The PAF1 Complex Recruits Integrator to Chromatin Globally to Terminate Non-Productive Transcription

2021 ◽  
Author(s):  
Xinhong Liu ◽  
Ziwei Guo ◽  
Jing Han ◽  
Bin Zhang ◽  
Xiaoyu Hu ◽  
...  
Keyword(s):  
2016 ◽  
Vol 6 (12) ◽  
pp. 3849-3857 ◽  
Author(s):  
Dhananjay Chaturvedi ◽  
Mayu Inaba ◽  
Shane Scoggin ◽  
Michael Buszczak

Abstract Conserved from yeast to humans, the Paf1 complex participates in a number of diverse processes including transcriptional initiation and polyadenylation. This complex typically includes five proteins: Paf1, Rtf1, Cdc73, Leo1, and Ctr9. Previous efforts identified clear Drosophila homologs of Paf1, Rtf1, and Cdc73 based on sequence similarity. Further work showed that these proteins help to regulate gene expression and are required for viability. To date, a Drosophila homolog of Ctr9 has remained uncharacterized. Here, we show that the gene CG2469 encodes a functional Drosophila Ctr9 homolog. Both human and Drosophila Ctr9 localize to the nuclei of Drosophila cells and appear enriched in histone locus bodies. RNAi knockdown of Drosophila Ctr9 results in a germline stem cell loss phenotype marked by defects in the morphology of germ cell nuclei. A molecular null mutation of Drosophila Ctr9 results in lethality and a human cDNA CTR9 transgene rescues this phenotype. Clonal analysis in the ovary using this null allele reveals that loss of Drosophila Ctr9 results in a reduction of global levels of histone H3 trimethylation of lysine 4 (H3K4me3), but does not compromise the maintenance of stem cells in ovaries. Given the differences between the null mutant and RNAi knockdown phenotypes, the germ cell defects caused by RNAi likely result from the combined loss of Drosophila Ctr9 and other unidentified genes. These data provide further evidence that the function of this Paf1 complex component is conserved across species.


2015 ◽  
Vol 8 (12) ◽  
pp. 1816-1819 ◽  
Author(s):  
Ying Cao ◽  
Liguo Wen ◽  
Zheng Wang ◽  
Ligeng Ma
Keyword(s):  

2017 ◽  
Vol 42 (10) ◽  
pp. 788-798 ◽  
Author(s):  
S. Branden Van Oss ◽  
Christine E. Cucinotta ◽  
Karen M. Arndt
Keyword(s):  

2018 ◽  
Vol 9 (1) ◽  
Author(s):  
Ying Xie ◽  
Minying Zheng ◽  
Xinlei Chu ◽  
Yue Chen ◽  
Huisha Xu ◽  
...  

2010 ◽  
Vol 153 (2) ◽  
pp. 821-831 ◽  
Author(s):  
Sunchung Park ◽  
Sookyung Oh ◽  
Julissa Ek-Ramos ◽  
Steven van Nocker

2019 ◽  
Vol 22 (6) ◽  
pp. 863-874 ◽  
Author(s):  
Lindsey D. Goodman ◽  
Mercedes Prudencio ◽  
Nicholas J. Kramer ◽  
Luis F. Martinez-Ramirez ◽  
Ananth R. Srinivasan ◽  
...  
Keyword(s):  

2003 ◽  
Vol 23 (8) ◽  
pp. 2800-2820 ◽  
Author(s):  
Mark J. Swanson ◽  
Hongfang Qiu ◽  
Laarni Sumibcay ◽  
Anna Krueger ◽  
Soon-ja Kim ◽  
...  

ABSTRACT Transcriptional activators interact with multisubunit coactivators that modify chromatin structure or recruit the general transcriptional machinery to their target genes. Budding yeast cells respond to amino acid starvation by inducing an activator of amino acid biosynthetic genes, Gcn4p. We conducted a comprehensive analysis of viable mutants affecting known coactivator subunits from the Saccharomyces Genome Deletion Project for defects in activation by Gcn4p in vivo. The results confirm previous findings that Gcn4p requires SAGA, SWI/SNF, and SRB mediator (SRB/MED) and identify key nonessential subunits of these complexes required for activation. Among the numerous histone acetyltransferases examined, only that present in SAGA, Gcn5p, was required by Gcn4p. We also uncovered a dependence on CCR4-NOT, RSC, and the Paf1 complex. In vitro binding experiments suggest that the Gcn4p activation domain interacts specifically with CCR4-NOT and RSC in addition to SAGA, SWI/SNF, and SRB/MED. Chromatin immunoprecipitation experiments show that Mbf1p, SAGA, SWI/SNF, SRB/MED, RSC, CCR4-NOT, and the Paf1 complex all are recruited by Gcn4p to one of its target genes (ARG1) in vivo. We observed considerable differences in coactivator requirements among several Gcn4p-dependent promoters; thus, only a subset of the array of coactivators that can be recruited by Gcn4p is required at a given target gene in vivo.


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