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F Catala

Publications and source records attributed to F Catala.

16 recordsLinked to original sources
PubMed2000

Phosphorylation of bicoid on MAP-kinase sites: contribution to its interaction with the torso pathway.

The Torso signal transduction pathway exhibits two opposite effects on the activity of the Bicoid (Bcd) morphogen: (i) Bcd function is repressed by Torso (Tor) at the anterior pole of the embryo leading to a retraction of the expression of many Bcd targets from the most anterior region of the embryo, where the Tor tyrosine kinase receptor is activated, and (ii) Bcd function is strengthened by Tor in a broader anterior region, as indicated by a shift of the posterior border of Bcd targets towards the anterior pole in embryos deprived from Tor activity. Anterior repression of Bcd targets was not observed in embryos lacking maternal contribution of D-sor, which acts downstream of Tor and encodes a MAP-kinase kinase. This indicates that the Ras signalling cascade is directly involved in this process, although the known transcriptional effectors of the Tor pathway, tll and hkb, are not (Ronchi, E., Treisman, J., Dostatni, N., Struhl, G. and Desplan, C. (1993) Cell 74, 347-355). Bcd is a good in vitro substrate for phosphorylation by MAP-kinase and phosphorylation of the protein occur in vivo on MAP-kinase sites. In the presence of a Bcd mutant that could no longer be phosphorylated by MAP-kinase, expression of Bcd targets remained repressed by Tor at the pole while strengthening of Bcd activity was reduced. These experiments indicate that phosphorylation of Bcd by MAP-kinase is likely to be required for the Tor pathway to induce its full positive effect on Bcd. This suggests that Tor signalling acts at a distance from the anterior pole by direct modification of the diffusing Bcd morphogen.

Amino Acid Sequence↗
PubMed1995

A skeletal muscle-specific enhancer regulated by factors binding to E and CArG boxes is present in the promoter of the mouse myosin light-chain 1A gene.

The mouse myosin light-chain 1A (MLC1A) gene, expressed in the atria of the adult heart, is one of the first muscle genes to be activated when skeletal as well as cardiac muscles form in the embryo. It is also transcribed in skeletal muscle cell lines at the onset of differentiation. Transient transfection assays of mouse skeletal muscle cell lines with DNA constructs containing MLC1A promoter fragments fused to the chloramphenicol acetyltransferase (CAT) gene show that the first 630 bp of the promoter is sufficient to direct expression of the reporter gene during myotube formation. Two E boxes located at bp -76 and -519 are necessary for this regulation. MyoD and myogenin proteins bind to them as heterodimers with E12 protein and, moreover, transactivate them in cotransfection experiments with the MLC1A promoter in nonmuscle cells. Interestingly, the effect of mutating each E box is less striking in primary cultures than in the C2 or Sol8 muscle cell line. A DNA fragment from bp -36 to -597 confers tissue- and stage-specific activity to the herpes simplex virus thymidine kinase promoter in both orientations, showing that the skeletal muscle-specific regulation of the MLC1A gene is under the control of a muscle-specific enhancer which extends into the proximal promoter region. At bp -89 is a diverged CArG box, CC(A/T)6AG, which binds the serum response factor (SRF) in myotube nuclear extracts, as does the wild-type sequence, CC(A/T)6GG. Both types of CArG box also bind a novel myotube-enriched complex which has contact points with the AT-rich part of the CArG box and adjacent 3' nucleotides. Mutations within the CArG box distinguish between the binding of this complex and binding of SRF; only SRF binding is directly involved in the specific regulation of the MLC1A gene in skeletal muscle cell lines.

Animals↗
PubMed1992

Alternative multimeric structures affect myogenin DNA binding activity.

The native molecular weight of the basic helix-loop-helix (bHLH) proteins myogenin, MyoD, and E12 was calculated from their mobilities on sucrose gradients and molecular sieve chromatography. The muscle bHLH proteins associate to form a variety of higher order complexes, most of which are larger than dimers. Homodimers bind to DNA sequences such as the MEF-1 site in the creatine kinase enhancer whereas homotetramers and larger forms do not recognize this DNA sequence. The ubiquitous bHLH protein E12 forms monomers or homodimers with little evidence for higher order complexes. Mixtures of myogenin and E12 show some heterodimeric structures, but most of the myogenin remains in large complexes. This result using purified proteins is also obtained in nuclear extracts from differentiated myotubes, in which most of the myogenin is present in large complexes that do not bind to the creatine kinase enhancer. A fusion protein containing only the myogenin HLH region forms large homomeric complexes. A model is presented in which each helix associates with a different subunit to form chains or ring structures to explain these observations. The partition of myogenin in nuclear extracts into dimers that recognize known DNA sequences and higher order complexes that do not raises important new issues concerning the regulation of skeletal muscle bHLH protein activity during myogenesis.

Animals↗
PubMed1992

Multimeric structures influence the binding activity of bHLH muscle regulatory factors.

Sucrose gradients and molecular sieve chromatography were used to determine the native molecular weight of the basic HLH proteins myogenin, MyoD and E12. The muscle bHLH proteins not only formed dimers but also associated in a variety of higher order complexes. Although homodimers bind to DNA sequences such as the MEF-1 site in the creatine kinase enhancer, homotetramers and larger forms do not recognize this DNA sequence. Little evidence for complexes larger than dimers was found for the ubiquitous bHLH protein E12. Most of the myogenin remains in large complexes when myogenin and E12 are mixed. The same result was obtained in nuclear extracts from differentiated myotubes, in which most of the myogenin was found to be present in large complexes that do not bind to the creatine kinase enhancer. A fusion protein that contains only the myogenin HLH region fused to glutathione-S-transferase also forms large homomeric complexes. A model to explain these results is that each helix of the HLH motif can associate with a different subunit to form chains or ring structures. The presence of myogenin in nuclear extracts as both dimers that recognize known DNA sequences as well as higher order complexes that do not raises significant issues concerning the regulation of skeletal muscle bHLH protein activity during myogenesis.

Animals↗
PubMed1989

Nuclear protein factors and erythroid transcription of the human A gamma-globin gene.

We have used DNaseI footprinting and gel mobility assays to analyze the upstream region of the human A gamma-globin gene promoter. Four protein factors were found to bind this region. A non-erythroid factor present in the 0.4M KCl fraction of a heparin agarose column binds to the CAC box (-140). A ubiquitous octamer factor present in the 0.2M fraction binds to an ATGCAAT element (-175), but is completed out by the erythroid specific factor NF-E1 (in the 0.4M KCl fraction), which binds a site (-186) immediately flanking the octamer. A novel factor binding to a stretch of 8A around -233, was identified in the 0.2M KCl fraction. This factor is not present in HeLa nuclear extracts. To study the transcriptional importance of these protein binding sites we have used an "A gamma-minilocus", similar to that described for the beta-globin gene (1) in K562 cells. This provides evidence that the NF-E1 and CAC box in the -210 to -122 region of the A gamma-promoter are important for the efficient expression of the gamma-globin gene.

Base Sequence↗
PubMed1989

CT findings in Swyer-James syndrome.

Swyer-James syndrome (SJS) is usually diagnosed with plain chest radiographs obtained during inspiration/expiration. The authors studied patients with CT to assess its value in the evaluation of this syndrome. In patients with SJS, CT was useful in the determination of bronchial patency (all nine patients), lung parenchymal changes (subpleural infiltrates in six patients, atelectasis in two, and cavities in two), and the extent and degree of bronchiectasis (all nine patients). If CT is used for the evaluation of bronchiectasis, knowledge of the main findings associated with SJS (hyperlucent lung without anteroposterior gradient attenuation [n = 8], small lung [n = 6], and diminished central and peripheral pulmonary arteries [n = 9]) should facilitate the diagnosis of associated SJS. Expiration CT would support the diagnosis with demonstration of air trapping.

Adolescent↗
PubMed1988

[Liposarcoma of the spermatic cord].

We review a new case of spermatic cord liposarcoma followed over a period of two years. After simple excision and 50 grays of radiotherapy had a local recurrence one year later; the patient a wide radical orchiectomy was then performed. A review of the literature illustrates the various clinicopathological data and their prognosis. The various treatments described are also analysed.

Aged↗
PubMed1986

DNA methylation and transcriptional controls of proviral DNA in avian sarcoma virus-transformed mammalian cells.

Restriction mapping has been used to study the integration state of the single provirus present in the DNA of two subclones, RS2/3 and RS2/6, of hamster cells transformed in vitro by Rous sarcoma virus, but differing markedly in their level of proviral transcription which was higher in RS2/3 cells. It was observed that both proviruses are complete and located at the same integration site in each DNA. However, the RS2/6 provirus and its flanking cellular sequences were found to be hypermethylated, although a very short region was hypomethylated at about 1 kb upstream of the src gene. A low level of methylation was observed in RS2/3 cells, in the proviral region. Northern analysis of viral RNA detected only the src mRNA in RS2/6 cells, whereas the two other viral mRNA were found in RS2/3 cells, however their levels were very low compared to that of the src mRNA. These findings suggest a correlation between the methylation state and the transcriptional control of the proviral genes. Sequences responsible for such a control by methylation should lie within both the provirus and its 5' flanking cellular sequences.

Animals↗
PubMed1979

Infectivity of proviral DNA from avian sarcoma virus-transformed mammalian cells.

The number of Rous viral genomes in the cellular DNA from two subclones (RS2/3, RS2/6) derived from the same clone of hamster BHK-21 cells transformed by Rous sarcoma virus was determined by hybridization with viral complementary DNA made in vitro, and the capacity of the cellular DNA to infect (transfect) chicken embryo fibroblasts was compared before and after shearing this DNA to about the size of the provirus (6 x 10(6) to 7 x 10(6) daltons). The two subclones differed widely both in their capacity to give rise to virus (inducibility) after fusion with chicken embryo fibroblasts and in level of expression of viral proteins. It was shown that cells of both subclones contain a single copy of Rous DNA and yield infectious DNA. However, whereas transfection of chicken embryo fibroblasts was successful with both unsheared (>/=18 x 10(6) daltons) and sheared DNA from the most inducible subclone (RS2/3 subclone), which also expresses viral proteins to an appreciable amount, transfection with DNA from the least inducible subclone (RS2/6 subclone), in which viral proteins are not expressed, succeeded only with sheared DNA. It was then about as successful as with sheared or unsheared RS2/3 DNA. The lack of infectivity of unsheared RS2/6 DNA may be explained by the hypothesis proposed by Cooper and Temin (G. M. Cooper and H. T. Temin, J. Virol. 17:422-430, 1976) to explain the lack of infectivity of DNA from certain chicken cells producing spontaneously low amounts of RAV-0 and resistant to exogenous RAV-0 infection, that is, that the viral genome (proviral DNA) is linked to a cis-acting control element which blocks its expression. This linkage might originate, in RS2/6 cells, from translocation of cellular DNA containing the single proviral copy.

Animals↗