Dynamic changes of the post-translational O-GIcNAc modification （O-GIcNAcylation） are controlled by O-linked β-N-acetylglucosamine （O-GIcNAc） transferase （OGT） and the glycoside hydrolase O-GIcNAcase （OGA） in...Dynamic changes of the post-translational O-GIcNAc modification （O-GIcNAcylation） are controlled by O-linked β-N-acetylglucosamine （O-GIcNAc） transferase （OGT） and the glycoside hydrolase O-GIcNAcase （OGA） in cells. O-GIcNAcylation often occurs on serine （Ser） and threonine （Thr） residues of the specific substrate proteins via the addition of O-GIcNAc group by OGT. It has been known that O-GIcNAcylation is not only involved in many fundamental cellular processes, but also plays an important role in cancer development through various mechanisms. Recently, accumulating data reveal that O-GIcNAcylation at histones or non-histone proteins can lead to the start of the subsequent biological processes, suggesting that O-GIcNAcylation as ＇protein code＇ or ＇histone code＇ may provide recognition platforms or executive instructions for subse- quent recruitment of proteins to carry out the specific functions. In this review, we summarize the interaction of O-GIcNAcylation and epigenetic changes, introduce recent research findings that link crosstalk between O- GIcNAcylation and epigenetic changes, and speculate on the potential coordination role of O-GIcNAcylation with epigenetic changes in intracellular biological processes.展开更多
The BCCIP （BRCA2. and CDKNIA-interacting protein） is an important cofactor for BRCA2 in tumor suppression. Although the low expression of BCClP is observed in multiple clinically diagnosed primary tumor tissues such...The BCCIP （BRCA2. and CDKNIA-interacting protein） is an important cofactor for BRCA2 in tumor suppression. Although the low expression of BCClP is observed in multiple clinically diagnosed primary tumor tissues such as ovarian cancer, renal cell carcinoma and col- orectal carcinoma, the mechanism of how BCCIP is regulated in cells is still unclear. The human INO80/YY1 chromatin remodeling complex composed of 15 sub- units catalyzes ATP-dependent sliding of nucleosomes along DNA. Here, we first report that BCClP is a novel target gene of the INO80/YY1 complex by presenting a series of experimental evidence. Gene expression studies combined with siRNA knockdown data locked candidate genes including BCCIP of the INO80/YY1 complex. Silencing or over-expressing the subunits of the INO80/YY1 complex regulates the expression level of BCCIP both in mRNA and proteins in cells. Also, the functions of INO80/YY1 complex in regulating the transactivation of BCCIP were confirmed by luciferase reporter assays. Chromatin immunoprecipitation （CHIP） experiments clarify the enrichment of INO80 and YY1 at ＋0.17 kb downstream of the BCClP transcriptional start site. However, this enrichment is significantly inhibited by either knocking down INO80 or YY1, suggesting the existence of both INO80 and YY1 is required for recruiting the INO80/YY1 complex to BCClP promoter region. Our findings strongly indicate that BCClP is a potential target gene of the INO80/YY1 complex.展开更多
Current research has dem on strated that the dynamic distribution of histone variant H2A.Z at specific loci can be regulated by ATP-dependent chromatin remodelers, histone chaperones and histone post-translational mod...Current research has dem on strated that the dynamic distribution of histone variant H2A.Z at specific loci can be regulated by ATP-dependent chromatin remodelers, histone chaperones and histone post-translational modifications (PTMs).展开更多
基金This work was supported by the National Natural Science Foundation of China （Grant No. 31571316） and the Project of Jilin Province Science and Technology Development Program （No. 20140414057GH）.
文摘Dynamic changes of the post-translational O-GIcNAc modification （O-GIcNAcylation） are controlled by O-linked β-N-acetylglucosamine （O-GIcNAc） transferase （OGT） and the glycoside hydrolase O-GIcNAcase （OGA） in cells. O-GIcNAcylation often occurs on serine （Ser） and threonine （Thr） residues of the specific substrate proteins via the addition of O-GIcNAc group by OGT. It has been known that O-GIcNAcylation is not only involved in many fundamental cellular processes, but also plays an important role in cancer development through various mechanisms. Recently, accumulating data reveal that O-GIcNAcylation at histones or non-histone proteins can lead to the start of the subsequent biological processes, suggesting that O-GIcNAcylation as ＇protein code＇ or ＇histone code＇ may provide recognition platforms or executive instructions for subse- quent recruitment of proteins to carry out the specific functions. In this review, we summarize the interaction of O-GIcNAcylation and epigenetic changes, introduce recent research findings that link crosstalk between O- GIcNAcylation and epigenetic changes, and speculate on the potential coordination role of O-GIcNAcylation with epigenetic changes in intracellular biological processes.
基金This work was supported by the National Natural Science Foundation of China （Grant Nos. 31071131 and 31171245）, by the National Laboratory of Biomacromolecules （O5SY02110A and 2012kf04）, and by the Project of Jilin Province Science and Technology Development Program （20130413002GH）.
文摘The BCCIP （BRCA2. and CDKNIA-interacting protein） is an important cofactor for BRCA2 in tumor suppression. Although the low expression of BCClP is observed in multiple clinically diagnosed primary tumor tissues such as ovarian cancer, renal cell carcinoma and col- orectal carcinoma, the mechanism of how BCCIP is regulated in cells is still unclear. The human INO80/YY1 chromatin remodeling complex composed of 15 sub- units catalyzes ATP-dependent sliding of nucleosomes along DNA. Here, we first report that BCClP is a novel target gene of the INO80/YY1 complex by presenting a series of experimental evidence. Gene expression studies combined with siRNA knockdown data locked candidate genes including BCCIP of the INO80/YY1 complex. Silencing or over-expressing the subunits of the INO80/YY1 complex regulates the expression level of BCCIP both in mRNA and proteins in cells. Also, the functions of INO80/YY1 complex in regulating the transactivation of BCCIP were confirmed by luciferase reporter assays. Chromatin immunoprecipitation （CHIP） experiments clarify the enrichment of INO80 and YY1 at ＋0.17 kb downstream of the BCClP transcriptional start site. However, this enrichment is significantly inhibited by either knocking down INO80 or YY1, suggesting the existence of both INO80 and YY1 is required for recruiting the INO80/YY1 complex to BCClP promoter region. Our findings strongly indicate that BCClP is a potential target gene of the INO80/YY1 complex.
文摘Current research has dem on strated that the dynamic distribution of histone variant H2A.Z at specific loci can be regulated by ATP-dependent chromatin remodelers, histone chaperones and histone post-translational modifications (PTMs).
