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Convergent genes shape budding yeast pericentromeres 期刊论文
NATURE, 2020
作者:  Yin, Xuefan;  Jin, Jicheng;  Soljacic, Marin;  Peng, Chao;  Zhen, Bo
收藏  |  浏览/下载:43/0  |  提交时间:2020/07/03

The three-dimensional structure of pericentromeres in budding yeast is defined by convergent genes, which mark pericentromere borders and trap cohesin complexes loaded at centromeres, generating an architecture that allows correct chromosome segregation.


The three-dimensional architecture of the genome governs its maintenance, expression and transmission. The cohesin protein complex organizes the genome by topologically linking distant loci, and is highly enriched in specialized chromosomal domains surrounding centromeres, called pericentromeres(1-6). Here we report the three-dimensional structure of pericentromeres in budding yeast (Saccharomyces cerevisiae) and establish the relationship between genome organization and function. We find that convergent genes mark pericentromere borders and, together with core centromeres, define their structure and function by positioning cohesin. Centromeres load cohesin, and convergent genes at pericentromere borders trap it. Each side of the pericentromere is organized into a looped conformation, with border convergent genes at the base. Microtubule attachment extends a single pericentromere loop, size-limited by convergent genes at its borders. Reorienting genes at borders into a tandem configuration repositions cohesin, enlarges the pericentromere and impairs chromosome biorientation during mitosis. Thus, the linear arrangement of transcriptional units together with targeted cohesin loading shapes pericentromeres into a structure that is competent for chromosome segregation. Our results reveal the architecture of the chromosomal region within which kinetochores are embedded, as well as the restructuring caused by microtubule attachment. Furthermore, we establish a direct, causal relationship between the three-dimensional genome organization of a specific chromosomal domain and cellular function.


  
Host-mediated ubiquitination of a mycobacterial protein suppresses immunity 期刊论文
NATURE, 2020, 577 (7792) : 682-+
作者:  Nahas, Y.;  Prokhorenko, S.;  Fischer, J.;  Xu, B.;  Carretero, C.;  Prosandeev, S.;  Bibes, M.;  Fusil, S.;  Dkhil, B.;  Garcia, V.;  Bellaiche, L.
收藏  |  浏览/下载:24/0  |  提交时间:2020/07/03

Mycobacterium tuberculosis suppresses the production of inflammatory cytokines by host cells through the host-mediated ubiquitination of a mycobacterial protein, enhancing the interaction of a host signalling inhibitor with another signalling molecule.


Mycobacterium tuberculosis is an intracellular pathogen that uses several strategies to interfere with the signalling functions of host immune molecules. Many other bacterial pathogens exploit the host ubiquitination system to promote pathogenesis(1,2), but whether this same system modulates the ubiquitination of M. tuberculosis proteins is unknown. Here we report that the host E3 ubiquitin ligase ANAPC2-a core subunit of the anaphase-promoting complex/cyclosome-interacts with the mycobacterial protein Rv0222 and promotes the attachment of lysine-11-linked ubiquitin chains to lysine 76 of Rv0222 in order to suppress the expression of proinflammatory cytokines. Inhibition of ANAPC2 by specific short hairpin RNA abolishes the inhibitory effect of Rv0222 on proinflammatory responses. Moreover, mutation of the ubiquitination site on Rv0222 impairs the inhibition of proinflammatory cytokines by Rv0222 and reduces virulence during infection in mice. Mechanistically, lysine-11-linked ubiquitination of Rv0222 by ANAPC2 facilitates the recruitment of the protein tyrosine phosphatase SHP1 to the adaptor protein TRAF6, preventing the lysine-63-linked ubiquitination and activation of TRAF6. Our findings identify a previously unrecognized mechanism that M. tuberculosis uses to suppress host immunity, and provide insights relevant to the development of effective immunomodulators that target M. tuberculosis.


  
Nevada National Security Site Environmental Report 2010, Attachment A: Site Description 科技报告
来源:US Department of Energy (DOE). 出版年: 2011
作者:  C. Wills, ed.
收藏  |  浏览/下载:7/0  |  提交时间:2019/04/05
NNSSER  Nevada National Security Site  Environmental Report  NNSS  2010  Attachment A: Site Description  
Environmental Baseline Survey Report for the Title Transfer of Parcel ED-9 at the East Tennessee Technology Park, Oak Ridge, Tennessee 科技报告
来源:US Department of Energy (DOE). 出版年: 2010
作者:  SAIC
收藏  |  浏览/下载:7/0  |  提交时间:2019/04/05
EBS Report  Attachment A  Title Transfer  Parcel ED-9