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B Suter

Publications and source records attributed to B Suter.

At least 19 recordsLinked to original sources
PubMed1995

The Drosophila melanogaster homolog of the mammalian MAPK-activated protein kinase-2 (MAPKAPK-2) lacks a proline-rich N-terminus.

Recently, a mammalian kinase cascade was discovered that is triggered by stress and heat shock, and leads to the stimulation of mitogen-activated protein kinase (MAPK)-activated protein kinase-2 (MAPKAPK-2). Surprisingly, this process turns out to be independent of the classical MAPK. The stress-induced activation of MAPKAPK-2, in turn, results in the phosphorylation of small heat-shock proteins (Hsp). We have isolated a Drosophila melanogaster (Dm) cDNA encoding a polypeptide that has extensive sequence similarity to the mammalian MAPKAPK-2. As in mammalian MAPKAPK-2, the Dm MAPKAPK-2 possesses a MAPK phosphorylation site and a nuclear targeting sequence located C-terminal to the catalytic domain. However, in contrast to its mammalian counterpart, it lacks the Pro-rich N-terminal region proposed to form Src-homology domain 3 (SH3) binding domains. A 2.4-kb MAPKAPK-2 message is expressed throughout development, while two shorter transcripts of 2.3 and 1.8 kb appear to be specifically expressed in the germline. The 1.8-kb transcript results from the usage of an atypical germline-specific polyadenylation signal (AATATA) located early within the 3' untranslated region. Dm MAPKAPK-2 is located at cytological position 5D in the Dm genome.

Amino Acid Sequence↗
PubMed1995

Cloning of the cDNA encoding the porcine p55 tumor necrosis factor receptor.

We have utilized RT-PCR to clone the porcine p55TNFR cDNA, encoding the 55-kDa tumor necrosis factor receptor (TNFR), encompassing the entire coding region and most of the 3' untranslated region. PCR was performed using total cellular RNA of porcine kidney cell line 15 [PK(15)] and primers for the human p55TNFR. Since the length of the entire fragment was over 2000 bp, we fused two amplified subfragments with the help of a restriction endonuclease. The entire fragment was cloned and its amino acid (aa) sequence was compared to the human, rat and mouse p55TNFR. This comparison revealed identities of 79, 71 and 72%, respectively. The highest identities of 90, 80 and 85% were detected in the so called "death domain" for the human, rat and mouse sequences, respectively. This domain is crucial for the cytotoxic signal transduction of p55TNFR.

Amino Acid Sequence↗
PubMed1995

Molecular cloning of the Drosophila homologue of the rat ribosomal protein L11 gene.

We report the isolation of the Drosophila melanogaster homologue of the rat ribosomal protein L11 gene. The gene is present in the Drosophila genome at polytene chromosome location 56D, on the right arm of the second chromosome. The Drosophila DL11 gene appears to encode two messages of 0.8 and 0.9 kb which are expressed throughout development with variations in their relative abundance. DL11 codes for a predicted protein of 184 amino acids with a molecular mass of 21.1 kDa.

Amino Acid Sequence↗
PubMed1994

Null alleles reveal novel requirements for Bic-D during Drosophila oogenesis and zygotic development.

In the Drosophila ovary, the Bicaudal-D (Bic-D) gene is required for the differentiation of one of 16 interconnected cystocyte sister cells into an oocyte. A new class of Bic-Dnull alleles reveals a novel requirement for Bic-D for zygotic viability. In the germ line, the null mutations show that developmental processes that take place in germarial region 1, even those that create asymmetry, are independent of Bic-D function. Bic-D is then required to establish oocyte identity in one cystocyte and is essential, not only for the oocyte-specific accumulation of all oocyte markers that we have tested so far, but also for the posterior migration of the oocyte. In addition, normal polarity amongst the nurse cells requires Bic-D, indicating that the creation of different nurse cell identities may depend on oocyte determination. Our results show that different processes in early oogenesis require different amounts of Bic-D in a process-specific way and certain later processes can proceed at low levels of Bic-D. This suggests that the patterning of the female germ line and the development of an oocyte depend on differential responses to a single activity that is capable of initiating distinct oogenesis processes and can establish different cell fates.

Alleles↗
PubMed1994

[Does acupuncture modify skin circulation via the autonomic nervous system?].

It has been postulated and there are indications that acupuncture affects the cardiovascular system via the autonomic nervous system. The blood vessels of the hand skin have sympathetic constrictor nerves only. Therefore, the possible effect of acupuncture on the ANS can be investigated by measurements of microvascular perfusion and thermoregulation of the hands. Knowing the physiological effects of acupuncture may help to improve acceptance of this unconventional medical approach.

Acupuncture Therapy↗
PubMed1991

Requirement for phosphorylation and localization of the Bicaudal-D protein in Drosophila oocyte differentiation.

In the Drosophila female the product of the germline stem cell, the cystoblast, gives rise to 16 interconnected cystocytes. One of them differentiates into the oocyte, while the 15 others become polyploid nurse cells. Bic-D is required for the differentiation of an oocyte and hence for fertility. Recessive mutations in Bic-D block the oocyte-specific accumulation of its own and other RNAs. Based on its properties and distribution, the Bic-D protein appears to be a component of a cytoskeletal transport or anchoring system. Additional results suggest that the phosphorylation of the Bic-D protein is essential for its accumulation in the pro-oocyte and that this process leads to the gradual localization to the pro-oocyte of factors required for oocyte differentiation.

Alleles↗
PubMed1989

Bicaudal-D, a Drosophila gene involved in developmental asymmetry: localized transcript accumulation in ovaries and sequence similarity to myosin heavy chain tail domains.

The Bicaudal-D (Bic-D) gene is essential for the differentiation of the oocyte in Drosophila. Dominant gain-of-function mutations result in the formation of double abdomen embryos. The Bic-D gene was cloned and identified using restriction fragment length polymorphisms, Northern analysis, and transformation rescue. Bic-D RNA accumulates in the oocyte during the earliest stages of oogenesis and is localized anteriorly in later stages. The predicted protein contains several extended amphipathic helices, and its similarity to myosin heavy chain tails, paramyosin, and kinesin suggests a similar type of coiled-coil protein interaction.

Amino Acid Sequence↗
PubMed1988

Identification of an amber nonsense mutation in the rosy516 gene by germline transformation of an amber suppressor tRNA gene.

Seven xanthine dehydrogenase and cross-reacting material negative Drosophila melanogaster rosy stocks were screened for amber and ochre nonsense mutations. Amber and ochre nonsense suppressors were created by site-directed mutagenesis starting from a wild-type tRNA(Tyr) gene. The suppressor tRNA genes were subcloned into a pUChsneo transformation vector providing heat-shock controlled neomycin resistance. The seven rosy stocks were germline transformed with amber and ochre tDNA(Tyr), and the G1 generation was screened for Geneticin resistance. Surviving rosy516 flies transformed with the amber suppressor showed an eye colour intermediate between the original ry516 stock and the wild-type, suggesting that ry516 is an amber nonsense mutant. This was confirmed by sequencing the relevant part of the ry516 gene; the analysis revealed a C-to-T transition in a CAG glutamine codon at nucleotide 1522 of the wild-type rosy gene.

Animals↗
PubMed1988

tRNA(Tyr) genes of Drosophila melanogaster: expression of single-copy genes studied by S1 mapping.

Six Drosophila melanogaster tRNA(Tyr) genes have been isolated and sequenced. They contained introns of different sequences and two size classes: 20 or 21 base pairs (bp) (five genes) and 113 bp (one gene). However, the sequences coding for the mature tRNA(Tyr) were identical in all six genes. The 113-bp intron-containing gene was a single-copy gene. Hence, its primary transcript could be traced by S1 mapping. The gene was turned on during embryogenesis and continually expressed to various degrees during the following developmental stages. Thus, S1 mapping is a feasible method to follow the transcriptional activity of individual genes with identical mature products, provided that their primary transcripts are unique. The six genes were organized in two clusters of three and two genes, respectively (each containing a 20- or a 21-bp intron; cytological localization, 85A), and a single-copy gene (113-bp intron; cytological localization, 28C). We show that four of the six tRNA(Tyr) genes characterized were localized in putative 5' control regions of developmentally controlled genes transcribed by polymerase II.

Animals↗
PubMed1988

Pseudouridine modification in the tRNA(Tyr) anticodon is dependent on the presence, but independent of the size and sequence, of the intron in eucaryotic tRNA(Tyr) genes.

In Saccharomyces cerevisiae, pseudouridine formation in the middle position of the tRNA(Tyr) anticodon (psi 35) is dependent on the presence of the intron in the tRNA(Tyr) gene (Johnson and Abelson, Nature 302:681-687, 1983). Drosophila melanogaster tRNA(Tyr) genes contain introns of three size classes: 20 or 21 base pairs (bp) (six genes), 48 bp (one gene), and 113 bp (one gene). As in yeast, removal of the intron led to loss of psi 35 in the anticodon when transcription was assayed in Xenopus laevis oocytes. All Drosophila intron sizes supported psi 35 formation. The same results were obtained with the homologous X. laevis tRNA(Tyr) genes containing introns of 12 or 13 bp or with a deleted intron. The introns of yeast (Nishikura and DeRobertis, J. Mol. Biol. 145:405-420, 1981), D. melanogaster, and X. laevis tRNA(Tyr) wild-type genes, while they all supported psi 35 synthesis, did not share any consensus sequences. As discussed, these results, taken together, suggest that for appropriate function the psi 35 enzyme in the X. laevis oocyte needs the presence of an unqualified intron in the tRNA gene and a tRNA(Tyr)-like structure in the unprocessed tRNA precursor.

Animals↗
PubMed1986

The nucleotide sequence of two homogeneic Drosophila melanogaster tRNATyr isoacceptors: application of a rapid tRNA anticodon sequencing method using S-1 nuclease.

The nucleotide sequence of the two major Drosophila melanogaster tRNATyr isoacceptors was determined to be pC-C-U-U-C-G-A-U-A-m2G-C-U-C-A-G-D-D-G-G-acp3 U-A-G-A-G-C-m2(2)G-G-psi-G-G-A-C-U-G/Q-psi-A-m1G-A-Um-C-C-A-U-A-G-m7 G-D-C-G-C-U-G-G-U(T)-psi-C-A-m1A-A-U-C-C-G-G-C-U-C-G-A-A-G-G-A-A-C-C-AOH . The two isoacceptors differ by the presence of a G or a Q in the wobble position. Both contain a partial modification in position 54 (U/T). Thus, these tRNAs are transcribed from a single gene (or many genes with identical sequences). A fast and sensitive postlabeling method for sequencing tRNA anticodons is described. Nuclease S-1-treated tRNA is labeled with 5[32P]-pCp using T-4 RNA ligase. The tRNA fragments are then separated on 7 M urea/20% PAA gels. After autoradiography the RNA is eluted and digested with T-2 RNase. The nature of the labeled nucleotides is determined by two-dimensional thin-layer chromatography. The same method can be used to determine the 5' sequence of a tRNA by 3' labeling 5' tRNA halves with 5[32P]-pCp and subsequent chemical sequencing.

Animals↗
PubMed1985

Queuosine modification of the wobble base in tRNAHis influences 'in vivo' decoding properties.

The 'in vivo' decoding properties of four tRNAHis isoacceptors, two from Drosophila melanogaster and two from brewer's yeast, were studied after their microinjection, along with turnip yellow mosaic virus (TYMV) coat protein mRNA, into Xenopus laevis oocytes. The two Drosophila isoacceptors are identical besides containing either a guanosine (G) or the hypermodified nucleoside queuosine (Q) in the wobble position. The brewer's yeast isoacceptors differ by four bases in the anticodon stem, and by one base in the amino acceptor stem. Our results show that, under competing 'in vivo' conditions, the Drosophila tRNAHis with the anticodon GUG clearly prefers the histidine codon CAC to the codon CAU, whereas little preference is observed for the tRNAHis with the anticodon QUG for the codon CAU, and no preference for either codon by the two yeast isoacceptors. Hence, it can be concluded that the presence of the Q-base clearly affects the choice of the codon. This is the first demonstration of an 'in vivo' codon preference by tRNA isoacceptors differing in the modification of the wobble base during the elongation step of protein synthesis. These results imply that one function of the Q-base is at the translational level.

Animals↗
PubMed1982

[Is the aorto-coronary bypass operation useful in patients with advanced coronary sclerosis and poor ventricular function?].

The prognosis and long term results in 56 patients with coronary artery disease and impaired left ventricular function (EF less than or equal to 40%) who underwent aortocoronary bypass surgery (all cases) and aneurysmectomy (26 cases) between 1972 and 1980 were compared with those in 47 equally ill patients treated medically. Survival was significantly higher in the surgical than in the non-surgical group, the survival rate being 80% and 58% respectively at 41 months after study entry (p = 0.012). No difference in survival was observed between grafted patients and patients in whom additional aneurysmectomy was performed. 26 patients were recatheterized postoperatively and this revealed an increase in left ventricular ejection fraction at rest from 33 +/- 5% to 44 +/- 11% (p less than 0.001) and a decrease in left ventricular end-diastolic pressure from 18 +/- 8 mm Hg to 14 +/- 8 mm Hg (p less than 0.025). Postoperatively the patients had less angina and physical working capacity increased. At restudy the average NYHA class had decreased in the surgical group from 2.9 +/- 0.7 to 2.1 +/- 0.9 (p less than 0.001) but was unchanged in the non-surgical group (2.6 +/- 0.6 and 2.6 +/- 0.7 respectively). It is concluded that aortocoronary bypass surgery improves survival, left ventricular function and symptoms in patients with coronary artery disease and severely impaired myocardial function.

Adult↗