ArticleBMC molecular biology2009
The zinc finger protein Zn72D and DEAD box helicase Belle interact and control maleless mRNA and protein levels.
Article in BMC molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Proteomics insights into fragile X syndrome: Unraveling molecular mechanisms and therapeutic avenues.Neurobiology of disease · 2024Review
- Combining affinity purification and mass spectrometry to define the network of the nuclear proteins interacting with the N-terminal region of FMRP.Frontiers in molecular biosciences · 2022Article
- One Actor, Multiple Roles: The Performances of Cryptochrome inFrontiers in physiology · 2020Review
- The RNA Helicase BELLE Is Involved in Circadian Rhythmicity and in Transposons Regulation inFrontiers in physiology · 2019Article
- ZFR coordinates crosstalk between RNA decay and transcription in innate immunity.Nature communications · 2018Article
- NF45 dimerizes with NF90, Zfr and SPNR via a conserved domain that has a nucleotidyltransferase fold.Nucleic acids research · 2012Article
- A late phase of germ plasm accumulation during Drosophila oogenesis requires lost and rumpelstiltskin.Development (Cambridge, England) · 2011Article
- DEAD-box RNA helicase Belle/DDX3 and the RNA interference pathway promote mitotic chromosome segregation.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The microRNA pathway regulates the temporal pattern of Notch signaling in Drosophila follicle cells.Development (Cambridge, England) · 2011Article
- Mutation of the DEAD-box helicase belle downregulates the cyclin-dependent kinase inhibitor Dacapo.Cell cycle (Georgetown, Tex.) · 2010Article
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3 authors.
Funding
Abstract
backgroundThe Male Specific Lethal (MSL) complex is enriched on the single X chromosome in male Drosophila cells and functions to upregulate X-linked gene expression and equalize X-linked gene dosage with XX females. The zinc finger protein Zn72D is required for productive splicing of the maleless (mle) transcript, which encodes an essential subunit of the MSL complex. In the absence of Zn72D, MLE levels are decreased, and as a result, the MSL complex no longer localizes to the X chromosome and dosage compensation is disrupted. To understand the molecular basis of Zn72D function, we identified proteins that interact with Zn72D.
resultsAmong several proteins that associate with Zn72D, we found the DEAD box helicase Belle (Bel). Simultaneous knockdown of Zn72D and bel restored MSL complex localization to the X chromosome and dosage compensation. MLE protein was restored to 70% of wild-type levels, although the level of productively spliced mle transcript was still four-fold lower than in wild-type cells. The increase in production of MLE protein relative to the amount of correctly spliced mle mRNA could not be attributed to an alteration in MLE stability.
conclusionThese data indicate that Zn72D and Bel work together to control mle splicing and protein levels. Thus Zn72D and Bel may be factors that coordinate splicing and translational regulation.
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