title: Two variants of zebrafish p100 are expressed during embryogenesis and regulated by Nodal signaling.
abstract: Human p100 protein was first identified as a transcriptional coactivator of Epstein-Barr virus nuclear antigen 2, and has been shown to be a coactivator of other cellular transactivators. Its roles in development of vertebrate embryos, however, have not been reported. We have identified a zebrafish ortholog of the human p100 coactivator. The zebrafish p100 transcript is processed to two alternative variants, long and short forms, referred to as p100L and p100S, respectively. Both GFP-p100L and GFP-p100S fusion proteins are located in the cytoplasm of transfected culture cells and microinjected embryonic cells. Analysis of transcripts with Northern blots revealed the presence of p100L and lower amounts of p100S mRNAs from the one-cell stage throughout the life cycle. Whole-mount in situ hybridization shows that p100L and p100S share the same spatiotemporal expression pattern. Their zygotic expression is initially restricted to axial mesoderm precursors during gastrulation, and then spreads over other tissues during segmentation, and finally is constrained to some internal organs at day 5. We also find that Nodal signaling is essential for the zygotic expression of p100. These studies pave the way to understanding in depth the role of p100 during vertebrate embryogenesis.
authors.affiliation: Department of Biological Sciences and Biotechnology, Protein Sciences Laboratory of the MOE, Tsinghua University, 100084, Beijing, PR China.
authors.forename: C T
authors.initials: CT
authors.lastname: Zhao
authors.forename: K H
authors.initials: KH
authors.lastname: Shi
authors.forename: Y
authors.initials: Y
authors.lastname: Su
authors.forename: L Y
authors.initials: LY
authors.lastname: Liang
authors.forename: Y
authors.initials: Y
authors.lastname: Yan
authors.forename: J
authors.initials: J
authors.lastname: Postlethwait
authors.forename: A M
authors.initials: AM
authors.lastname: Meng
mesh_terms: D017398:Alternative Splicing; D000818:Animals; D003593:Cytoplasm / Q000737:chemistry; D004622:Embryo, Mammalian / Q000033:anatomy & histology / Q000737:chemistry / Q000378:metabolism; D004625:Embryo, Nonmammalian; D018507:Gene Expression Regulation, Developmental; D006367:HeLa Cells; D006801:Humans; D017403:In Situ Hybridization; D055457:Nodal Protein; D014176:Protein Biosynthesis; D011506:Proteins / Q000235:genetics*; D012333:RNA, Messenger / Q000032:analysis / Q000096:biosynthesis; D011993:Recombinant Fusion Proteins / Q000032:analysis; D015398:Signal Transduction; D016212:Transforming Growth Factor beta / Q000502:physiology*; D014981:Xenopus / Q000196:embryology* / Q000235:genetics / Q000378:metabolism; D029867:Xenopus Proteins
chemical_list: C526007:NODAL protein, human; D055457:Nodal Protein; D011506:Proteins; D012333:RNA, Messenger; D011993:Recombinant Fusion Proteins; D016212:Transforming Growth Factor beta; D029867:Xenopus Proteins; C075198:PATL2 protein, Xenopus