nanos (nos) mR.NA is locali/ed to t fie posterior j>o]e nf the I)ro,-.ophil.i earlv embryos where Nos protein is synthesized. Nos encodes au evolutionary cunserved protein with a novel (C(H)2 Zn binding domain. Nos acts together with pumilio (pnm) to negatively con t roi translation of the maternal K piovided product of the transcription factor hunchback (lib). Consecpien protein is distributed in a gradient rorupleinentary to of Nos. Absence of lib protein from the posterior region of the embryos is necessary foi normal abdomen lor mation. P u m contains a novel R.N A-binding motif composed of eighi sejnnm' repeats thai bind specifically to sequences in the 3 U'TR ot hb RXA. A similar ItiNA binding motif with similar but not identical sequence sprdiiuU is piest-nt in a oPum-likeo protein from humans. We are invesligating t fie nun hanisms by which Nos and Puni control translation, nos and purn affect targets, in addition to ilb. Maternally provided Nos protein is present in I he pnmondai cells (PGC) when thev form and persists throughout embryogenesis. To study the role of nos in genn cell development, we generated eggs that lack Nos and Hb. role hese eggs, when fertilized bv wild type sperm, give rise to HOT m ally segmented embryos tfuit lonn PCX's which lat k tnateinal No- protein. V lind that germ cell migration is dramatically affected resulting in mal and feinil that lack germ line. Nos, and Pum also play a role in early oogencsis uhen hot h gene are required lot the noimal developmem of germ line stem cells.
|Original language||English (US)|
|State||Published - Dec 1 1998|
ASJC Scopus subject areas
- Molecular Biology