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G Gingras

Publications and source records attributed to G Gingras.

At least 19 recordsLinked to original sources
PubMed1990

Plasmid from photosynthetic bacterium Ectothiorhodospira Sp. carries a transposable streptomycin resistance gene.

Centrifugation through a cesium chloride density gradient and agarose gel electrophoresis of the DNA from the purple non-sulfur photosynthetic bacterium Ectothiorhodospira sp. resolved a single extrachromosomal element, plasmid pDG1. Its size was estimated to be 13.2 kilobases by restriction endonuclease mapping. Plasmid pDG1 and two restriction fragments thereof were cloned in Escherichia coli C600 with plasmid pBR327 as a vector to form mixed plasmids pDGBR1, pDGBR2, and pDGBR3. The resistance to streptomycin and mercury found in Ectothiorhodospira sp. was transferred to E. coli C600 after transformation with pDGBR1 but not with pDGBR2 and pDGBR3. The replication origin of pDG1 was estimated to be within a 2-kilobase restriction fragment of pDG1 by monitoring its replication in E. coli HB101, using a kanamycin resistance reporter gene. High stringency molecular hybridization with 32P-labeled pDG1 identified specific fragments of genomic DNA, suggesting the integration of some plasmid sequences. In accordance with the hypothesis that this integration is due to a transposon, we tested the transfer of streptomycin resistance from pDG1 into plasmid pVK100 used as a target. For this test, we regrouped in the same cells of E. coli HB101, pDGBR1 and mobilizable plasmid pVK100 (tetr,kmr). We used the conjugation capacity of the pVK100/pRK2013 system to rescue the target plasmid pVK100 into nalidixic acid-resistant E. coli DH1. The transfer frequency of streptomycin resistance into pVK100 was 10(-5), compatible with a transposition event. In line with the existence of a transposon on pDG1, heteroduplex mapping indicated the presence of inverted repeats approximately 7.5 kb from one another.

Chromatiaceae↗
PubMed1989

Mapping of the puh messenger RNAs from Rhodospirillum rubrum. Evidence for tandem promoters.

The mRNA transcripts of Rhodospirillum rubrum gene puh, coding for the H subunit of the photoreaction center, and of genes flanking puh were analyzed by blot hybridization. Open reading frame G115, upstream of structural gene puh, is transcribed as a 2.25-kilobase mRNA. Gene puh itself is transcribed as two mRNAs of 1118 and 1032 nucleotides. Mung bean nuclease protection analysis shows that the puh transcripts have different 5' termini within open reading frame G115 and a unique rho-independent termination signal within open reading frame I2372. The lifetimes of the puh messages, as determined by an oxygen blockade of transcription, were 10 and 12 min for the large and small puh mRNAs, respectively. An expression vector carrying a chloramphenicol acetyltransferase gene was used to select promoters in DNA stretches upstream of the startpoints of each of these transcripts. Chloramphenicol resistance was expressed in Escherichia coli, using as a promoter a 179-nucleotide stretch upstream of the small mRNA startpoint but not from a 124-nucleotide stretch upstream of the large mRNA startpoint. The promoter for the small mRNA, designated Ppuh2, is thought to encompass in its -10 and -35 regions a sigma 70-like RNA polymerase recognition sequence. The region upstream of the large message startpoint contains a sequence similar in its -12 and -24 regions to promoter sequences recognized by the sigma 60 RNA polymerase holoenzyme. This is designated as promoter Ppuh1.Ppuh1 is proposed to be strictly regulated by light intensity and by oxygen tension while Ppuh2 would be less sensitive to these parameters.

Bacterial Proteins↗
PubMed1985

Isolation and partial characterization of the messenger RNA encoding the B880 holochrome protein of Rhodospirillum rubrum.

The B880 holochrome messenger RNA was extracted from cultures of the photosynthetic bacterium Rhodospirillum rubrum. It was purified by chromatography on Sepharose 4B followed by sucrose density gradient centrifugation. The purified fractions were shown to program an Escherichia coli cell-free system into synthesizing both the alpha and the beta polypeptides of the holochrome. The translation products were identified by immunoprecipitation with specific antibodies raised against these polypeptides. The latter are effective competitors with the translation products for antigen-antibody complex formation. The purest mRNA preparations contained approximately 33% holochrome messenger RNA activity. Its most probable size, as determined by agarose gel electrophoresis in the presence of 6 M urea or methylmercuric hydroxide, is approximately 620 nucleotides. Since the combined sizes of the alpha and beta polypeptides add up to only 106 amino acid residues, we conclude that the holochrome mRNA is most probably polycistronic.

Bacterial Proteins↗
PubMed1979

Photoreaction center of photosynthetic bacteria. 1. Further chemical characterization of the photoreaction center from Rhodospirillum rubrum.

The photoreaction center from Rhodospirillum rubrum contains about 90% protein, 6% pigment, mere traces of lipids, and no cytochromes. It also contains at least 1 mol of ubiquinone and 1 iron atom per mol. Its three-component polypeptide chains were isolated by preparative electrophoresis, and their molar stoichiometry was established as 1:1:1. The amino acid composition of the photoreaction center from strain S1 and from its subunits is reported. The protein as a whole contains about 65% nonpolar residues, and the degree of hydrophobicity of its subunits is alpha less than beta less than gamma. The minimal molecular weight based on the extinction coefficient and on the amino acid content is 90 000. This corresponds to a half-cystine mole number of 6.

Amino Acids↗
PubMed1979

Photoreaction center of photosynthetic bacteria. 2. Size and quaternary structure of the photoreaction centers from Rhodospirillum rubrum strain G9 and from Rhodopseudomonas sphaeroides strain 2.4.1.

The photoreaction center from Rhodospirillum rubrum strain G9 binds about 6 times as much sodium dodecyl sulfate as certain proteins commonly used as molecular weight markers for sodium dodecyl sulfate--polyacrylamide gel electrophoresis. This presumably explains the apparent discrepancy between the molecular weight of the photoreaction center determined by electrophoresis (76 000) and its minimal molecular weight (87 000). The molecular weight of the photoreaction center solubilized with Triton X-100 was determined by three different methods: conventional sedimentation equilibrium, a combination of sedimentation velocity and gel filtration measurements, and sedimentation equilibrium in H2O and in D2O. Each technique required a determination of the amount of bound detergent. All three methods gave molecular weight values close to 60 000. A similar molecular weight was found for the photoactive beta gamma dimer obtained from the photoreaction center of Rhodopseudomonas sphaeroides strain 2.4.1 which, as a whole, had a molecular weight of 87 000. These results indicate that the photoreaction center from Rp. sphaeroides is an oligomer of the type alpha 1 beta 1 gamma 1. In contrast, the photoreaction center from Rs. rubrum appears to be dissociated, in solution, into a photoactive beta gamma dimer and a free polypeptide alpha.

Bacterial Proteins↗
PubMed1978

The Handicapped.

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Persons with Disabilities↗
PubMed1977

Evidence for monomeric bacteriochlorophyll in P800 of the photoreaction center from Rhodospirillum rubrum.

To find out whether weak or strong coupling exists between the bacteriochlorophyll molecules of the photoreaction center, the relative efficiency of energy transfer to P870 was measured at 795 nm and at 808 nm, at room temperature and at 77 degrees K. At room temperature, both relative efficiencies are close to 100%. However, at 77 degrees K, 795 nm light has a quantum efficiency of 76% and 808 nm light has an efficiency of 87%. These results confirm the fact that P800 is formed of at least one short wavelength component and one long wavelength component. Moreover, the short wavelength component is weakly coupled to both P870 and to the long wavelength component of P800. The conclusion is that the short wavelength component is due to monomeric bacteriochlorophyll. By comparison with other data, all four bacteriochlorophyll molecules of the photoreaction center are inferred to be monomeric.

Bacteriochlorophylls↗
PubMed1976

Photodichroic studies of the photoreaction center from Rhodospirillum rubrum. I. Attribution of P870 to two non parallel dipoles.

A randomly oriented sample of photoreaction center prepared from Rhodospirillum rubrum was excited at 77 degrees K by an actinic linearly polarized light of 870 nm. Under such conditions, only those chromophores with components of their absorption dipoles oriented parallel to the polarization of the actinic light are bleached. The change in absorbance at 900 nm of this photoselected sample was observed while varying the angle of polarization of a weak measuring light. The polarization of the absorbance change was thus evaluated as 0.25. This value is interpreted to mean that P870 is attributable to two absorption dipoles forming an angle included between 35.75 degrees and 90 degrees. Comparison with the p value of 0.5 obtained on a similar preparation by polarization of fluorescence (Ebrey, T. G. and Clayton, R.K. (1969) Photochem. Photobiol. 10, 109-117) leads to the conclusion that either these two dipoles emit fluorescence without being coupled by singlet-singlet energy transfer or that only one of them is a fluorescence emitter in the absence of reversible singlet-singlet energy transfer.

Cytochromes↗
PubMed1976

Design and evaluation of head unit for wheelchair control by quadriplegic patients.

A control unit was designed to allow persons who have lost hand and arm function to control the speed, steering, reversal and on-off switching of an electric wheelchair by means of backward movement and rotation of the head. When possible, shoulder movement was used to control both reversal and on-off switching. Clinical evaluation in 10 patients with quadriplegia and 2 with severe neuromuscular disease showed that the unit neither interfered with nor restrained the patients' residual body movements, permitted use of natural head movements for smooth and fast control of the wheelchair, and was well accepted by and integrated into the life of the patients.

Accident Prevention↗