Clear Search sequence regions


Sizes of these terms reflect their relevance to your search.

Many multicellular organisms specify germ cells during early embryogenesis by the inheritance of ribonucleoprotein (RNP) granules known as germplasm. However, the role of complex interactions of RNP granules during germ cell specification remains elusive. This study characterizes the interaction of RNP granules, Buc, and zebrafish Vasa (zfVasa) during germ cell specification. We identify a novel zfVasa-binding motif (Buc-VBM) in Buc and a Buc-binding motif (zfVasa-BBM) in zfVasa. Moreover, we show that Buc and zfVasa directly bind in vitro and that this interaction is independent of the RNA. Our circular dichroism spectroscopy data reveal that the intrinsically disordered Buc-VBM peptide forms alpha-helices in the presence of the solvent trifluoroethanol. Intriguingly, we further demonstrate that Buc-VBM enhances zfVasa ATPase activity, thereby annotating the first biochemical function of Buc as a zfVasa ATPase activator. Collectively, these results propose a model in which the activity of zfVasa is a central regulator of primordial germ cell (PGC) formation and is tightly controlled by the germplasm organizer Buc.

Citation

Roshan Priyarangana Perera, Alaa Shaikhqasem, Nadia Rostam, Achim Dickmanns, Ralf Ficner, Kai Tittmann, Roland Dosch. Bucky Ball Is a Novel Zebrafish Vasa ATPase Activator. Biomolecules. 2021 Oct 13;11(10)

Expand section icon Mesh Tags

Expand section icon Substances


PMID: 34680140

View Full Text