New Partners in Regulation of Gene Expression: The Enhancer of Trithorax and Polycomb Corto Interacts with Methylated Ribosomal Protein L12 Via Its Chromodomain

Coléno-Costes, Anne; Jang, Suk Min; Vanssay, Augustin de; Rougeot, Julien; Bouceba, Tahar; Randsholt, Neel B.; Gibert, Jean‐Michel; Crom, Stéphane Le; Mouchel-Vielh, Emmanuèle; Bloyer, Sébastien; Peronnet, Frédérique

doi:10.1371/journal.pgen.1003006

Cited by 19 publications

(40 citation statements)

References 67 publications

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“…Despite the consensus that ribosomal subunits are inactive in the nucleus, it has been previously reported that many ribosomal proteins (RPs), rRNA, and some translation factors (including eIF5b) seem to associate with nascent transcripts at polytene chromosomal transcription sites in Drosophila (Brogna et al 2002;Coleno-Costes et al 2012;Rugjee et al 2013). These observations suggest the presence of ribosomal subunits at these sites.…”

Section: Introductionmentioning

confidence: 99%

Visualization of the joining of ribosomal subunits reveals the presence of 80S ribosomes in the nucleus

Al-Jubran

Wen

Abdullahi

et al. 2013

RNA

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In eukaryotes the 40S and 60S ribosomal subunits are assembled in the nucleolus, but there appear to be mechanisms preventing mRNA binding, 80S formation, and initiation of translation in the nucleus. To visualize association between ribosomal subunits, we tagged pairs of Drosophila ribosomal proteins (RPs) located in different subunits with mutually complementing halves of fluorescent proteins. Pairs of tagged RPs expected to interact, or be adjacent in the 80S structure, showed strong fluorescence, while pairs that were not in close proximity did not. Moreover, the complementation signal is found in ribosomal fractions and it was enhanced by translation elongation inhibitors and reduced by initiation inhibitors. Our technique achieved 80S visualization both in cultured cells and in fly tissues in vivo. Notably, while the main 80S signal was in the cytoplasm, clear signals were also seen in the nucleolus and at other nuclear sites. Furthermore, we detected rapid puromycin incorporation in the nucleolus and at transcription sites, providing an independent indication of functional 80S in the nucleolus and 80S association with nascent transcripts.

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Section: Introductionmentioning

confidence: 99%

Visualization of the joining of ribosomal subunits reveals the presence of 80S ribosomes in the nucleus

Al-Jubran

Wen

Abdullahi

et al. 2013

RNA

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“…For example the effect of RpL11 on cMyc is specific for RpL11 since other RPs do not show similar activities. There is also evidence that some RPs might bind chromatin-associated proteins in Drosophila and regulate transcription (Ni et al, 2006; Coleno-Costes et al, 2012). Tri-methylated RpL12, for example, interacts with the Corto protein at the chromosomes and regulates a set of heat response and RP genes (Coleno-Costes et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Fluorescent protein tagging confirms the presence of ribosomal proteins atDrosophilapolytene chromosomes

Rugjee

Chaudhury

Al-Jubran

et al. 2013

PeerJ

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Most ribosomal proteins (RPs) are stoichiometrically incorporated into ribosomal subunits and play essential roles in ribosome biogenesis and function. However, a number of RPs appear to have non-ribosomal functions, which involve direct association with pre-mRNA and transcription factors at transcription sites. The consensus is that the RPs found at these sites are off ribosomal subunits, but observation that different RPs are usually found together suggests that ribosomal or ribosomal-like subunits might be present. Notably, it has previously been reported that antibodies against 20 different RPs stain the same Pol II transcription sites in Drosophila polytene chromosomes. Some concerns, however, were raised about the specificity of the antibodies. To investigate further whether RPs are present at transcription sites in Drosophila, we have generated several transgenic flies expressing RPs (RpS2, RpS5a, RpS9, RpS11, RpS13, RpS18, RpL8, RpL11, RpL32, and RpL36) tagged with either green or red fluorescent protein. Imaging of salivary gland cells showed that these proteins are, as expected, abundant in the cytoplasm as well as in the nucleolus. However, these RPs are also apparent in the nucleus in the region occupied by the chromosomes. Indeed, polytene chromosome immunostaining of a representative subset of tagged RPs confirms the association with transcribed loci. Furthermore, characterization of a strain expressing RpL41 functionally tagged at its native genomic locus with YFP, also showed apparent nuclear accumulation and chromosomal association, suggesting that such a nuclear localization pattern might be a shared feature of RPs and is biologically important. We anticipate that the transgenes described here should provide a useful research tool to visualize ribosomal subunits in Drosophila tissues and to study the non-ribosomal functions of RPs.

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“…kis mutants present ectopic wing veins, and increase ectopic vein phenotypes of mutants affecting the BAP complex component SNR1 [22], [24], [29]. Finally, loss of the ETP Corto [30], [31] induces ectopic veins and enhances ectopic vein phenotypes of several TrxG gene mutants [24], [32], implicating corto in control of vein vs intervein fate. Interestingly, Corto associates with ERK and its scaffold protein MP1 on chromatin, potentially linking ERK signaling to transcriptional regulation mediated by TrxG and ETPs [15], [32], [33].…”

Section: Introductionmentioning

confidence: 91%

The Elongin Complex Antagonizes the Chromatin Factor Corto for Vein versus Intervein Cell Identity in Drosophila Wings

et al. 2013

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Drosophila wings mainly consist of two cell types, vein and intervein cells. Acquisition of either fate depends on specific expression of genes that are controlled by several signaling pathways. The nuclear mechanisms that translate signaling into regulation of gene expression are not completely understood, but they involve chromatin factors from the Trithorax (TrxG) and Enhancers of Trithorax and Polycomb (ETP) families. One of these is the ETP Corto that participates in intervein fate through interaction with the Drosophila EGF Receptor – MAP kinase ERK pathway. Precise mechanisms and molecular targets of Corto in this process are not known. We show here that Corto interacts with the Elongin transcription elongation complex. This complex, that consists of three subunits (Elongin A, B, C), increases RNA polymerase II elongation rate in vitro by suppressing transient pausing. Analysis of phenotypes induced by EloA, B, or C deregulation as well as genetic interactions suggest that the Elongin complex might participate in vein vs intervein specification, and antagonizes corto as well as several TrxG genes in this process. Chromatin immunoprecipitation experiments indicate that Elongin C and Corto bind the vein-promoting gene rhomboid in wing imaginal discs. We propose that Corto and the Elongin complex participate together in vein vs intervein fate, possibly through tissue-specific transcriptional regulation of rhomboid.

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New Partners in Regulation of Gene Expression: The Enhancer of Trithorax and Polycomb Corto Interacts with Methylated Ribosomal Protein L12 Via Its Chromodomain

Cited by 19 publications

References 67 publications

Visualization of the joining of ribosomal subunits reveals the presence of 80S ribosomes in the nucleus

Visualization of the joining of ribosomal subunits reveals the presence of 80S ribosomes in the nucleus

Fluorescent protein tagging confirms the presence of ribosomal proteins atDrosophilapolytene chromosomes

The Elongin Complex Antagonizes the Chromatin Factor Corto for Vein versus Intervein Cell Identity in Drosophila Wings

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