Structure of the minimal automaton of a numeration language

in Actes de LaCIM 2010 (2010, August)

We study the structure of automata accepting the greedy representations of N in a wide class of numeration systems. We describe the conditions under which such automata can have more than one strongly ... [more ▼]

We study the structure of automata accepting the greedy representations of N in a wide class of numeration systems. We describe the conditions under which such automata can have more than one strongly connected component and the form of any such additional components. Our characterization applies, in particular, to any automaton arising from a Bertrand numeration system. Furthermore, we show that for any automaton A arising from a system with a dominant root beta>1, there is a morphism mapping A onto the automaton arising from the Bertrand system associated with the number beta. [less ▲]

Structure of the Telomeric Ends of Mt DNA, Transcriptional Analysis and Complex I Assembly in the Dum24 Mitochondrial Mutant of Chlamydomonas Reinhardtii

in Molecular Genetics & Genomics (2001), 266(1), 109-14

The dum24 mutant of Chlamydomonas reinhardtii contains four types of altered mitochondrial linear genomes: two types of deleted monomers and two types of dimers resulting from fusions between some ... [more ▼]

The dum24 mutant of Chlamydomonas reinhardtii contains four types of altered mitochondrial linear genomes: two types of deleted monomers and two types of dimers resulting from fusions between some monomers via their deleted ends. All molecules lack at least cob, nd4 and the 3' end of nd5, three adjacent genes located in the left part of the genome. We present evidence showing that in dum24, as in other deletion mutants, the deletions extend to the left telomeric end, and propose that the only replicative forms in the mutants are the dimeric DNA molecules that possess intact telomeric structures at both ends. Two abnormally large transcripts produced from chimeric genes are detected in dum24, which throws some light on the location of potential promoter sequences and processing signals in the mitochondrial genome. Using BN-PAGE analysis and immunological methods to detect complex I, we further show that dum24 mitochondria do not possess the normal multimeric complex I (850 kDa), but produce a smaller, partially assembled, complex (650 kDa), demonstrating a role for ND4 and/or ND5 subunits(s) in complex I assembly. [less ▲]

Structure of the wall peptidoglycan of streptomyces R39 and the specificity profile of its exocellular DD-carboxypeptidase-transpeptidase for peptide acceptors

in Biochemistry (1973), 12(7), 1243-1251

Benzylpenicillin and cephaloridine reacted with the exocellular dd-carboxypeptidase–transpeptidase from Streptomyces R39 to form equimolar and inactive antibiotic–enzyme complexes. At saturation, the ... [more ▼]

Benzylpenicillin and cephaloridine reacted with the exocellular dd-carboxypeptidase–transpeptidase from Streptomyces R39 to form equimolar and inactive antibiotic–enzyme complexes. At saturation, the molar ratio of chromogenic cephalosporin 87-312 to enzyme was 1.3:1, but this discrepancy might be due to a lack of accuracy in the measurement of the antibiotic. Spectrophotometric studies showed that binding of cephaloridine and cephalosporin 87-312 to the enzyme caused opening of their β-lactam rings. Benzylpenicillin and cephalosporin 87-312 competed for the same site on the free enzyme, suggesting that binding of benzylpenicillin also resulted in the opening of its β-lactam ring. In Tris–NaCl–MgCl2 buffer at pH7.7 and 37°C, the rate constants for the dissociation of the antibiotic–enzyme complexes were 2.8×10−6, 1.5×10−6 and 0.63×10−6s−1 (half-lives 70, 130 and 300h) for benzylpenicillin, cephalosporin 87-312 and cephaloridine respectively. During the process, the protein underwent reactivation. The enzyme that was regenerated from its complex with benzylpenicillin was as sensitive to fresh benzylpenicillin as the native enzyme. With [14C]benzylpenicillin, the released radioactive compound was neither benzylpenicillin nor benzylpenicilloic acid. The Streptomyces R39 enzyme thus behaved as a β-lactam-antibiotic-destroying enzyme but did not function as a β-lactamase. Incubation at 37°C in 0.01m-phosphate buffer, pH7.0, and in the same buffer supplemented with sodium dodecyl sulphate caused a more rapid reversion of the [14C]benzylpenicillin–enzyme complex. The rate constants were 1.6×10−5s−1 and 0.8×10−4s−1 respectively. Under these conditions, however, there was no concomitant reactivation of the enzyme and the released radioactive compound(s) appeared not to be the same as before. The Streptomyces R39 enzyme and the exocellular dd-carboxypeptidase–transpeptidase from Streptomyces R61 appeared to differ from each other with regard to the topography of their penicillin-binding site. [less ▲]

Structure of triosephosphate isomerase from Escherichia coli determined at 2.6 A resolution

in Acta Crystallographica Section D-Biological Crystallography (1993), 49(Pt 4), 403-17

The structure of triosephosphate isomerase (TIM) from the organism Escherichia coli has been determined at a resolution of 2.6 A. The structure was solved by the molecular replacement method, first at 2.8 ... [more ▼]

The structure of triosephosphate isomerase (TIM) from the organism Escherichia coli has been determined at a resolution of 2.6 A. The structure was solved by the molecular replacement method, first at 2.8 A resolution with a crystal grown by the technique of hanging-drop crystallization from a mother liquor containing the transition-state analogue 2-phosphoglycolate (2PG). As a search model in the molecular replacement calculations, the refined structure of TIM from Trypanosoma brucei, which has a sequence identity of 46% compared to the enzyme from E. coli, was used. An E. coli TIM crystal grown in the absence of 2PG, diffracting to 2.6 A resolution, was later obtained by application of the technique of macro-seeding using a seed crystal grown from a mother liquor without 2PG. The final 2.6 A model has a crystallographic R factor of 11.9%, and agrees well with standard stereochemical parameters. The structure of E. coli TIM suggests the importance of residues which favour helix initiation for the formation of the TIM fold. In addition, TIM from E. coli shows peculiarities in its dimer interface, and in the packing of core residues within the beta-barrel. [less ▲]

The structure of two fengycins from Bacillus subtilis S499.

in Zeitschrift für Naturforschung. C, Journal of Biosciences (1999), 54(11), 859-66

The structures of the two fengycins, lipopeptides from Bacillus subtilis, were elucidated by spectroscopic methods and chemical degradation. They show a close structural relationship to the plipastatins ... [more ▼]

The structures of the two fengycins, lipopeptides from Bacillus subtilis, were elucidated by spectroscopic methods and chemical degradation. They show a close structural relationship to the plipastatins from Bacillus cereus differing only in the stereochemistry of the Tyr residues. [less ▲]

Structure sociologique de l'élecotrat écologiste en Wallonie : une première exploration

in Res Publica (1993), 25

The paper describes the main characteristics of ecological constituency through results of surveys. It shows how ecologist voter differ sharply from the rest of the population beeing much younger and much ... [more ▼]

The paper describes the main characteristics of ecological constituency through results of surveys. It shows how ecologist voter differ sharply from the rest of the population beeing much younger and much more educated, e.a. [less ▲]

Structure spatiale des marchés fonciers et production de l’urbanisation. Application à la Belgique et à ses nouveaux espaces résidentiels

Scientific conference (2007, February 12)

Structure spatiale et impact écologique des processus d'anthropisation des paysages terrestres: développement d'une instrumentation générique d'analyse

Poster (2011, March 28)

The current research project aims to develop a generic set of analysis methods which enables to characterize quantitatively anthropogenic degradation of terrestrial ecosystems. This characterization will ... [more ▼]

The current research project aims to develop a generic set of analysis methods which enables to characterize quantitatively anthropogenic degradation of terrestrial ecosystems. This characterization will assist in landscape planning oriented towards a sustainable management of human impacts and towards a restoration of degraded ecosystems. The analysis methods will enable to detect landscape degradation and its anthropogenic drivers based on their spatial properties, a type of information that is less complex and less expensive to obtain than ecological data collected in situ. The project is composed of two parts: (1) methodological research and development, based on the principles of landscape ecology and combined with other disciplines like remote sensing, geographic information systems, sociology and agronomy; (2) application of the developed pattern metrics on new study cases for evaluation and validation. Using study cases of degradation situated worldwide, the development of a typology will enable to identify, classify and analyze the causes of degradation, their spatial properties and the ecosystems involved. These study cases will be chosen based on the types of ecosystems degraded, the spatial scale of degradation, the climatic zone, and the intensity and speed of landscape degradation. Every type will be analyzed with regard to its impact on spatial pattern. Afterwards, the different metrics will be evaluated statistically for comparison with regard to their potential to capture anthropogenic effects. The development of new metrics is hereby not excluded. Critical thresholds will be defined in order to detect critical degradation levels of the terrestrial ecosystems. The best metrics selected in this way will be calculated for new cases of anthropogenic impacts on landscapes, cases selected by application of the aforementioned typology, in order to validate the correlation between metric outcomes and in situ observations. [less ▲]

Structure, chromosomal location, and expression pattern of three mouse genes homologous to the human MAGE genes.

in Genomics (1995), 28(1), 74-83

The human MAGE1 gene directs the expression of an antigen recognized on a melanoma by autologous cytolytic T lymphocytes. MAGE1 belongs to a family of genes that are expressed in a number of tumors of ... [more ▼]

The human MAGE1 gene directs the expression of an antigen recognized on a melanoma by autologous cytolytic T lymphocytes. MAGE1 belongs to a family of genes that are expressed in a number of tumors of various histological types but not in normal tissues except testis. The MAGE genes are arranged in two groups that are located within two different regions of the human X chromosome (Xq26-qter and Xp21.3). By hybridizing mouse genomic libraries with a MAGE1 probe, we identified three homologous genes. Two of these mouse genes, Smage1 and Smage2, are more than 99% identical to each other and encode the same protein of 330 aa. The 5' noncoding region of Smage2 provides the potential for regulating the expression of the gene through several different promoters located in front of alternative first exons. The third gene, Smage3, has the structure of a processed transcript. It codes for a protein with only 11 aa substitutions with respect to the Smage1/2 product. Somatic cell hybrids and interspecific backcross analysis showed that Smage3 is autosomal and that Smage1 and Smage2 are located between the Dmd and the Ar loci on the mouse X chromosome. Since this region is syntenic to the human Xp21.1-p22.1 region, we conclude that Smage1 and Smage2 are homologous to the MAGE-Xp rather than to the MAGE-Xq genes. Smage1/2 transcripts were detected in several tumor and embryonal cell lines but not in normal mouse tissues with the exception of testis. Expression of Smage3 was found in embryos from Day 11 to Day 15. [less ▲]

Structure, function, and fate of the BlaR signal transducer involved in induction of beta-lactamase in Bacillus licheniformis

in Journal of Bacteriology (1992), 174(19), 6171-6178

The membrane-spanning protein BlaR is essential for the induction of beta-lactamase in Bacillus licheniformis. Its nature and location were confirmed by the use of an antiserum specific for its carboxy ... [more ▼]

The membrane-spanning protein BlaR is essential for the induction of beta-lactamase in Bacillus licheniformis. Its nature and location were confirmed by the use of an antiserum specific for its carboxy-terminal penicillin sensor, its function was studied by genetic dissection, and the structure of the penicillin sensor was derived from hydrophobic cluster analysis of the amino acid sequence by using, as a reference, the class A beta-lactamases with known three-dimensional structures. During the first 2 h after the addition of the beta-lactam inducer, full-size BlaR, bound to the plasma membrane, is produced, and then beta-lactamase is produced. By 2 h after induction, BlaR is present in various (membrane-bound and cytosolic) forms, and there is a gradual decrease in beta-lactamase production. The penicillin sensors of BlaR and the class D beta-lactamases show strong similarities in primary structures. They appear to have the same basic spatial disposition of secondary structures as that of the class A beta-lactamases, except that they lack several alpha helices and, therefore, have a partially uncovered five-stranded beta sheet and a more readily accessible active site. Alterations of BlaR affecting conserved secondary structures of the penicillin sensor and specific sites of the transducer annihilate beta-lactamase inducibility. [less ▲]