp1. The Pr visible spectrum was unaffected by temperatures of 20–45°C, whereas irradiated samples exhibited a clear temperature effect in the 30–40°C range in which prolonged irradiation resulted in the photoconversion of Pfr into a new spectral species termed Prx. Pfr to Prx photoconversion was dependent on the His-kinase module of Agp1; normal photoconversion occurred at 40°C in the mutant Agp1-M15, which lacks the C-terminal His-kinase module, and in a domain-swap mutant in which the His-kinase module of Agp1 is replaced by the His-kinase/response regulator module of the other A. tumefaciens phytochrome, Agp2. The temperature-dependent kinase activity and spectral properties in the physiological temperature range suggest that Agp1 serves as an integrated light and temperature sensor in A. tumefaciens .
    Keywords: Research Article ; Biology ; Molecular Biology ; Biochemistry
    E-ISSN: 1932-6203
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  • 5
    Language: German
    In: Forum der Psychoanalyse, 2014, Vol.30(1), pp.27-39
    Description: Die alte Frage von „Deutung und Beziehung“ aufgreifend, führt die Arbeit in die Unterscheidung von impliziter und expliziter Behandlungspraxis bei Michael Ermann ein. Im Anschluss daran werden implizite Wirkfaktoren in der psychoanalytischen Praxis anhand der therapeutischen Alltagserfahrung beschrieben. Schließlich wird die „Plica in der Gegenübertragung“ als ein Wirkfaktor für den weiteren Verlauf einer Behandlung abgegrenzt: die Verortung der Geschichte des Patienten in der persönlichen Welt des Analytikers. Mögliche Anwendungen des Konzepts werden diskutiert. Taking up the age-old question of „interpretation and relationship“ leads this article into the differentiation between implicit and explicit treatment practice by Michael Ermann. Subsequent to this, implicit effect factors in the psychoanalytical practice are described based on routine daily therapeutic experience. Finally, the “plica in countertransference” is singled out as an effective factor for the further course of treatment: the positioning of the history of the patient in the personal world of the analyst. Possible applications of this concept are discussed.
    Keywords: Psychology ; Psychology, General ; Psychiatry ; Psychotherapy ; Psychoanalysis ; Psychology;
    ISSN: 0178-7667
    E-ISSN: 1437-0751
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  • 6
    Language: English
    In: PLoS ONE, Oct 7, 2014, Vol.9(10)
    Description: Bacteriophytochromes (BphPs) are light-sensing regulatory proteins encoded in photosynthetic and non-photosynthetic bacteria. This protein class incorporate bilin as their chromophore, with majority of them bearing a light- regulated His kinase or His kinase related module in the C-terminal. We studied the His kinase actives in the temperature range of 5#176;C to 40#176;C on two BphPs, Agp1 from Agrobacterium tumefaciens and Cph1 from cyanobacterium Synechocystis PCC 6803. As reported, the phosphorylation activities of the far red (FR) irradiated form of the holoprotein is stronger than that of the red (R) irradiated form in both phytochromes. We observed for the apoprotein and FR irradiated holoprotein of Agp1 an increase in the phosphorylation activities from 5#176;C to 25#176;C and a decrease from 25#176;C to 40#176;C. At 5#176;C the activities of the apoprotein were significantly lower than those of the FR irradiated holoprotein, which was opposite at 40#176;C. A similar temperature pattern was observed for Cph1, but the maximum of the apoprotein was at 20#176;C while the maximum of the FR irradiated holoprotein was at 10#176;C. At 40#176;C, prolonged R irradiation leads to an irreversible bleaching of Cph1, an effect which depends on the C-terminal His kinase module. A more prominent and reversible temperature effect on spectral properties of Agp1, mediated by the His kinase, has been reported before. His kinases in phytochromes could therefore share similar temperature characteristics. We also found that phytochrome B mutants of Arabidopsis have reduced hypocotyl growth at 37#176;C in darkness, suggesting that this phytochrome senses the temperature or mediates signal transduction of temperature effects.
    Keywords: Cellular Signal Transduction ; Photosynthesis ; Proteins ; Phytochrome ; Phosphotransferases
    ISSN: 1932-6203
    Source: Cengage Learning, Inc.
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  • 7
    Language: English
    In: Journal of bacteriology, October 2010, Vol.192(19), pp.5124-33
    Description: Phytochromes are biliprotein photoreceptors that are found in plants, bacteria, and fungi. Prototypical phytochromes have a Pr ground state that absorbs in the red spectral range and is converted by light into the Pfr form, which absorbs longer-wavelength, far-red light. Recently, some bacterial phytochromes have been described that undergo dark conversion of Pr to Pfr and thus have a Pfr ground state. We show here that such so-called bathy phytochromes are widely distributed among bacteria that belong to the order Rhizobiales. We measured in vivo spectral properties and the direction of dark conversion for species which have either one or two phytochrome genes. Agrobacterium tumefaciens C58 contains one bathy phytochrome and a second phytochrome which undergoes dark conversion of Pfr to Pr in vivo. The related species Agrobacterium vitis S4 contains also one bathy phytochrome and another phytochrome with novel spectral properties. Rhizobium leguminosarum 3841, Rhizobium etli CIAT652, and Azorhizobium caulinodans ORS571 contain a single phytochrome of the bathy type, whereas Xanthobacter autotrophicus Py2 contains a single phytochrome with dark conversion of Pfr to Pr. We propose that bathy phytochromes are adaptations to the light regime in the soil. Most bacterial phytochromes are light-regulated histidine kinases, some of which have a C-terminal response regulator subunit on the same protein. According to our phylogenetic studies, the group of phytochromes with this domain arrangement has evolved from a bathy phytochrome progenitor.
    Keywords: Bacterial Proteins -- Metabolism ; Phytochrome -- Metabolism ; Rhizobium -- Metabolism
    ISSN: 00219193
    E-ISSN: 1098-5530
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  • 8
    Language: English
    In: Journal of Physical Chemistry A, Dec 5, 2013, Vol.117(48), p.14940-14950
    Keywords: Phytochrome -- Analysis ; Chemical Reactions -- Analysis
    ISSN: 1089-5639
    Source: Cengage Learning, Inc.
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  • 9
    Language: English
    In: The journal of physical chemistry. B, 05 December 2013, Vol.117(48), pp.14940-50
    Description: Fluorescence line narrowing (FLN) spectroscopy was used to study bacteriophytochromes and variants from various species in their red-absorbing Pr ground state, including phytochromes Agp1 from Agrobacterium tumefaciens , DrBphP from Deinococcus radiodurans , and RpBphP2 and RpBphP3 from Rhodopseudomonas palustris . A species-dependent narrowing of the fluorescence emission bands is observed. The results suggest varied pigment-protein interactions, possibly connected to chromophore mobility or extended water pyrrole networks inside of the differing binding pockets. Solvent water isotope exchange from H2O-based buffer to D2O-based buffer solutions was used to identify specific vibrational modes of the chromophore. In addition to the expected frequency shifts upon isotope exchange, the line narrowing efficiency is increased in deuterated compared to protonated surroundings. We conclude that proton dynamics inside of the protein binding pocket are a dominant source of spectral diffusion at low temperatures, which possibly relates to the previous observation that the electronic transition is directly coupled to proton transfer. The FLN spectra of Agp1 reconstituted with a synthesized pigment shows strong line narrowing efficiency even in protonated buffer solution. The FLN spectra of a point mutant of RpBphP3 highlight the involvement of aspartate 216 in a hydrogen bond network around the chromophore. On the basis of similar FLN characteristics in RpBphP2 and RpBphP3, we propose a similarly extended hydrogen bond network around their chromophores despite the different photoreactions leading to red- or blue-shifted absorption relative to the respective photoreceptors' ground-state absorption.
    Keywords: Biliverdine -- Chemistry ; Phytochrome -- Chemistry
    ISSN: 15206106
    E-ISSN: 1520-5207
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  • 10
    Language: English
    In: The Journal of biological chemistry, 23 September 2016, Vol.291(39), pp.20674-91
    Description: Agp1 is a canonical biliverdin-binding bacteriophytochrome from the soil bacterium Agrobacterium fabrum that acts as a light-regulated histidine kinase. Crystal structures of the photosensory core modules (PCMs) of homologous phytochromes have provided a consistent picture of the structural changes that these proteins undergo during photoconversion between the parent red light-absorbing state (Pr) and the far-red light-absorbing state (Pfr). These changes include secondary structure rearrangements in the so-called tongue of the phytochrome-specific (PHY) domain and structural rearrangements within the long α-helix that connects the cGMP-specific phosphodiesterase, adenylyl cyclase, and FhlA (GAF) and the PHY domains. We present the crystal structures of the PCM of Agp1 at 2.70 Å resolution and of a surface-engineered mutant of this PCM at 1.85 Å resolution in the dark-adapted Pr states. Whereas in the mutant structure the dimer subunits are in anti-parallel orientation, the wild-type structure contains parallel subunits. The relative orientations between the PAS-GAF bidomain and the PHY domain are different in the two structures, due to movement involving two hinge regions in the GAF-PHY connecting α-helix and the tongue, indicating pronounced structural flexibility that may give rise to a dynamic Pr state. The resolution of the mutant structure enabled us to detect a sterically strained conformation of the chromophore at ring A that we attribute to the tight interaction with Pro-461 of the conserved PRXSF motif in the tongue. Based on this observation and on data from mutants where residues in the tongue region were replaced by alanine, we discuss the crucial roles of those residues in Pr-to-Pfr photoconversion.
    Keywords: Agrobacterium ; Conformational Change ; Crystal Structure ; Histidine Kinase ; Photoreceptor ; Phytochrome ; Quaternary Structure ; Signal Transduction ; Tertiary Structure ; Protein Multimerization ; Agrobacterium -- Chemistry ; Bacterial Proteins -- Chemistry ; Phytochrome -- Chemistry
    E-ISSN: 1083-351X
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