Abstract
The Drosophila fs(1)Ya protein (YA) is an essential component of the early embryonic nuclear lamina. Mutant zygotes lacking functional YA arrest in the first division cycles following fertilization, hence having a 'Young Arrest' of their development. The nuclear lamina is thought to act as the structural backbone for the nucleus and to provide anchoring sites for interphase chromosomes. Here, we demonstrate in vitro that YA is not required for the de novo formation of nuclear structures. Since YA's sequence predicts potential DNA binding motifs, this protein may instead function to connect the lamina and chromosomes, and thus aid in organizing the nucleus. We ectopically expressed YA in polytene cells and demonstrated its association with polytene chromosomes, preferentially at interbands. Furthermore, our in vitro studies indicate that embryonic YA protein is capable of associating with decondensed chromatin. These observations suggest that YA may be required for the interaction between chromatin and the nuclear envelope during early embryogenesis.
