Role of nuclear WW domains and proline-rich proteins in dinoflagellate transcription

Autor: Yvonne Bhaud, Delphine Guillebault, Hervé Moreau, Evelyne Derelle
Přispěvatelé: Biologie intégrative des organismes marins (BIOM), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Observatoire océanologique de Banyuls (OOB), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS)
Rok vydání: 2001
Předmět:
Proline
Transcription
Genetic
[SDV]Life Sciences [q-bio]
Recombinant Fusion Proteins
Molecular Sequence Data
Protozoan Proteins
[SDV.BC]Life Sciences [q-bio]/Cellular Biology
Biology
Ligands
Microbiology
[SDV.MP.PRO]Life Sciences [q-bio]/Microbiology and Parasitology/Protistology
WW domain
03 medical and health sciences
Mice
0302 clinical medicine
Transcription (biology)
Gene expression
Animals
Drosophila Proteins
Humans
Amino Acid Sequence
Nuclear protein
Phosphorylation
ComputingMilieux_MISCELLANEOUS
030304 developmental biology
Zinc finger
Cell Nucleus
0303 health sciences
General transcription factor
Sequence Homology
Amino Acid
Helix-Loop-Helix Motifs
Nuclear Proteins
Crypthecodinium cohnii
DNA
biology.organism_classification
Molecular biology
Cell biology
Protein Structure
Tertiary
Histone
Gene Expression Regulation
biology.protein
Dinoflagellida
Proline-Rich Protein Domains
Peptides
030217 neurology & neurosurgery
Transcription Factors
Zdroj: Protist
Protist, Elsevier, 2001, 152 (2), pp.127-138. ⟨10.1078/1434-4610-00051⟩
ISSN: 1434-4610
DOI: 10.1078/1434-4610-00051⟩
Popis: Summary Dinoflagellates are unique among eukaryotes in their lack of histones and nucleosomes, and permanently condensed chromosomes. These unusual features raise questions as how chromatin condensation and gene expression are achieved. In this study, we investigated nuclear proteins potentially implicated in the regulation of the transcription. Dinap1 is a dinoflagellate nuclear protein that has a WW domain and is synthesized mainly in G1 and S phases of the cell cycle. In this study, we found that Dip1, a proline-rich potential ligand of Dinap1, and DapC, a Dip1 potential ligand, were both present in the nucleus of Crypthecodinium cohnii during the G1 phase. Dip1 contained a PPXY motif, and its domain organization was similar to that of the splicing factor FBP21 in that it possessed one zinc finger and two WW domains. Although DapC has no known homolog, 22 repeats of a PPXPXGX heptapeptide were identified at the N-terminus, and this structure is similar to that of the C-terminal part of the mouse splicing factor SAP62. Dinap1 was co-precipitated with Dip1 and DapC in vitro and in vivo, but despite their nuclear location, these three proteins did not bind directly to DNA. Dinap1 activated up to 40% of the basal transcription activity of C. cohnii in an in vitro assay, whereas DapC inhibited it by 40% and Dip1 had no effect. These dinoflagellate proteins appear to be the subunits of a nuclear complex that may be involved in regulating transcription.
Databáze: OpenAIRE
Externí odkaz: