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( Yue Qun Wang ),( Xiang Li Ye ),( Jun Mei Zhou ),( Yong Qi Wan ),( Hua Ping Xie ),( Yun Deng ),( Yan Yan ),( Yong Qing Li ),( Xiong Wei Fan ),( Wu Zhou Yuan ),( Xiao Yang Mo ),( Xiu Shan Wu ) 생화학분자생물학회(구 한국생화학분자생물학회) 2011 BMB Reports Vol.44 No.1
Zinc finger (ZNF) proteins play a critical role in cell growth, proliferation, apoptosis, and intracellular signal transduction. In this paper, we cloned and characterized a novel human KRAB-related zinc finger gene, ZNF425, which encodes a protein of 752 amino acids. ZNF425 is strongly expressed in the three month old human embryos and then is almost undetectable in six month old embryos and in adult tissues. An EGFP-ZNF425 fusion protein can be found in both the nucleus and the cytoplasm. ZNF425 appears to act as a transcription repressor. Over-expression of ZNF425 inhibits the transcriptional activities of SRE, AP-1, and SRF. Deletion analysis indicates that the C2H2 domain is the main region responsible for the repression. Our results suggest that the ZNF425 gene is a new transcriptional inhibitor that functions in the MAPK signaling pathway. [BMB reports 2011; 44(1): 58-63]
( Yun Deng ),( Yong Qing Li ),( Xiong Wei Fan ),( Wu Zhou Yuan ),( Hua Ping Xie ),( Xiao Yang Mo ),( Yan Yan ),( Jun Mei Zhou ),( Yue Qun Wang ),( Xian Li Ye ),( Yong Qi Wan ),( Xiu Shan Wu ) 생화학분자생물학회 (구 한국생화학분자생물학회) 2010 BMB Reports Vol.43 No.6
LBH is a transcription factor as a candidate gene for CHD associated with partial trisomy 2p syndrome. To identify potential LBH-interacting partners, a yeast two-hybrid screen using LBH as a bait was performed with a human heart cDNA library. One of the clones identified encodes αB-crystallin. Co-immunoprecipitation and GST pull-down assays showed that LBH interacts with αB-crystallin, which is further confirmed by mammalian two-hybrid assays. Co-localization analysis showed that in COS-7 cells, αB-crystallin that is cytoplasmic alone, accumulates partialy in the nucleus when co-transfected with LBH. Transient transfection assays indicated that overexpression of LBH or αB-crystallin reduced the transcriptional activities of p53 and p21, respectively, Overexpression of both αB-crystallin and LBH together resulted in a stronger repression of the transcriptional activities of p21 and p53. These results showed that the interaction of LBH and αB-crystallin may inhibit synergistically the transcriptional regulation of p53 and p21. [BMB reports 2010; 43(6): 432-437]
( Na Luo ),( Guan Li ),( Yong Qing Li ),( Xiong Wei Fan ),( Yue Qun Wang ),( Xiang Li Ye ),( Xiao Yan Mo ),( Jun Mei Zhou ),( Wu Zhou Yuan ),( Ming Tan ),( Hua Ping Xie ),( Karen Ocorr ),( Rolf Bodmer 생화학분자생물학회 (구 한국생화학분자생물학회) 2010 BMB Reports Vol.43 No.5
The sterile alpha motif (SAM) is a putative protein interaction domain involved in a wide variety of biological processes. Here we report the identification and characterization of a novel gene, SAMD4B, which encodes a putative protein of 694 amino acids with a SAM domain. Northern blot and RT-PCR analysis showed that SAMD4B is widely expressed in human embryonic and adult tissues. Transcriptional activity assays show SAMD4B suppresses transcriptional activity of L8G5-luciferase. Over-expression of SAMD4B in mammalian cells inhibited the transcriptional activities of activator protein-1 (AP-1), p53 and p21, and the inhibitory effects can be relieved by siRNA. Deletion analysis indicates that the SAM domain is the main region for transcriptional suppression. The results suggest that SAMD4B is a widely expressed gene involved in AP-1-, p53-and p21-mediated transcriptional signaling activity. [BMB reports 2010; 43(5): 355-361]
N-terminal arginylation generates a bimodal degron that modulates autophagic proteolysis
Yoo, Young Dong,Mun, Su Ran,Ji, Chang Hoon,Sung, Ki Woon,Kang, Keum Young,Heo, Ah Jung,Lee, Su Hyun,An, Jee Young,Hwang, Joonsung,Xie, Xiang-Qun,Ciechanover, Aaron,Kim, Bo Yeon,Kwon, Yong Tae National Academy of Sciences 2018 PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF Vol.115 No.12
<P>The conjugation of amino acids to the protein N termini is universally observed in eukaryotes and prokaryotes, yet its functions remain poorly understood. In eukaryotes, the amino acid L-arginine (L-Arg) is conjugated to N-terminal Asp (Nt-Asp), Glu, Gln, Asn, and Cys, directly or associated with posttranslational modifications. Following Ntarginylation, the Nt-Arg is recognized by UBR boxes of N-recognins such as UBR1, UBR2, UBR4/p600, and UBR5/EDD, leading to substrate ubiquitination and proteasomal degradation via the N-end rule pathway. It has been a mystery, however, why studies for the past five decades identified only a handful of Nt-arginylated substrates in mammals, although five of 20 principal amino acids are eligible for arginylation. Here, we show that the Nt-Arg functions as a bimodal degron that directs substrates to either the ubiquitin (Ub)proteasome system (UPS) or macroautophagy depending on physiological states. In normal conditions, the arginylated forms of proteolytic cleavage products, D101-CDC6 and D1156-BRCA1, are targeted to UBR box-containing N-recognins and degraded by the proteasome. However, when proteostasis by the UPS is perturbed, their Nt-Arg redirects these otherwise cellularwastes tomacroautophagy through its binding to the ZZ domain of the autophagic adaptor p62/STQSM/Sequestosome-1. Upon binding to the Nt-Arg, p62 acts as an autophagic N-recognin that undergoes self-polymerization, facilitating cargo collection and lysosomal degradation of p62-cargo complexes. A chemical mimic of Nt-Arg redirects Ub-conjugated substrates from the UPS to macroautophagy and promotes their lysosomal degradation. Our results suggest that the Nt-Arg proteome of arginylated proteins contributes to reprogramming global proteolytic flux under stresses.</P>