Msi1-Like (MSIL) Proteins in Fungi

Msi1-like (MSIL) proteins, which are eukaryote-specific and contain a series of WD40 repeats, have pleiotropic roles in chromatin assembly, DNA damage repair, and regulation of nutrient/stress-sensing signaling pathways. In the fungal kingdom, the functions of MSIL proteins have been studied most intensively in the budding yeast model Saccharomyces cerevisiae, an ascomycete. Yet their functions are largely unknown in other fungi. Recently, an MSIL protein, Msl1, was discovered and functionally characterized in the pathogenic yeast Cryptococcus neoformans, a basidiomycete. Interestingly, MSIL proteins appear to have redundant and unique roles in both fungi, suggesting that MSIL proteins may have evolutionarily divergent roles in different parts of the fungal kingdom. In this review, we will describe the current findings regarding the role of MSIL proteins in fungi and discuss future directions for research on this topic.

ULTRASTRUCTURAL STUDY ON THE PROCESS OF NUCLEAR RECONSTITUTION IN A CELL-FREE SYSTEM FROM XENOPUS EGGS / 解剖学报

Nuclear reconstitution around Lambda DNA in a cell-free system from Xenopus eggs involves distinct steps at ultrastructural level. First, Lambda DNA polymers were induced to form chromatin-like structures with the proteins in egg extracts. Then, along with membrane vesicles and nuclear pore components attached to them to assemble double nuclear membranes, these chromatin-like structures underwent variations from condensation to decondensation, simultaneously. It is different from the nuclear reconstitution induced by chromatin in that, while membrane vesicles were attaching to the chromatin-like structures to fuse each other, the assembly of nuclear pore complexes occurred practically.