Male meiosis behaviour and heterochromatin characterization of three big water bug species were studied. Belostoma dentatum (Mayr, 1863), Belostoma elongatum Montandon, 1908 and Belostoma gestroi Montandon, 1903 possess 2n = 26 + X1X2Y (male). In these species, male meiosis is similar to that previously observed in Belostoma Latreille, 1807. In general, autosomal bivalents show a single chiasma terminally located and divide reductionally at anaphase I. On the other hand, sex chromosomes are achiasmatic, behave as univalents and segregate their chromatids equationally at anaphase I. The analysis of heterochromatin distribution and composition revealed a C-positive block at the terminal region of all autosomes in Belostoma dentatum, a C-positive block at the terminal region and C-positive interstitial dots on all autosomes in Belostoma elongatum, and a little C-positive band at the terminal region of autosomes in Belostoma gestroi. A C-positive band on one bivalent was DAPI negative/CMA3 positive in the three species. The CMA3-bright band, enriched in GC base pairs, was coincident with a NOR detected by FISH. The results obtained support the hypothesis that all species of Belostoma with multiple sex chromosome systems preserve NORs in autosomal bivalents. The karyotype analyses allow the cytogenetic characterization and identification of these species belonging to a difficult taxonomic group. Besides, the cytogenetic characterization will be useful in discussions about evolutionary trends of the genome organization and karyotype evolution in this genus.
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http://dx.doi.org/10.3897/CompCytogen.v7i2.4462 | DOI Listing |
Sci Rep
December 2024
Hy-Line International, 2583 240th St, PO Box 310, Dallas Center, 50063, IA, USA.
Marek's Disease (MD), which can result in neurological damage and tumour formation, has large effects on the economy and animal welfare of the poultry industry worldwide. Previously, we mapped autosomal MD QTL regions (QTLRs) by individual genotyping of an F population from a full-sib advanced intercross line. We further mapped MD QTLRs on the chicken Z chromosome (GGZ) using the same F population, and by selective DNA pooling (SDP) of 8 elite egg production lines.
View Article and Find Full Text PDFJ Eur Acad Dermatol Venereol
December 2024
Department of Dermatology, Medical University of Vienna, Vienna, Austria.
Background: Conventional photodynamic therapy (cPDT) is an effective treatment option for field cancerization and multiple actinic keratoses (AK). The main side effect of cPDT is pain during illumination which in severe cases might necessitate early termination of treatment. Modification of treatment parameters such as light dose and fluence rate is a promising approach to mitigate PDT-associated pain.
View Article and Find Full Text PDFFEBS Lett
December 2024
School of Pharmacy at Fukuoka, International University of Health and Welfare, Fukuoka, Japan.
Fused in sarcoma (FUS) is a causative factor of amyotrophic lateral sclerosis (ALS) and is believed to propagate pathologically by transmission from cell to cell. However, the mechanism underlying FUS release from cells, which is a critical step for the propagation system, remains poorly understood. This study conducted an analysis of the release of human and mouse FUS from neurons, revealing that human FUS is significantly released into the media compared to its mouse counterpart.
View Article and Find Full Text PDFAntiviral Res
December 2024
Department of Biochemistry and Pharmacology, University of Melbourne, Parkville, VIC 3010, Australia; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia. Electronic address:
The Phosphoprotein (P protein) of the rabies virus has multiple roles in virus replication. A critical function is to act as a cofactor in genome replication and mRNA production through binding via its N-terminal region to the L protein, the essential enzyme for mRNA and genome synthesis/processing, and via its C-terminal domain (P) to the N protein and viral RNA (N-RNA) ribonucleoprotein complex. The binding site of the P on the N protein is a disordered loop that is expected to be phosphorylated at Ser389.
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