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R Dudler

Publications and source records attributed to R Dudler.

35 records · Page 2Linked to original sources
PubMed1992

Structure of an mdr-like gene from Arabidopsis thaliana. Evolutionary implications.

Multidrug resistance of mammalian tumor cells is caused by the enhanced expression of P-glycoproteins. These proteins are encoded by mdr genes and mediate the energy-dependent efflux of a variety of lipophilic drugs from cells. To test whether in plants mdr-like genes might be involved in certain cases of cross-resistance to different herbicides, we have cloned and characterized a gene from Arabidopsis thaliana, atpgp1, encoding a putative P-glycoprotein homologue. Like the mammalian P-glycoproteins, with which it shares extensive sequence homology and a similar organization in structural domains, this protein is internally duplicated. Seven of the nine introns in the atpgp1 gene match introns in the mammalian mdr genes to within a few nucleotides, and the positions of these suggest that P-glycoprotein genes evolved by duplication and subsequent fusion of an intron-containing primordial gene prior to the evolutionary separation of plants and mammals. The atpgp1 gene gives rise to transcripts present in all plant parts but particularly abundant in inflorescence axes.

ATP Binding Cassette Transporter, Subfamily B, Mem↗
PubMed1991

Sequence and tissue-specific expression of a putative peroxidase gene from wheat (Triticum aestivum L.).

We have used a cDNA clone encoding a pathogen-induced putative wheat peroxidase to screen a genomic library of wheat (Triticum aestivum L. cv. Cheyenne) and isolated one positive clone, lambda POX1. Sequence analysis revealed that this clone contains a gene encoding a putative peroxidase with a calculated pI of 8.1 which exhibits 58% and 83% sequence identity to the amino acid sequence of the turnip (Brassica rapa) peroxidase and a pathogen-induced putative wheat peroxidase, respectively. The two introns in the wheat gene are at the same positions as introns in the peroxidase genes of tomato and horseradish. Results of S1-mapping experiments suggest that this gene is neither pathogen- nor wound-induced in leaves but is constitutively expressed in roots.

Amino Acid Sequence↗
PubMed1991

Cloning and sequencing of cDNAs encoding a pathogen-induced putative peroxidase of wheat (Triticum aestivum L.).

We report here the complete amino acid sequence of a pathogen-induced putative peroxidase from wheat (Triticum aestivum L.) as deduced from cDNA clones representing mRNA from leaves infected with the powdery mildew fungus Erysiphe graminis. The protein consists of 312 amino acids, of which the first 22 form a putative signal sequence, and has a calculated pI of 5.7. Sequence comparison revealed that the putative wheat peroxidase is most similar to the turnip (Brassica rapa) peroxidase, with which it shares 57% identical and 13% conserved amino acids.

Amino Acid Sequence↗
PubMed1990

The single-copy actin gene of Phytophthora megasperma encodes a protein considerably diverged from any other known actin.

This paper reports the cloning and sequencing of a Phytophthora megasperma actin gene. Sequence analysis revealed that the gene does not contain introns and encodes a putative actin protein remarkably diverged from any other known actins. Genomic Southern analysis indicates that there is a single actin gene per haploid genome, which is actively transcribed in vivo, as revealed by S1 mapping of the transcripts. The transcripts are heterogeneous in size because they have different 3' termini, none of which contains the conventional AATAAA polyadenylation signal.

Actins↗
PubMed1990

A mycoplasmal protein influences tumour cell invasiveness and contact inhibition in vitro.

Fab fragments of a monoclonal antibody directed against p37, a protein associated with the surface of FS9 mouse sarcoma cells, were previously found to inhibit the highly invasive behaviour of FS9 cells in vitro. We show that p37 originates from Mycoplasma hyorhinis. Infecting various cell lines with the mycoplasma consistently increased their invasiveness when confronted with chicken heart fibroblasts using Abercrombie's confronted explant technique. Conversely, removing the mycoplasmas or blocking p37 with specific Fab fragments reduced invasiveness. Analysis of individual cell collisions using time-lapse filming showed that the addition of Fab fragments to cells infected with M. hyorhinis greatly increased the level of contact inhibition. The antibody also reduced the invasiveness of transformed cells that did not express the p37 antigen. Hence, a cellular protein or proteins that are structurally related to p37 apparently influence invasive behavior.

Animals↗
PubMed1988

A mycoplasma high-affinity transport system and the in vitro invasiveness of mouse sarcoma cells.

FS9 mouse sarcoma cells were previously shown to be highly invasive when confronted with chicken heart fibroblasts using Abercrombie's confronted explant technique. This invasion could be inhibited by addition to the assay of Fab fragments of a monoclonal antibody directed against p37, a protein associated with the surface of FS9 cells. We have cloned and sequenced the gene for p37. We show that it originates from Mycoplasma hyorhinis and that UGA is a tryptophan codon in this organism. We present evidence that the p37 gene is part of an operon encoding two additional proteins which are highly similar to components of the periplasmic binding-protein-dependent transport systems of Gram-negative bacteria, and we suggest that p37 is part of a homologous, high-affinity transport system in M. hyorhinis, a Gram-positive bacterium. We discuss the influence of p37 and M. hyorhinis on contact inhibition of locomotion of mammalian cells.

Amino Acid Sequence↗
PubMed1988

Evidence for high affinity binding-protein dependent transport systems in gram-positive bacteria and in Mycoplasma.

Gram-negative bacteria are surrounded by two membranes. In these bacteria, a class of high affinity transport systems for concentrating substrates from the medium into the cell, involves a binding protein located between the outer and inner membranes, in the periplasmic region. These 'periplasmic binding-proteins' are thought to bind the substrate in the vicinity of the inner membrane, and to transfer it to a complex of inner membrane proteins for concentration into the cytoplasm. We report evidence leading us to propose that a Gram-positive bacterium, Streptococcus pneumoniae, and a mycoplasma, Mycoplasma hyorhinis, which are surrounded by a single membrane and have therefore no periplasmic region, possess an equivalent to the high affinity periplasmic binding-protein dependent transport systems, i.e. extra-cytoplasmic binding lipoprotein dependent transport systems. The 'binding lipoproteins' would be maintained at proximity of the inner membrane by insertion of their N-terminal glyceride-cysteine into this membrane.

Amino Acid Sequence↗
PubMed1984

Upstream elements necessary for optimal function of the hsp 70 promoter in transformed flies.

Deletion mutants of the Drosophila hsp 70 promoter region have been fused to a truncated Drosophila Adh gene lacking its own promoter. These fusion genes were introduced into the Drosophila genome using the P-element transformation system. S1 mapping of fusion transcripts in transformed flies shows that their expression is completely dependent on the function of the hsp 70 promoter, and that 97 bp of hsp 70 5'-flanking DNA is sufficient to induce transcription upon heat shock to a level similar to that of the wild-type hsp 70 gene. By contrast, a deletion containing 68 bp of 5'-flanking DNA is only inducible to a low level even though this deletion retains the consensus sequence, which is sufficient for induction and maximal expression of this gene in COS cells and Xenopus oocytes. A sequence centered at -125 with the potential for forming an S1 nuclease-sensitive structure does not affect inducibility or efficiency of expression.

Alcohol Dehydrogenase↗
PubMed1983

The genes coding for 4 snRNAs of Drosophila melanogaster: localization and determination of gene numbers.

Four small nuclear RNAs (snRNAs) have been isolated from Drosophila melanogaster flies. They have been characterized by base analysis, fingerprinting, and injection into Axolotl oocytes. The size of the molecules and the modified base composition suggest that the following correlations can be made: snRNA1 approximately U2-snRNA; snRNA2 approximately U3-snRNA; snRNA3 approximately U4-snRNA; snRNA4 approximately U6-snRNA. The snRNAs injected into Axolotl oocytes move into the nuclei, where they are protected from degradation. The genes coding for these snRNAs have been localized by "in situ" hybridization of 125-I-snRNAs to salivary gland chromosomes. Most of the snRNAs hybridize to different regions of the genome: snRNA1 to the cytological regions 39B and 40AB; snRNA2 to 22A, 82E, and 95C; snRNA3 to 14B, 23D, 34A, 35EF, 39B, and 63A; snRNA4 to 96A. The estimated gene numbers (Southern-blot analysis) are: snRNA1:3; snRNA2:7; snRNA3:7; snRNA4:1-3. The gene numbers correspond to the number of sites labeled on the polytene salivary gland chromosomes.

Ambystoma↗
PubMed1981

The genes coding for tRNA Tyr of Drosophila melanogaster: localization of determination of the gene numbers.

Transfer RNA(Tyr) (anticodon G psi A) was isolated from Drosophila melanogaster by means of Sepharose 4B, RPC-5, and polyacrylamide gel electrophoresis. The rRNA was iodinated in vitro with Na125 I and hybridized in situ to salivary gland chromosomes from Drosophila. The genes of rRNA(Tyr) were localized in eight regions of the genome by autoradiography. Restriction enzyme analysis of genomic DNA indicated that the haploid Drosophila genome codes for about 23 tRNA(Tyr) genes. The regions 22F and 85A each contain four to five tRNA(Tyr) genes, whereas the regions 28C, 41AB, 42A, 42E, and 56D each contain two to three tRNA(Tyr) genes.

Animals↗
PubMed1980

Transfer RNA genes of Drosophila melanogaster.

Three recombinant plasmids containing randomly sheared genomic D. melanogaster tRNAs have been identified and characterized in detail. One of these, the plasmid 14C4, has a D. melanogaster (Dm) DNA segment of 18 kb, and has three tRNA2Arg and two tRNAAsN genes. The second plasmid, 38B10, has tRNAHis genes, while the third plasmid, 63H5, contains coding sequences for tRNA2Asp. The Dm DNA segments in each recombinant plasmid are derived from unique cytogenetic loci. 14C4 is from 84 F, 38B10 is from 48 F and 63H5 is from 70 A.

Animals↗
PubMedDate not supplied

A pathogen-induced wheat gene encodes a protein homologous to glutathione-S-transferases.

Winter wheat (Triticum aestivum) shows local, induced resistance against the plant-pathogenic fungus Erysiphe graminis f. sp. tritici following exposure to the nonpathogen E. g. f. sp. hordei. The onset of this resistance has been shown to be correlated with the activation of putative defense genes, and cDNA clones representing transcripts of induced genes have been obtained (P. Schweizer, W. Hunziker, and E. Mösinger, Plant Molecular Biology 12:643-654, 1989). We have cloned and sequenced a gene corresponding to one of these cDNAs, WIR5. Sequence analysis indicated that this gene contains three exons and encodes a protein of 229 amino acids. S1 mapping showed that transcripts homologous to this gene are at least 20 times more abundant in leaves infected 14 hr earlier with E. g. f. sp. hordei than in control leaves. Sequence comparison showed that the WIR5 gene product is highly homologous to glutathione-S-transferases (GSTs; EC 25.1.18) of maize. This, together with the fact that the intron positions of both the wheat gene and the maize GSTI gene are conserved, suggests that the cloned pathogen-induced gene, named GstA1, encodes a wheat glutathione-S-transferase.

Amino Acid Sequence↗
PubMedDate not supplied

Sequence and expression of a wheat gene that encodes a novel protein associated with pathogen defense.

Wheat (Triticum aestivum) exhibits local acquired resistance to the powdery mildew pathogen Erysiphe graminis f. sp. tritici. The resistant state can be induced by a preinoculation with the nonhost pathogen E. g.f. sp. hordei, the barley powdery mildew, and is accompanied by the activation of putative defense genes. Here, we report the sequence of a pathogen-induced gene, WIR1a, and a corresponding cDNA, WIR1, that encode novel defense-related proteins of 88 and 85 amino acids, respectively. Analysis of the primary structure of these proteins predicts them to be integral membrane proteins with extracytoplasmic C-terminal domains rich in proline and glycine, through which the proteins possibly interact with the cell wall.

Amino Acid Sequence↗