Crystallization and preliminary crystallographic analysis of the terminal oxygenase component of carbazole 1,9a-dioxygenase of Pseudomonas resinovorans strain CA10

2002 ◽  
Vol 58 (8) ◽  
pp. 1350-1352 ◽  
Author(s):  
Jeong Won Nam ◽  
Zui Fujimoto ◽  
Hiroshi Mizuno ◽  
Hisakazu Yamane ◽  
Takako Yoshida ◽  
...  
Keyword(s):  
Crystallographic Analysis ◽  
Pseudomonas Resinovorans ◽  
Strain Ca10

scholarly journals Transcriptional Regulation of the ant Operon, Encoding Two-Component Anthranilate 1,2-Dioxygenase, on the Carbazole-Degradative Plasmid pCAR1 of Pseudomonas resinovorans Strain CA10

2004 ◽  
Vol 186 (20) ◽  
pp. 6815-6823 ◽  
Author(s):  
Masaaki Urata ◽  
Masatoshi Miyakoshi ◽  
Satoshi Kai ◽  
Kana Maeda ◽  
Hiroshi Habe ◽  
...  
Keyword(s):  
Transcriptional Unit ◽  
Northern Hybridization ◽  
Luciferase Expression ◽  
Transcription Start Point ◽  
Rt Pcr ◽  
Transcription Start ◽  
Pseudomonas Resinovorans ◽  
Two Component ◽  
Degradative Plasmid ◽  
Strain Ca10

ABSTRACT The carbazole-degradative plasmid pCAR1 of Pseudomonas resinovorans strain CA10 has two gene clusters, carAaAaBaBbCAcAdDFE and antABC, which are involved in the conversions of carbazole to anthranilate and anthranilate to catechol, respectively. We proved that the antABC gene cluster, encoding two-component anthranilate 1,2-dioxygenase, constitutes a single transcriptional unit through Northern hybridization and reverse transcription-PCR (RT-PCR) analyses. The transcription start point of antA was mapped at 53 bp upstream point of its translation start point, and the −10 and −35 boxes were homologous to conserved σ70 recognition sequence. Hence the promoter of the ant operon was designated P ant . 5′ Deletion analyses using luciferase as a reporter showed that the region up to at least 70 bp from the transcription start point of antA was necessary for the activation of P ant . Luciferase expression from P ant was induced by anthranilate itself, but not by catechol. Two probable AraC/XylS-type regulatory genes found on pCAR1, open reading frame 22 (ORF22) and ORF23, are tandemly located 3.2 kb upstream of the antA gene. We revealed that the product of ORF23, designated AntR, is indispensable for the stimulation of P ant in Pseudomonas putida cells. Northern hybridization and RT-PCR analyses revealed that another copy of P ant , which is thought to be translocated about 2.1 kb upstream of the carAa gene as a consequence of the transposition of ISPre1, actually drives transcription of the carAa gene in the presence of anthranilate, indicating that both ant and car operons are simultaneously regulated by AntR.

scholarly journals Purification and Characterization of Carbazole 1,9a-Dioxygenase, a Three-Component Dioxygenase System of Pseudomonas resinovorans Strain CA10

2002 ◽  
Vol 68 (12) ◽  
pp. 5882-5890 ◽  
Author(s):  
Jeong-Won Nam ◽  
Hideaki Nojiri ◽  
Haruko Noguchi ◽  
Hiromasa Uchimura ◽  
Takako Yoshida ◽  
...  
Keyword(s):  
Native Form ◽  
Mononuclear Iron ◽  
Pseudomonas Resinovorans ◽  
Apparent Homogeneity ◽  
Strain Bl21 ◽  
Prosthetic Groups ◽  
Strain Ca10 ◽  
Iron Center

ABSTRACT The carbazole 1,9a-dioxygenase (CARDO) system of Pseudomonas resinovorans strain CA10 consists of terminal oxygenase (CarAa), ferredoxin (CarAc), and ferredoxin reductase (CarAd). Each component of CARDO was expressed in Escherichia coli strain BL21(DE3) as a native form (CarAa) or a His-tagged form (CarAc and CarAd) and was purified to apparent homogeneity. CarAa was found to be trimeric and to have one Rieske type [2Fe-2S] cluster and one mononuclear iron center in each monomer. Both His-tagged proteins were found to be monomeric and to contain the prosthetic groups predicted from the deduced amino acid sequence (His-tagged CarAd, one FAD and one [2Fe-2S] cluster per monomer protein; His-tagged CarAc, one Rieske type [2Fe-2S] cluster per monomer protein). Both NADH and NADPH were effective as electron donors for His-tagged CarAd. However, since the k cat/Km for NADH is 22.3-fold higher than that for NADPH in the 2,6-dichlorophenolindophenol reductase assay, NADH was supposed to be the physiological electron donor of CarAd. In the presence of NADH, His-tagged CarAc was reduced by His-tagged CarAd. Similarly, CarAa was reduced by His-tagged CarAc, His-tagged CarAd, and NADH. The three purified proteins could reconstitute the CARDO activity in vitro. In the reconstituted CARDO system, His-tagged CarAc seemed to be indispensable for electron transport, while His-tagged CarAd could be replaced by some unrelated reductases.

scholarly journals Complete Genome Sequence of the Carbazole Degrader Pseudomonas resinovorans Strain CA10 (NBRC 106553)

2013 ◽  
Vol 1 (4) ◽  
Author(s):  
M. Shintani ◽  
A. Hosoyama ◽  
S. Ohji ◽  
K. Tsuchikane ◽  
H. Takarada ◽  
...  
Keyword(s):  
Genome Sequence ◽  
Complete Genome Sequence ◽  
Complete Genome ◽  
Pseudomonas Resinovorans ◽  
Strain Ca10

Enhanced degradation of carbazole and 2,3-dichlorodibenzo-p-dioxin in soils by Pseudomonas resinovorans strain CA10

Chemosphere ◽  
2002 ◽  
Vol 49 (5) ◽  
pp. 485-491 ◽  
Author(s):  
Jaka Widada ◽  
Hideaki Nojiri ◽  
Takako Yoshida ◽  
Hiroshi Habe ◽  
Toshio Omori
Keyword(s):  
Pseudomonas Resinovorans ◽  
Enhanced Degradation ◽  
Strain Ca10

Quaternary structure of Limulus polyphemus hemocyanin

1978 ◽  
Vol 36 (2) ◽  
pp. 176-177
Author(s):  
T. Wichertjes ◽  
E.J. Kwak ◽  
E.F.J. Van Bruggen
Keyword(s):  
Electron Microscopy ◽  
Functional Properties ◽  
Horseshoe Crab ◽  
Temperature Jump ◽  
Quaternary Structure ◽  
Crystallographic Analysis ◽  
Limulus Polyphemus ◽  
Oxygen Binding ◽  
X Ray ◽  
Intact Molecule

Hemocyanin of the horseshoe crab (Limulus polyphemus) has been studied in nany ways. Recently the structure, dissociation and reassembly was studied using electron microscopy of negatively stained specimens as the method of investigation. Crystallization of the protein proved to be possible and X-ray crystallographic analysis was started. Also fluorescence properties of the hemocyanin after dialysis against Tris-glycine buffer + 0.01 M EDTA pH 8.9 (so called “stripped” hemocyanin) and its fractions II and V were studied, as well as functional properties of the fractions by NMR. Finally the temperature-jump method was used for assaying the oxygen binding of the dissociating molecule and of preparations of isolated subunits. Nevertheless very little is known about the structure of the intact molecule. Schutter et al. suggested that the molecule possibly consists of two halves, combined in a staggered way, the halves themselves consisting of four subunits arranged in a square.

Some Observations on Intra-Mitochondrial Crystals

1977 ◽  
Vol 35 ◽  
pp. 406-407
Author(s):  
J. A. Clarke ◽  
D. N. Landon ◽  
P. R. Ward
Keyword(s):  
Cytochrome B ◽  
Mitochondrial Myopathy ◽  
Crystallographic Analysis ◽  
Mitochondrial Membranes ◽  
Electron Microscopes ◽  
Muscle Biopsies

Intra-mitochondrial crystals have been noted in muscle biopsies from patients in a wide variety of diseased states. As far as we are aware, none of these crystals have been subjected to detailed crystallographic analysis. Recently, similar crystals were observed in a biopsy from a patient with a mitochondrial myopathy, characterised by a deficiency in reducible cytochrome b (Morgan-Hughes, J. A., Darveniza, P., Kahn, S. N., Landon, D. N., Sherratt, R. M., Land, J. M. and Clark, J. B., 1977, Brain, In Press). Aldehyde-fixed, osmicated resin imbedded material was examined using Siemens, JEOL and Phillips electron microscopes with goniometer specimen stages. The crystals generally lay between the outer and inner mitochondrial membranes and measured 1 - 3 μm in length and 0.1 - 0.3 μm in width. Characteristically, these crystals revealed specific periodicities.

Morphology of Σ3{/70.53°} grain boundaries in a C15 intermetallic compound

1994 ◽  
Vol 52 ◽  
pp. 684-685
Author(s):  
Fuming Chu ◽  
D. P. Pope ◽  
D. S. Zhou ◽  
T. E. Mitchell
Keyword(s):  
Grain Boundary ◽  
Grain Boundaries ◽  
Crystallographic Analysis ◽  
Laves Phase ◽  
Second Phase ◽  
Bright Field Image ◽  
Boundary Edge ◽  
Arc Melting ◽  
Fcc Lattice ◽  
Diffraction Patterns

A C15 Laves phase, HfV2+Nb, shows promising mechanical properties and here we describe the structure of its grain boundaries. The C15 Laves phase has a fcc lattice with a=7.4Å. An alloy of composition Hf14V64Nb22 (including a C15 matrix and a second phase of V-rich bcc solution) was made by arc-melting. The alloy was homogenized at 1200°C for 120h. Preliminary study concentrated on Σ3{<110>/70.53°} grain boundaries in the C15 phase using Philips 400T and CM 30 microscopes.The most-commonly observed morphology of Σ3{<110>/70.53°} grain boundaries in the C15 phase is a faceted boundary. A bright field image (BFI) of the faceted boundary and the corresponding diffraction patterns with the grain boundary edge-on are shown in Fig. 1(a). From the diffraction patterns using a <110> zone axis for both grains, it is obvious that this is a Σ3{<110>/70.53°} grain boundary. Crystallographic analysis shows that the Σ3{<110>/70.53°} grain boundaries selectively facet with the following relationships between the two grains: {111}1//{111}2, {112}1//{112}2, {111}1//{115}2, and {001}1//{221}2.

A crystallographic analysis of the CoSi/Si(111) interface using Transmission Electron Microscopy

1990 ◽  
Vol 48 (4) ◽  
pp. 574-575
Author(s):  
A.C. Daykin ◽  
C.J. Kiely ◽  
R.C. Pond ◽  
J.L. Batstone
Keyword(s):  
Electron Microscopy ◽  
Transmission Electron Microscopy ◽  
Defect Structure ◽  
Room Temperature ◽  
Theoretical Method ◽  
Crystallographic Analysis ◽  
Si Substrate ◽  
Transmission Electron ◽  
Theoretical Predictions

When CoSi2 is grown onto a Si(111) surface it can form in two distinct orientations. A-type CoSi2 has the same orientation as the Si substrate and B-type is rotated by 180° degrees about the [111] surface normal.One method of producing epitaxial CoSi2 is to deposit Co at room temperature and anneal to 650°C.If greater than 10Å of Co is deposited then both A and B-type CoSi2 form via a number of intermediate silicides .The literature suggests that the co-existence of A and B-type CoSi2 is in some way linked to these intermediate silicides analogous to the NiSi2/Si(111) system. The phase which forms prior to complete CoSi2 formation is CoSi. This paper is a crystallographic analysis of the CoSi2/Si(l11) bicrystal using a theoretical method developed by Pond. Transmission electron microscopy (TEM) has been used to verify the theoretical predictions and to characterise the defect structure at the interface.

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