Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1209035 | PMC |
http://dx.doi.org/10.1093/genetics/24.2.202 | DOI Listing |
Protoplasma
January 2025
Core Facility Center "Cultivation of Microorganisms", Saint-Petersburg State University, Saint-Petersburg, Russian Federation.
Ciliates often form symbiotic associations with other microorganisms, both prokaryotic and eukaryotic. We are now starting to rediscover the symbiotic systems recorded before molecular analysis became available. Here, we provide a morphological and molecular characterization of a symbiotic association between the ciliate Paramecium tritobursaria and the yeast Rhodotorula mucilaginosa (syn.
View Article and Find Full Text PDFFront Biosci (Landmark Ed)
November 2024
Department of Cancer Cell Biology, Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991 Moscow, Russia.
Background: In the twentieth century, the textbook idea of packaging genomic material in the cell nucleus and metaphase chromosomes was the presence of a hierarchy of structural levels of chromatin organization: nucleosomes - nucleosomal fibrils -30 nm fibrils - chromomeres - chromonemata - mitotic chromosomes. Chromomeres were observed in partially decondensed chromosomes and interphase chromatin as ~100 nm globular structures. They were thought to consist of loops of chromatin fibres attached at their bases to a central protein core.
View Article and Find Full Text PDFEMBO Rep
January 2025
Institute of Cell Biology, University of Bern, Baltzerstrasse 4, 3012, Bern, Switzerland.
Facultative heterochromatin is marked by the repressive histone modification H3K27me3 in eukaryotes. Deposited by the PRC2 complex, H3K27me3 is essential for regulating gene expression during development, and chromatin bearing this mark is generally considered transcriptionally inert. The PRC2 complex has also been linked to programmed DNA elimination during development in ciliates such as Paramecium.
View Article and Find Full Text PDFNucleic Acids Res
January 2025
Université Paris Cité, CNRS, Institut Jacques Monod, 15 rue Hélène Brion, F-75013 Paris, France.
Protein Sci
December 2024
Basque Research and Technology Alliance (BRTA), Center for Cooperative Research in Biosciences (CIC bioGUNE), Derio, Spain.
Protein A075L is a β-xylosyltransferase that participates in producing the core of the N-glycans found in VP54, the major viral capsid protein of Paramecium bursaria chlorella virus-1 (PBCV-1). In this study, we present an X-ray crystallographic analysis of the apo form of A075L, along with its complexes with the sugar donor and with a trisaccharide acceptor. The protein structure shows a typical GT-B folding, with two Rossmann-like fold domains, in which the acceptor substrate binds to the N-terminal region, and the nucleotide-sugar donor binds to the C-terminal region.
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!