Direct interaction between Teashirt and Sex combs reduced proteins, via Tsh's acidic domain, is essential for specifying the identity of the prothorax in Drosophila
Autor: | Laurent Fasano, Pascale Malapert, Armel Gallet, Frédéric Leroy, Ouarda Taghli-Lamallem, Christine Vola, Stephen Kerridge |
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Přispěvatelé: | Institut de Biologie du Développement de Marseille (IBDM), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS) |
Rok vydání: | 2007 |
Předmět: |
endocrine system
Transcriptional repression endocrine system diseases Morphogenesis Context (language use) [SDV.BC]Life Sciences [q-bio]/Cellular Biology behavioral disciplines and activities 03 medical and health sciences 0302 clinical medicine Animals Drosophila Proteins Binding site Drosophila (subgenus) Hox gene Molecular Biology 030304 developmental biology Genetics 0303 health sciences Sex combs reduced Binding Sites biology Trunk Embryo Cell Biology Thorax biology.organism_classification Hox Repressor Proteins Prothorax Prothoracic identity Drosophila Teashirt 030217 neurology & neurosurgery Function (biology) hormones hormone substitutes and hormone antagonists Transcription Factors Developmental Biology |
Zdroj: | HAL Developmental Biology Developmental Biology, 2007, 307, pp.142-151 Developmental Biology, Elsevier, 2007, 307, pp.142-151 |
ISSN: | 0012-1606 1095-564X |
DOI: | 10.1016/j.ydbio.2007.04.028 |
Popis: | teashirt (tsh) encodes a zinc-finger protein that is thought to be part of a network that contributes to regionalization of the Drosophila embryo and establishes the domains of Hox protein function. tsh and the Hox gene Sex combs reduced (Scr) are essential to establish the identity of the first thoracic segment. We used the development of the first thoracic segment as a paradigm for Scr dependent regional morphological distinctions. In this specific context, we asked whether Tsh protein could have a direct influence on Scr activity. Here we present evidence that Tsh interacts directly with Scr and this interaction depends in part on the presence of a short domain located in the N-terminal half of Teashirt called “acidic domain”. In vivo, expression of full length Tsh can rescue the tsh null phenotype throughout the trunk whereas Tsh lacking the Scr interacting domain rescues all the trunk defects except in the prothorax. We suggest this provides insights into the mechanism by which Tsh, in concert with Scr, specifies the prothoracic identity. |
Databáze: | OpenAIRE |
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