scholarly journals Transcriptional Initiation in Ribosomal Protein Genes in the Fission Yeast Schizosaccharomyces pombe

Author(s):  
Diego A. Rojas ◽  
Sandra Moreira-Ramos ◽  
Fabiola Urbina ◽  
Edio Maldonado
2015 ◽  
Vol 35 (17) ◽  
pp. 2947-2964 ◽  
Author(s):  
Bhawana Uprety ◽  
Rwik Sen ◽  
Sukesh R. Bhaumik

NuA4 (nucleosome acetyltransferase of H4) promotes transcriptional initiation of TFIID (a complex of TBP and TBP-associated factors [TAFs])-dependent ribosomal protein genes involved in ribosome biogenesis. However, it is not clearly understood how NuA4 regulates the transcription of ribosomal protein genes. Here, we show that NuA4 is recruited to the promoters of ribosomal protein genes, such asRPS5,RPL2B, andRPS11B, for TFIID recruitment to initiate transcription, and the recruitment of NuA4 to these promoters is impaired in the absence of its Eaf1p component. Intriguingly, impaired NuA4 recruitment in aΔeaf1strain depletes recruitment of TFIID (a TAF-dependent form of TBP) but not the TAF-independent form of TBP to the promoters of ribosomal protein genes. However, in the absence of NuA4, SAGA (Spt-Ada-Gcn5-acetyltransferase) is involved in targeting the TAF-independent form of TBP to the promoters of ribosomal protein genes for transcriptional initiation. Thus, NuA4 plays an important role in targeting TFIID to the promoters of ribosomal protein genes for transcriptional initiationin vivo. Such a function is mediated via its targeted histone acetyltransferase activity. In the absence of NuA4, ribosomal protein genes lose TFIID dependency and become SAGA dependent for transcriptional initiation. Collectively, these results provide significant insights into the regulation of ribosomal protein gene expression and, hence, ribosome biogenesis and functions.


1986 ◽  
Vol 10 (5) ◽  
pp. 365-370 ◽  
Author(s):  
Roswitha Nischt ◽  
Eduardo Th�roff ◽  
Norbert F. K�ufer

Genome ◽  
2000 ◽  
Vol 43 (1) ◽  
pp. 205-207 ◽  
Author(s):  
Christine Bonnet ◽  
Eric Perret ◽  
Odile Bonnin ◽  
André Picard ◽  
Daniel Caput ◽  
...  

In the fission yeast, four genes (rpaP1-1, rpaP1-3,rpaP2-2, and rpaP2-4) encoding two variants of the RpaP1 and RpaP2 ribosomal proteins (rp) have been characterized. We have identified cDNA for additional variants called RpaP1.5 and RpaP2.6. Sequence comparison suggests that RpaP1.5 diverged before RpaP1.1 and RpaP1.3 and that RpaP2.6 is closer to RpaP2.2 than to RpaP2.4. The corresponding genes, rpaP1-5 and rpaP2-6, are transcribed coordinately with other rp genes. Key words: acidic ribosomal protein, RpaP1.5, RpaP2.6, rpaP1-5, rpaP2-6, variants.


2013 ◽  
Vol 12 (3) ◽  
pp. 450-459 ◽  
Author(s):  
Rongpeng Li ◽  
Xuesong Li ◽  
Lei Sun ◽  
Feifei Chen ◽  
Zhenxing Liu ◽  
...  

ABSTRACTDeletion of ribosomal protein L32 genes resulted in a nonsexual flocculation of fission yeast. Nonsexual flocculation also occurred when two other ribosomal protein genes,rpl21-2andrpl9-2, were deleted. However, deletion of two nonribosomal protein genes,mpgandfbp, did not cause flocculation. Overall transcript levels ofrpl32inrpl32-1Δ andrpl32-2Δ cells were reduced by 35.9% and 46.9%, respectively, and overall ribosome levels inrpl32-1Δ andrpl32-2Δ cells dropped 31.1% and 27.8%, respectively, compared to wild-type cells. Interestingly, ribosome protein expression levels and ribosome levels were also reduced greatly in sexually flocculating diploid YHL6381/WT (h+/h−) cells compared to a mixture of YHL6381 (h+) and WT (h−) nonflocculating haploid cells. Transcriptome analysis indicated that the reduction of ribosomal levels in sexual flocculating cells was caused by more-extensive suppression of ribosomal biosynthesis gene expression, while the reduction of ribosomal levels caused by deleting ribosomal protein genes in nonsexual flocculating cells was due to an imbalance between ribosomal proteins. We propose that once the reduction of ribosomal levels is below a certain threshold value, flocculation is triggered.


2018 ◽  
Vol 38 (14) ◽  
Author(s):  
Bhawana Uprety ◽  
Amala Kaja ◽  
Sukesh R. Bhaumik

ABSTRACT TOR (target of rapamycin) has been previously implicated in transcriptional stimulation of the ribosomal protein (RP) genes via enhanced recruitment of NuA4 (nucleosome acetyltransferase of H4) to the promoters. However, it is not clearly understood how TOR enhances NuA4 recruitment to the promoters of the RP genes. Here we show that TOR facilitates the recruitment of the 19S proteasome subcomplex to the activator to enhance the targeting of NuA4 to the promoters of the RP genes. NuA4, in turn, promotes the recruitment of TFIID (transcription factor IID, composed of TATA box-binding protein [TBP] and a set of TBP-associated factors [TAFs]) and RNA polymerase II to the promoters of the RP genes to enhance transcriptional initiation. Therefore, our results demonstrate that TOR facilitates the recruitment of the 19S proteasome subcomplex to the promoters of the RP genes to promote the targeting of NuA4 for enhanced preinitiation complex (PIC) formation and consequently transcriptional initiation, hence illuminating TOR regulation of RP gene activation. Further, our results reveal that TOR differentially regulates PIC formation (and hence transcription) at the non-RP genes, thus demonstrating a complex regulation of gene activation by TOR.


2016 ◽  
Vol 36 (6) ◽  
pp. 992-1006 ◽  
Author(s):  
Bhawana Uprety ◽  
Amala Kaja ◽  
Jannatul Ferdoush ◽  
Rwik Sen ◽  
Sukesh R. Bhaumik

NuA4 histone lysine (K) acetyltransferase (KAT) promotes transcriptional initiation of TATA-binding protein (TBP)-associated factor (TAF)-dependent ribosomal protein genes. TAFs have also been recently found to enhance antisense transcription from the 3′ end of theGAL10coding sequence. However, it remains unknown whether, like sense transcription of the ribosomal protein genes, TAF-dependent antisense transcription ofGAL10also requires NuA4 KAT. Here, we show that NuA4 KAT associates with theGAL10antisense transcription initiation site at the 3′ end of the coding sequence. Such association of NuA4 KAT depends on the Reb1p-binding site that recruits Reb1p activator to theGAL10antisense transcription initiation site. Targeted recruitment of NuA4 KAT to theGAL10antisense transcription initiation site promotesGAL10antisense transcription. Like NuA4 KAT, histone H3 K4/36 methyltransferases and histone H2B ubiquitin conjugase facilitateGAL10antisense transcription, while the Swi/Snf and SAGA chromatin remodeling/modification factors are dispensable for antisense, but not sense, transcription ofGAL10. Taken together, our results demonstrate for the first time the roles of NuA4 KAT and other chromatin regulatory factors in controlling antisense transcription, thus illuminating chromatin regulation of antisense transcription.


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