Binding of Drosophila maternal Mamo protein to chromatin and specific DNA sequences

Hira, Seiji; Okamoto, Tomoko; Fujiwara, Masato; Kita, Hiroaki; Kobayashi, Satoru; Mukai, Masanori

doi:10.1016/j.bbrc.2013.07.045

Cited by 12 publications

(20 citation statements)

References 18 publications

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“…Because a mamo mutant specific for the short isoform was not available, we used overexpression experiments to evaluate the function of the short isoform. Previously, we generated a UAS line (UAS-MZD-FLAG) to produce a truncated Mamo protein lacking the BTB/POZ domain 18 (hereafter, referred to as MamoAF). When it was expressed in embryos under the control of matα4-Gal-VP16 , MamoAF preferentially accumulated in the nuclear fraction (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…To determine whether MamoAF directly binds vas , we performed electrophoretic mobility shift assays (EMSA) and chromatin immunoprecipitation assays (ChIP) on MamoAF-OE embryos. Although the upstream region (~ 2 kbp) of the vas gene does not contain cis-elements containing a Mamo-binding consensus sequence 18 , the first intron of vas contains several possible cis-elements, suggesting that MamoAF activates vas through previously unidentified cis-elements in the first intron. One such cis-element, hereafter referred to as the vas -A element, is conserved among several Drosophila species (Supplementary Fig.…”

Section: Resultsmentioning

confidence: 99%

“…However, MamoAF could also activate vas transcription through other cis-elements that remain to be identified. We previously reported that Mamo has a role in the regulation of chromatin structure 18 . Therefore, Mamo may regulate chromatin structure, in addition to transcriptional activation, to promote vas expression.…”

Section: Discussionmentioning

confidence: 99%

“…Mamo protein is detectable in the nuclei of PGCs at stage 15, in which vas is actively expressed 17 . Mamo can bind chromosomes when Mamo is expressed in salivary gland cells 18 . Biochemical analyses demonstrated that the C 2 H 2 Zn-finger domains of Mamo directly bind specific DNA sequences 18 .…”

Section: Introductionmentioning

confidence: 99%

“…Mamo can bind chromosomes when Mamo is expressed in salivary gland cells 18 . Biochemical analyses demonstrated that the C 2 H 2 Zn-finger domains of Mamo directly bind specific DNA sequences 18 . C 2 H 2 Zn-finger domains are among the most common domains in the transcription factors of metazoans 19 .…”

Section: Introductionmentioning

confidence: 99%

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A truncated form of a transcription factor Mamo activates vasa in Drosophila embryos

et al. 2019

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Expression of the vasa gene is associated with germline establishment. Therefore, identification of vasa activator(s) should provide insights into germline development. However, the genes sufficient for vasa activation remain unknown. Previously, we showed that the BTB/POZ-Zn-finger protein Mamo is necessary for vasa expression in Drosophila. Here, we show that the truncated Mamo lacking the BTB/POZ domain (MamoAF) is a potent vasa activator. Overexpression of MamoAF was sufficient to induce vasa expression in both primordial germ cells and brain. Indeed, Mamo mRNA encoding a truncated Mamo isoform, which is similar to MamoAF, was predominantly expressed in primordial germ cells. The results of our genetic and biochemical studies showed that MamoAF, together with CBP, epigenetically activates vasa expression. Furthermore, MamoAF and the germline transcriptional activator OvoB exhibited synergy in activating vasa transcription. We propose that a Mamo-mediated network of epigenetic and transcriptional regulators activates vasa expression.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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A truncated form of a transcription factor Mamo activates vasa in Drosophila embryos

et al. 2019

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Hormone-controlled changes in the differentiation state of post-mitotic neurons

et al. 2022

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An RNAi screen to identify proteins required for cohesion rejuvenation during meiotic prophase in Drosophila oocytes

Haseeb,

Bernys,

Dickert

et al. 2024

G3: Genes, Genomes, Genetics

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Accurate chromosome segregation during meiosis requires maintenance of sister chromatid cohesion, initially established during premeiotic S phase. In human oocytes, DNA replication and cohesion establishment occur decades before chromosome segregation and deterioration of meiotic cohesion is one factor that leads to increased segregation errors as women age. Our previous work led us to propose that a cohesion rejuvenation program operates to establish new cohesive linkages during meiotic prophase in Drosophila oocytes and depends on the cohesin loader Nipped-B and the cohesion establishment factor Eco. In support of this model, we recently demonstrated that chromosome-associated cohesin turns over extensively during meiotic prophase and failure to load cohesin onto chromosomes after premeiotic S phase results in arm cohesion defects in Drosophila oocytes. To identify proteins required for prophase cohesion rejuvenation but not S phase establishment, we conducted a Gal4-UAS inducible RNAi screen that utilized two distinct germline drivers. Using this strategy, we identified 29 gene products for which hairpin expression during meiotic prophase, but not premeiotic S phase, significantly increased segregation errors. Prophase knockdown of Brahma or Pumilio, two positives with functional links to the cohesin loader, caused a significant elevation in the missegregation of recombinant homologs, a phenotype consistent with premature loss of arm cohesion. Moreover, fluorescence in situ hybridization confirmed that Brahma, Pumilio and Nipped-B are required during meiotic prophase for maintenance of arm cohesion. Our data support the model that Brahma and Pumilio regulate Nipped-B dependent cohesin loading during rejuvenation. Future analyses will better define the mechanism(s) that govern meiotic cohesion rejuvenation and whether additional prophase-specific positives function in this process.

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Binding of Drosophila maternal Mamo protein to chromatin and specific DNA sequences

Cited by 12 publications

References 18 publications

A truncated form of a transcription factor Mamo activates vasa in Drosophila embryos

A truncated form of a transcription factor Mamo activates vasa in Drosophila embryos

Hormone-controlled changes in the differentiation state of post-mitotic neurons

An RNAi screen to identify proteins required for cohesion rejuvenation during meiotic prophase in Drosophila oocytes

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