scholarly journals Unique and Shared Roles for Histone H3K36 Methylation States in Transcription Regulation Functions

Cell Reports ◽  
2020 ◽  
Vol 31 (10) ◽  
pp. 107751 ◽  
Author(s):  
Julia V. DiFiore ◽  
Travis S. Ptacek ◽  
Yi Wang ◽  
Bing Li ◽  
Jeremy M. Simon ◽  
...  
2017 ◽  
Vol 114 (40) ◽  
pp. E8402-E8410 ◽  
Author(s):  
Reed B. Wickner ◽  
Amy C. Kelly ◽  
Evgeny E. Bezsonov ◽  
Herman K. Edskes

The yeast prions [PSI+] and [URE3] are folded in-register parallel β-sheet amyloids of Sup35p and Ure2p, respectively. In a screen for antiprion systems curing [PSI+] without protein overproduction, we detected Siw14p as an antiprion element. An array of genetic tests confirmed that many variants of [PSI+] arising in the absence of Siw14p are cured by restoring normal levels of the protein. Siw14p is a pyrophosphatase specifically cleaving the β phosphate from 5-diphosphoinositol pentakisphosphate (5PP-IP5), suggesting that increased levels of this or some other inositol polyphosphate favors [PSI+] propagation. In support of this notion, we found that nearly all variants of [PSI+] isolated in a WT strain were lost upon loss of ARG82, which encodes inositol polyphosphate multikinase. Inactivation of the Arg82p kinase by D131A and K133A mutations (preserving Arg82p’s nonkinase transcription regulation functions) resulted the loss of its ability to support [PSI+] propagation. The loss of [PSI+] in arg82Δ is independent of Hsp104’s antiprion activity. [PSI+] variants requiring Arg82p could propagate in ipk1Δ (IP5 kinase), kcs1Δ (IP6 5-kinase), vip1Δ (IP6 1-kinase), ddp1Δ (inositol pyrophosphatase), or kcs1Δ vip1Δ mutants but not in ipk1Δ kcs1Δ or ddp1Δ kcs1Δ double mutants. Thus, nearly all [PSI+] prion variants require inositol poly-/pyrophosphates for their propagation, and at least IP6 or 5PP-IP4 can support [PSI+] propagation.


2007 ◽  
Vol 28 (4) ◽  
pp. 1348-1360 ◽  
Author(s):  
Lin Xu ◽  
Zhong Zhao ◽  
Aiwu Dong ◽  
Ludivine Soubigou-Taconnat ◽  
Jean-Pierre Renou ◽  
...  

ABSTRACT Histone lysines can be mono-, di-, or trimethylated, providing an ample magnitude of epigenetic information for transcription regulation. In fungi, SET2 is the sole methyltransferase responsible for mono-, di-, and trimethylation of H3K36. Here we show that in Arabidopsis thaliana, the degree of H3K36 methylation is regulated by distinct methyltransferases. The SET2 homologs SDG8 and SDG26 each can methylate oligonucleosomes in vitro, and both proteins are localized in the nucleus. While the previously reported loss-of-function sdg8 mutants have an early-flowering phenotype, the loss-of-function sdg26 mutants show a late-flowering phenotype. Consistently, several MADS-box flowering repressors are down-regulated by sdg8 but up-regulated by sdg26. The sdg8 but not the sdg26 mutant plants show a dramatically reduced level of both di- and trimethyl-H3K36 and an increased level of monomethyl-H3K36. SDG8 is thus specifically required for di- and trimethylation of H3K36. Our results further establish that H3K36 di- and tri- but not monomethylation correlates with transcription activation. Finally, we show that SDG8 and VIP4, which encodes a component of the PAF1 complex, act independently and synergistically in transcription regulation. Together our results reveal that the deposition of H3K36 methylation is finely regulated, possibly to cope with the complex regulation of growth and development in higher eukaryotes.


Author(s):  
Della Jacobsen

Responsibility for a corporate Internet programme will typically go to an individual within the information services or computer resources group. The information professional given this responsibility must have the communication skills needed to forge effective relationships between a diverse array of individuals, functional work groups, and departments. The opportunity to establish effective working relationships is realized when common goals are shared, roles are defined, information is communicated, and conflicts are resolved.


2012 ◽  
Vol 39 (9) ◽  
pp. 843-852 ◽  
Author(s):  
Hui LIU ◽  
Zi-Heng Zhuang ◽  
Ji-Hong GUAN ◽  
Shui-Geng ZHOU

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