580 research outputs found
The lemming gene encodes the Apc11 subunit of the anaphase-promoting complex in Drosophila melanogaster
Two Cases of Hallermann-Streiff Syndrome with Retinal Abnormalities
Hallermann-Streiff syndrome is a rare congenital disorder
that is characterized by malformations of the craniofacial
region with ocular abnormalities. Some ophthalmic signs can
be observed in early age and some in adulthood. The visual
functions are determined by a lot of factors including
microphthalmos, cataract and fundus abnormalities. We report
two cases of Hallermann-Streiff syndrome identified in our
department in the last decade
Mária-kultusz Adorjánban
The village Adorján, laying on the bank of the River Tisza (today Vojvodina, Yu) wasfounded in the 18th century. The inhabitants are Catholics being employed in the agriculture. Their church was builtin 1858. Their religious life is dominated by the function of the religious confraternities. The authors describe the life of the holy rosary confraternity, the Marian girls' confraternity, the Confraternity of St. Francise, theConfraternity ofthe Sacred Heart ofJesus, theConfraternity ofMary's Heart and some other paraliturgical devotions
Role of the deubiquitylating enzyme DmUsp5 in coupling ubiquitin equilibrium to development and apoptosis in Drosophila melanogaster.
Protein ubiquitylation is a dynamic process that affects the function and stability of proteins and controls essential cellular processes ranging from cell proliferation to cell death. This process is regulated through the balanced action of E3 ubiquitin ligases and deubiquitylating enzymes (DUB) which conjugate ubiquitins to, and remove them from target proteins, respectively. Our genetic analysis has revealed that the deubiquitylating enzyme DmUsp5 is required for maintenance of the ubiquitin equilibrium, cell survival and normal development in Drosophila. Loss of the DmUsp5 function leads to late larval lethality accompanied by the induction of apoptosis. Detailed analyses at a cellular level demonstrated that DmUsp5 mutants carry multiple abnormalities, including a drop in the free monoubiquitin level, the excessive accumulation of free polyubiquitins, polyubiquitylated proteins and subunits of the 26S proteasome. A shortage in free ubiquitins results in the induction of a ubiquitin stress response previously described only in the unicellular budding yeast. It is characterized by the induction of the proteasome-associated deubiquitylase DmUsp14 and sensitivity to cycloheximide. Removal of DmUsp5 also activates the pro-apoptotic machinery thereby resulting in widespread apoptosis, indicative of an anti-apoptotic role of DmUsp5. Collectively, the pleiotropic effects of a loss of DmUsp5 function can be explained in terms of the existence of a limited pool of free monoubiquitins which makes the ubiquitin-dependent processes mutually interdependent
Egy széki mesemondó önéletírása : Győri Klára: Kiszáradt az én örömem zöld fája. Emlékezés. Sajtó alá rendezte, az előszót írta: Nagy Olga. Bukarest, 1975, 206 p.
lemmingA encodes the Apc11 subunit of the APC/C in Drosophila melanogaster that forms a ternary complex with the E2-C type ubiquitin conjugating enzyme, Vihar and Morula/Apc2
<p>Abstract</p> <p>Background</p> <p>Ubiquitin-dependent protein degradation is a critical step in key cell cycle events, such as metaphase-anaphase transition and mitotic exit. The anaphase promoting complex/cyclosome (APC/C) plays a pivotal role in these transitions by recognizing and marking regulatory proteins for proteasomal degradation. Its overall structure and function has been elucidated mostly in yeasts and mammalian cell lines. The APC/C is, however, a multisubunit assembly with at least 13 subunits and their function and interaction within the complex is still relatively uncharacterized, particularly in metazoan systems. Here, <it>lemming </it>(<it>lmg</it>) mutants were used to study the APC/C subunit, Apc11, and its interaction partners in <it>Drosophila melanogaster</it>.</p> <p>Results</p> <p>The <it>lmg </it>gene was initially identified through a pharate adult lethal P element insertion mutation expressing developmental abnormalities and widespread apoptosis in larval imaginal discs and pupal abdominal histoblasts. Larval neuroblasts were observed to arrest mitosis in a metaphase-like state with highly condensed, scattered chromosomes and frequent polyploidy. These neuroblasts contain high levels of both cyclin A and cyclin B. The <it>lmg </it>gene was cloned by virtue of the <it>lmg<sup>03424 </sup></it>P element insertion which is located in the 5' untranslated region. The <it>lemming </it>locus is transcribed to give a 2.0 kb mRNA that contains two ORFs, <it>lmgA </it>and <it>lmgB</it>. The <it>lmgA </it>ORF codes for a putative protein with more than 80% sequence homology to the APC11 subunit of the human APC/C. The 85 amino acid protein also contains a RING-finger motif characteristic of known APC11 subunits. The <it>lmgA </it>ORF alone was sufficient to rescue the lethal and mitotic phenotypes of the <it>lmg<sup>138 </sup></it>null allele and to complement the temperature sensitive lethal phenotype of the <it>APC11-myc9 </it>budding yeast mutant. The LmgA protein interacts with Mr/Apc2, and they together form a binding site for Vihar, the E2-C type ubiquitin conjugating enzyme. Despite being conserved among <it>Drosophila </it>species, the LmgB protein is not required for viability or fertility.</p> <p>Conclusions</p> <p>Our work provides insight into the subunit structure of the <it>Drosophila </it>APC/C with implications for its function. Based on the presented data, we suggest that the Lmg/Apc11 subunit recruits the E2-C type ubiquitin conjugating enzyme, Vihar, to the APC/C together with Mr/Apc2 by forming a ternary complex.</p
Measuring expression levels of small regulatory RNA molecules from body fluids and formalin-fixed, paraffin-embedded samples
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