TY - JOUR
A1 - Flügge, U. I.
A1 - Fischer, K.
A1 - Gross, A.
A1 - Sebald, Walter
A1 - Lottspeich, F.
A1 - Eckerskorn, C.
T1 - The triose phosphate-3-phosphoglycerate-phosphate translocator from spinach chloroplasts: nucleotide sequence of a full-length cDNA clone and import of the in vitro synthesized precursor protein into chloroplasts
N2 - No abstract available
KW - Biochemie
Y1 - 1989
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62559
ER -
TY - JOUR
A1 - Gessler, Manfred
A1 - Bruns, G. A. P.
T1 - A physical map around the WAGR complex on the short arm of chromosome 11
N2 - A long-range restriction map of part of the short arm of ehromosome 11 including the WAGR region has been constructed using pulsed-field gel electrophoresis and a number of infrequently cutting restriction enzymes. A total of 15.4 Mbp has been mapped in detall, extending from proximal 11p14 to the distal part of 11p12. The map localizes 35 different DNA probes and reveals at least nine areas with features eharaeteristle of BTF islands, some of which may be candidates for the different loci underlying the phenotype of the WAGR syndrome. This map will furthermore allow screening of DNA from individuals with WAGR-related phenotypes and from Wilms tumors for associated chromosomal rearrangements.
KW - Biochemie
Y1 - 1989
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-59246
ER -
TY - JOUR
A1 - Gessler, Manfred
A1 - Thomas, G. H.
A1 - Couillin, P.
A1 - Junien, C.
A1 - McGillivray, B. C.
A1 - Hayden, M.
A1 - Jaschek, G.
A1 - Bruns, G. A.
T1 - A deletion map of the WAGR region on chromosome II
N2 - The WAGR (Wilms tumor, aniridia, genitourinary anomalies, and mental retardation) region has been assigned to chromosome 11p13 on the basis of overlapping constitutional deletions found in affected individuals. We have utilized 31 DNA probes which map to the WAGR deletion region, together with six reference loci and 13 WAGR-related deletions, to subdivide this area into 16 intervals. Specific intervals have been correlated with phenotypic features, leading to the identification of individual subregions for the aniridia and Wilms tumor loci. Delineation, by specific probes, of multiple intervals above and below the critical region and of five intervals within the overlap area provides a framework map for molecular characterization of WAGR gene loci and of deletion boundary regions.
KW - Biochemie
Y1 - 1989
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-59255
ER -
TY - JOUR
A1 - Gessler, Manfred
A1 - Bruns, Gail A. P.
T1 - Molecular mapping and cloning of the breakpoints of a chromosome 11p14.1-p13 deletion associated with the AGR syndrome
N2 - Chromosome 11p13 is frequently rearranged in individuals with the WAGR syndrome (Wilms tumor, aniridia, genitourinary anomalies, and mental retardation) or parts of this syndrome. To map the cytogenetic aberrations molecularly, we screened DNA from cell Unes with known WAGR-related chromosome abnormalities for rearrangements with pulsed fleld gel (PFG) analysis using probes deleted from one chromosome 11 homolog of a WAGR patient. The first alteration was detected in a cell line from an individual with aniridia, genitourinary anomalies, mental retardation, and a deletion described as 11p14.1-p13. We have located one breakpoint close to probe HU11-164B and we have cloned both breakpoint sites as well as the junctional fragment. The breakpoints subdivide current intervals on the genetic map, and the probes for both sides will serve as important additional markers for a long-range restriction map of this region. Further characterization and sequencing of the breakpoints may yield insight into the mechanisms by which these deletions occur.
KW - Biochemie
Y1 - 1988
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-59264
ER -
TY - JOUR
A1 - Kleene, R.
A1 - Pfanner, N.
A1 - Pfaller, R.
A1 - Link, T. A.
A1 - Sebald, Walter
A1 - Neupert, W.
A1 - Tropschug, M.
T1 - Mitochondrial porin of Neurospora crassa: cDNA cloning, in vitro expression and import into mitochondria
N2 - No abstract available
KW - Biochemie
Y1 - 1987
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62566
ER -
TY - JOUR
A1 - Römisch, J.
A1 - Tropschug, M.
A1 - Sebald, Walter
A1 - Weiss, H.
T1 - The primary structure of cytochrome c\(_1\) from Neurospora crassa
N2 - No abstract available
KW - Biochemie
Y1 - 1987
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62578
ER -
TY - JOUR
A1 - Barnekow, Angelika
A1 - Gessler, Manfred
T1 - Activation of the pp60\(^{c-src}\) kinase during differentiation of monomyelocytic cells in vitro
N2 - Tbe proto-oncogene c-src, the cellular homolog of the Rous sarcoma virus (RSV) transforming gene v-src, is expressed in a tissue-specific and age-dependent manner. Its physiological function, although still unknown, appears to be more closely related to differentiation processes than to proliferation processes. To obtain more information about the physiological role of the c-src gene in cells, we have studied differentiation-dependent alterations using the human HL-60 leukaemia cell line as a model system. Induction of monocytic and granulocytic differentiation of HL-60 cells by 12-0-tetradecanoylphorbol-13-acetate (TPA) and dimethylsulfoxide (DMSO) is associated with an activation of the pp60c-src tyrosine kinase, but not with increased c-src gene expression. Control experiments exclude an interaction of TPA and DMSO themselves with the pp60c-src kinase.
KW - Biochemie
KW - c-src
KW - differentiation
KW - protein tyrosine kinase
KW - protooncogene
Y1 - 1986
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-59278
ER -
TY - JOUR
A1 - Weich, H. A.
A1 - Sebald, Walter
A1 - Schairer, H. U.
A1 - Hoppe, J.
T1 - The human osteosarcoma cell line U-2 OS expresses a 3.8 kilobase mRNA which codes for the sequence of the PDGF-B chain
N2 - A cDNA clone of about 2500 basepairswas prepared from the human osteosarcoma cellline U-2 OS by hybridizing with a v-sis probe. Sequence analysis showed that this cDNA contains the coding region for the PDGF-B chain. Here we report that the mitogen secreted by these osteosarcoma cells contains the PDGF-B chain and is probably a homodimer of two B-chains.
KW - Biochemie
KW - Platelet-derived growthfactor
KW - cDNA
KW - Oncogene
KW - Tumor cell
Y1 - 1986
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62588
ER -
TY - JOUR
A1 - Hoppe, J.
A1 - Gatti, D.
A1 - Weber, H.
A1 - Sebald, Walter
T1 - Labeling of individual amino acid residues in the membrane-embedded F\(_0\) part of the F\(_1\) F\(_0\) ATP synthase from Neurospora crassa. Influence of oligomycin and dicyclohexylcarbodiimide
N2 - Three F0 subunits and the F\(_1\) subunit P of the ATP synthase from Neurospora crassa were labeled with the lipophilic photoactivatable reagent 3-(trifluoromethyl)-3-(m-[\(^{125}\)I]iodophenyl)diazirine ([\(^{125}\)I]TID). In the proteolipid subunit which was the most heavily labeled polypeptide labeling was confmed to five residues at the NH2-terminus and five residues at the C-terminus ofthe protein. Labeling occurred at similar positions compared with the homologaus protein (subunit c) in the ATP synthase from Escherichia coli, indicating a similar structure of the proteolipid subunits in their respective organisms. The inhibitors oligomycin and dicyclohexylcarbodiimide did not change the pattern of accessible surface residues in the proteolipid, suggesting that neither inhibitor induces gross conformational changes. However, in the presence of oligomycin, the extent oflabeling in some residues was reduced. Apparently, these residues provide part of the binding site for the inhibitor. After reaction with dicyclohexylcarbodiimide an additional labeled amino acid was found at position 65 corresponding to the invariant carbodümide-binding glutamic acid. These results and previous observations indicate that the carboxyl side chain of Glu-65 is located at the protein-lipid interphase. The idea is discussed that proton translocation occurs at the interphase between different types if F\(_0\) subunits. Dicyclohexylcarbodiimide or oligomycin might disturb this essential interaction between the F\(_0\) subunits.
KW - Biochemie
Y1 - 1986
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62598
ER -
TY - JOUR
A1 - Hoppe, J.
A1 - Sebald, Walter
T1 - Topological studies suggest that the pathway of the protons through F\(_0\) is provided by amino acid residues accessible from the lipid phase
N2 - The structure of the F0 part of ATP synthases from E. coli and Neurospora crassa was analyzed by hydrophobic surface labeling with [125I]TID. In the E. co/i F0 all three subunits were freely accessible to the reagent, suggesting that these subunits are independently integrated in the membrane. Labeted amino acid residues were identified by Edman degradation of the dicyclohexylcarbodiimide binding (DCCD) proteins from E. coli and Neurospora crassa. The very similar patterns obtained with the two homologaus proteins suggested the existence of tightly packed cx-helices. The oligomeric structure of the DCCD binding protein appeared to be very rigid since little, if any, change in the labeling patternwas observed upon addition of oligomycin or DCCD to membranes from Neurospora crassa. When membrancs were pretrcated with DCCD prior to the reaction with [125I]TID an additionally labeled amino acid appeared at the position of Glu·65 which binds DCCD covalently, indicating the Jocation of this inhibitor on the outside of the oligomer. It is suggested that proton conduction occurs at the surface of the oligomer of the DCCD binding protein. Possibly this oligomer rotates against the subunit a or b and thus enables proton translocation. Conserved residues in subunit a, probably located in the Iipid bilayer, might participate in the pro· ton translocation mechanism.
N2 - La structure de la partie F0 de l'ATP synthase a ete analysee au moyen de marquage par /e reactif hydrophobe TJD[125 I]. Les trois sous-unites de E. coli F0 sont accessibles au reactif ce qui semble indiquer que ces sous-unites sont integrees dans Ia membrane defaron independante. Les amino-acides marques ont ete identifies par Ia degradation d'Edman des profeines d'E. coli et de Neurospora associees au dicyclohexylcarbodiimide (DCCD). L 'analogie des courbes obtenues pour /es deux proteines homologues suggere l'existence d'a-helices rangees de faron serree. La structure oligomerique de Ia proreine associee au DCCD semble etre tres rigide puisque pratiquement aucun changement dans /e marquage n 'a ete observe par addition d'oligomycine ou de DCCD aux membranes de Neurospora crassa. Quand /es membranes sont traitees avec /e DCCD avant Ia reaction avec TJD[125 I], un amino-acide additionnellement marque apparait a Ia position Glu·65 et forme avec le DCCD une Iiaison covalente. Ce dernier resu/tat indique Ia localisation de cet inhibiteur a /'exterieur de J'oligo· mere. II semble donc que Ia conduction des protons ait lieu a Ia surface de /'oligomere de Ia proteine associee au DCCD. II serait possib/e que l'o/igomere se retourne contre Ia sous-unite a ou b, permettunt de ce fait Ia translocation des protons. Les residus conserves de Ia sous-unite a, probab/ement Jocalises dans Ia double couche lipidique, pourraient participer au mecanisme de translocation des protons.
KW - Biochemie
KW - conduction de protons
KW - proteines membranaires
KW - carbenes
KW - proton conduction
KW - membrane proteins
KW - carbenes
Y1 - 1986
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62602
ER -
TY - JOUR
A1 - Gabellini, N.
A1 - Sebald, Walter
T1 - Nucleotide sequence and transcription of the fbc operon from Rhodopseudomonas sphaeroides. Evaluation of the deduced amino acid sequences of the FeS protein, cytochrome b and cytochrome c\(_1\)
N2 - No abstract available
KW - Biochemie
Y1 - 1986
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62615
ER -
TY - JOUR
A1 - McCarthy, J. E.
A1 - Sebald, Walter
A1 - Gross, G.
A1 - Lammers, R.
T1 - Enhancement of translational efficiency by the Escherichia coli atpE translational initiation region: its fusion with two human genes
N2 - No abstract available
KW - Biochemie
Y1 - 1986
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62626
ER -
TY - JOUR
A1 - Harnisch, U.
A1 - Weiss, H.
A1 - Sebald, Walter
T1 - The primary structure of the iron-sulfur subunit of ubiquinol-cytochrome c reductase from Neurospora, determined by cDNA and gene sequencing
N2 - No abstract available
KW - Biochemie
Y1 - 1985
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62631
ER -
TY - JOUR
A1 - Gabellini, N.
A1 - Harnisch, U.
A1 - McCarthy, J. E.
A1 - Hauska, G.
A1 - Sebald, Walter
T1 - Cloning and expression of the fbc operon encoding the FeS protein, cytochrome b and cytochrome c\(_1\) from the Rhodopseudomonas sphaeroides b/c\(_1\) complex
N2 - The gene for the FeS protein of the Rhodopseudomonas sphaeroides b/c1 complex was identified by means of crosshybridization with a segment of the gene encoding the corresponding FeS protein of Neurospora crassa. Plasmids (pRSF1-14) containing the cross-hybridizing region, covering in total 13.5 kb of chromosomal DNA, were expressed in vitro in a homologous system. One RSF plasmid directed the synthesis of all three main polypeptides of the R. sphaeroides blc1 complex: the FeS protein, cytochrome b and cytochrome c1• The FeS protein and cytochrome c1 were apparently synthesized as precursor fonns. None of the pRSF plasmids directed the synthesis of the 10-kd polypeptide found in b/c1 complex preparations. Partial sequencing of the cloned region was performed. Several sites of strong homology between R. sphaeroides and eukaryotic polypeptides of the b/c1 complex were identified. The genes encode the three b/c1 polypeptides in the order: (5') FeS protein, cytochrome b, cytochrome c1• The three genes are transcribed to give a polycistronic mRNA of 2.9 kb. This transcriptional unit has been designated the jbc operon; its coding capacity corresponds to the size of the polycistronic mRNA assuming that only the genes for the FeS protein (jbcF), cytochrome b (jbcß) and cytochrome c1 (jbcC) are present. This could indicate that these three subunits constitute the minimal catalytic unit of the b/c1 complex from photosynthetic membranes.
KW - Biochemie
KW - R. sphaeroidesl
KW - b/c1 complex
KW - gene
KW - cloning
KW - in vitro expression
KW - polycistronic mRNA
Y1 - 1985
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62642
ER -
TY - JOUR
A1 - McCarthy, J. E.
A1 - Schairer, H. U.
A1 - Sebald, Walter
T1 - Translational initiation frequency of atp genes from Escherichia coli: identification of an intercistronic sequence that enhances translation
N2 - The c, b and ö subunit genes of the Escherichia coli atp operon were cloned individually in an expression vector between the tac fusion promoter and the galK gene. The relative rates of subunit synthesis directed by the cloned genes were similar in vitro andin vivo and compared favourably with the subunit stoichiometry of the assembled proton-translocating A TP synthase of E. coli in vivo. The rate of synthesis of subunit c was at least six times that of subunit b and 18 times that of subunit ö. Progressive shortening of the long intercistronic sequence lying upstream of the subunit c gene showed that maximal expression of this gene is dependent upon the presence of a sequence stretching > 20 bp upstream of the Shine-Dalgarno site. This sequence thus acts to enhance the rate of translational initiation. The possibility that similar sequences might perform the same function in other operons of E. coli and bacteriophage A is also discussed. Translation of the subunit b cistron is partially coupled to translation of the preceding subunit c cistron. In conclusion, the expression of all the atp operon genes could be adjusted to accommodate the subunit requirements of A TP synthase assembly primarily by means of mechanisms which control the efficiency of translational initiation and re-initiation at the respective cistron start codons.
KW - Biochemie
KW - E. coli atp operon
KW - subunit stoichiometry
KW - in vitro and in vivo expression
KW - translational initiation
Y1 - 1985
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62657
ER -
TY - JOUR
A1 - Lindenmaier, W.
A1 - Dittmar, K. E.
A1 - Hauser, H.
A1 - Necker, A.
A1 - Sebald, Walter
T1 - Isolation of a functional human interleukin 2 gene from a cosmid library by recombination in vivo
N2 - A method has been developed that allows the isolation of genomic clones from a cosmid library by homologaus recombination in vivo. This method was used to isolate a human genomic interleukin 2 (IL2) gene. The genomic cosmid library was packaged in vivo into A. phage particles. A recombination-proficient host strain carrying IL2 cDNA sequences in a non-homologaus plasmid vector was infected by the packaged cosmid library. After in vivo packaging and reinfection, recombinants carrying the antibiotic resistance genes of both vectors were selected. From a recombinant cosmid clone the chromosomal IL2 genewas restored. After DNA mediated gene transfer into mouse Ltk- cells human IL2 was expressed constitutively.
KW - Biochemie
KW - Recombinant DNA
KW - DNA mediated gene transfer
KW - expression plasmid
KW - screening
KW - packaging
KW - bacteriophage lambda
Y1 - 1985
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62662
ER -
TY - JOUR
A1 - Gessler, Manfred
A1 - Barnekow, Angelika
T1 - Differential expression of the cellular oncogenes c-src and c-yes in embryonal and adult chicken tissues
N2 - The cellular onc-genes c-src and c-yes are expressed very differently during chicken embryonic development. The c-src mRNA and its translational product are detectable at high levels in brain extracts of chicken embryos and adult chickens, whereas muscle extracts show an age-dependent decrease in the amounts of c-src-specific mRNA and pp60c-src kinase activity. In contrast, the Ievels of c-yes mRNA in brain, heart, and muscle are relatively low in early embryonic stages and increase later on to values comparable to those found for liver, while in adult animals the pattern of c-yes expression is similar to that of the c-src gene. From the close correlation between the Ievels of pp60c-src, its enzymatic activity, and its corresponding mRNA at a given stage of development and in given tissues, it appears that the expression of pp60c-src is primarily controlled at the level of transcription. It is suggested that because of the different patterns of expression, the two cellular oncogenes, c-src and c-yes, play different roles in cell proliferation during early embryonic stages as weil as in ensuing differentiation processes.
KW - Biochemie
Y1 - 1984
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-59289
ER -
TY - JOUR
A1 - Arends, H.
A1 - Sebald, Walter
T1 - Nucleotide sequence of the cloned mRNA and gene of the ADP/ATP carrier from Neurospora crassa
N2 - A cDNA complementary to the mRNA of the ADPIATP carrier from Neurospora crassa was identified among ordered cDNA clones by hybridizing total polyadenylated RNA to pools of 96 cDNA recombinant plasmids and subsequent cellfree translation of hybridization-selected mRNA. Further carrier cDNAs were found by colony fdter hybridization at a frequency of 0.2-0.3%. The gene of the carrier was cloned and isolated on a 4.6-kbp EcoRl fragment of total Neurospora DNA, and the start of the mRNA was determined by Sl nuclease mapping. From the nucleotide sequence of the cDNA and the genomic DNA, the primary structure of the gene, of the mRNA and of the ADP I ATP carrier protein could be deduced. The gene occurs in a single copy in the genome and related genes are absent. It contains two short introns, and a pyrimidine-rieb promoter region. The mRNA has a 46-bp 5 1 end and a 219-bp 3 1 end. There is an open reading frame coding for the 313 amino acid residues of the Neurospora carrier protein. The amino acid sequence is homologous in 148 positions with the established primary structure of the beef heart carrier.
KW - Biochemie
KW - mitochondrial ADP
KW - ATP carrier
KW - Neurospora crassa
KW - mRNA and gene
KW - nucleotide sequence
KW - hybrid-selected translation
Y1 - 1984
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62684
ER -
TY - JOUR
A1 - Velours, J.
A1 - Esparza, M.
A1 - Hoppe, J.
A1 - Sebald, Walter
A1 - Guerin, B.
T1 - Amino acid sequence of a new mitochondrially synthesized proteolipid of the ATP synthase of Saccharomyces cerevisiae
N2 - The purification and the amino acid sequence of a proteolipid translated on ribosomes in yeast mitochondria is reported. This protein, which is a subunit of the A TP synthase, was purified by extraction with chloroform/methanol (2/1) and subsequent chromatography on phosphocellulose and reverse phase h.p.l.c. A mol. wt. of 5500 was estimated by chromatography on Bio-Gel P-30 in 8011/o fonnie acid. The complete amino acid sequence of this protein was determined by automated solid phase Edman degradation of the whole protein and of fragments obtained after cleavage with cyanogen bromide. The sequence analysis indicates a length of 48 amino acid residues. The calculated mol. wt. of 5870 corresponds to the value found by gel chromatography. This polypeptide contains three basic residues and no negatively charged side chain. The three basic residues are clustered at the C terminus. The primary structure of this protein is in full agreement with the predicted amino acid sequence of the putative polypeptide encoded by the mitochondrial aap1 gene recently discovered in Saccharomyces cerevisiae. Moreover, this protein shows 5011/o homology with the amino acid sequence of a putative polypeptide encoded by an unidentified reading frame also discovered near the mitochondrial ATPase subunit 6 genein Aspergillus nidulans.
KW - Biochemie
KW - ATP synthase
KW - mitochondrially translated
KW - proteolipid
KW - sequence subunit
Y1 - 1984
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62695
ER -
TY - JOUR
A1 - Schmidt, B.
A1 - Wachter, E.
A1 - Sebald, Walter
A1 - Neupert, W.
T1 - Processing peptidase of Neurospora mitochondria. Two-step cleavage of imported ATPase subunit 9
N2 - Subunit 9 (dicyclohexylcarbodümide binding protein, 'proteolipid') of the mitochondrial F 1F0-ATPase is a nuclearly coded protein in Neurospora crassa. lt is synthesized on free cytoplasmic ribosomes as a larger precursor with an NH2-terminal peptide extension. The peptide extension is cleaved ofT after transport of the protein into the mitochondria. A processing activity referred to as processing peptidase that cleaves the precursor to subunit 9 and other mitochondrial proteins is described and characterized using a cell-free system. Precursor synthesized in vitro was incubated with extracts of mitochondria. Processing peptidase required Mn2 + for its activity. Localization studies suggested that it is a soluble component of the mitochondrial matrix. The precursor was cleaved in two sequential steps via an intermediate-sized polypeptide. The intermediate form in the processing of subunit 9 was also seen in vivo and upon import of the precursor into isolated mitochondria in vitro. The two dcavage sites in the precursor molecule were determined. The data indicate that: {a) the correct NH2-terminus of the mature protein was generated, (b) the NH2-terminal amino acid of the intermediate-sized polypeptide is isoleueine in position -31. The cleavage sites show similarity ofprimary structure. It is concluded that processing peptidase removes the peptide extension from the precursor to subunit 9 (and probably other precursors) after translocation of these polypeptides (or the NHrterminal part of these polypeptides) into the matrix space of mitochondria.
KW - Biochemie
Y1 - 1984
U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-62674
ER -