Search

Your search keyword '"Zhai, Guijin"' showing total 39 results
Start Over Author "Zhai, Guijin"
39 results on '"Zhai, Guijin"'

16. Systematic Proteome and Lysine Succinylome Analysis Reveals Enhanced Cell Migration by Hyposuccinylation in Esophageal Squamous Cell Carcinoma

Author

Guo, Zhenchang, primary, Pan, Feng, additional, Peng, Liu, additional, Tian, Shanshan, additional, Jiao, Jiwei, additional, Liao, Liandi, additional, Lu, Congcong, additional, Zhai, Guijin, additional, Wu, Zhiyong, additional, Dong, Hanyang, additional, Xu, Xiue, additional, Wu, Jianyi, additional, Chen, Pu, additional, Bai, Xue, additional, Lin, Dechen, additional, Xu, Liyan, additional, Li, Enmin, additional, and Zhang, Kai, additional

Published
2021
Full Text
View/download PDF

21. An Efficient Approach for Selective Enrichment of Histone Modification Readers Using Self-Assembled Multivalent Photoaffinity Peptide Probes

Author

Zhai, Guijin, primary, Dong, Hanyang, additional, Guo, Zhenchang, additional, Feng, Wei, additional, Jin, Jin, additional, Zhang, Tao, additional, Chen, Cong, additional, Chen, Pu, additional, Tian, Shanshan, additional, Bai, Xue, additional, Shi, Lei, additional, Fan, Enguo, additional, Zhang, Yukui, additional, and Zhang, Kai, additional

Published
2018
Full Text
View/download PDF

22. Systematic Identification of Lysine 2-hydroxyisobutyrylated Proteins in Proteus mirabilis

Author

Dong, Hanyang, primary, Guo, Zhenchang, additional, Feng, Wei, additional, Zhang, Tao, additional, Zhai, Guijin, additional, Palusiak, Agata, additional, Rozalski, Antoni, additional, Tian, Shanshan, additional, Bai, Xue, additional, Shen, Lijin, additional, Chen, Pu, additional, Wang, Quan, additional, Fan, Enguo, additional, Cheng, Zhongyi, additional, and Zhang, Kai, additional

Published
2018
Full Text
View/download PDF

28. An Integrated Approach Based on a DNA Self-Assembly Technique for Characterization of Crosstalk among Combinatorial Histone Modifications

Author

Bai, Xue, Bi, Wenjing, Dong, Hanyang, Chen, Pu, Tian, Shanshan, Zhai, Guijin, and Zhang, Kai

Abstract

Combinatorial histone post-translational modifications (HPTMs) form a complex epigenetic code that can be decoded by specific binding proteins, termed as readers. Their specific interplays have been thought to determine gene expression and downstream biological functions. However, it is still a big challenge to analyze such interactions due to various limitations including rather weak, transient, and complicated interactions between HPTMs and readers, the high dynamic property of HPTMs, and the low abundance of reader proteins. Here we sought to take advantage of DNA-templated and photo-cross-linking techniques to design a group of combinatorial histone PTM peptide probes for the identification of multivalent interactions among histone PTMs and readers. By use of trimethylation on histone H3K4 (H3K4me3) and phosphorylation on H3T3, we demonstrated that this approach can be successfully utilized for identification of the PTM crosstalk on the same histone. By use of H3K4me3 and acetylation on H4K16, we showed the potential application of the probe in the multivalent interactions among PTMs on different histones. Thus, this new chemical proteomics tool combined with mass spectrometry holds a promising potential in profiling of the readers of combinatorial HPTMs and characterization of crosstalk among multiple PTMs on histones and can be adapted for broad biomedical applications.

Published
2024
Full Text
View/download PDF

34. Analysis of lysine 2-hydroxyisobutyrylation proteins in Proteus mirabilis

Author

Zhang Kai, Dong Hanyang, Tian Shanshan, Zhai Guijin, and Guo Zhenchang

Subjects
Chromatography, biology, Chemistry, General Chemical Engineering, Organic Chemistry, Lysine, Electrochemistry, biology.organism_classification, Biochemistry, Proteus mirabilis, Analytical Chemistry
Abstract

蛋白质的赖氨酸修饰广泛参与基因调控、转录、代谢等重要的生物过程。在真核细胞组蛋白上发现了一种新的赖氨酸修饰——2-羟基异丁酰化，这种修饰对于生殖细胞分化具有调控功能。该研究旨在探索这种修饰在原核生物非组蛋白中的特征。通过亲和富集、高效液相色谱-串联质谱鉴定和生物信息学分析，在奇异变形杆菌中鉴定到大量未见报道的2-羟基异丁酰化蛋白及其位点，进而考察了原核生物中2-羟基异丁酰化修饰蛋白的分布特征、分子网络和通路特点。研究表明，赖氨酸-2-羟基异丁酰化在原核生物中具有广泛的分布，其生物学意义值得进一步研究。

Published
2016

35. Quantitative Mass Spectrometry Combined with Separation and Enrichment of Phosphopeptides by Titania Coated Magnetic Mesoporous Silica Microspheres for Screening of Protein Kinase Inhibitors

Author

Ji, Liyun, primary, Wu, Jian-Hong, additional, Luo, Qun, additional, Li, Xianchan, additional, Zheng, Wei, additional, Zhai, Guijin, additional, Wang, Fuyi, additional, Lü, Shuang, additional, Feng, Yu-Qi, additional, Liu, Jianan, additional, and Xiong, Shaoxiang, additional

Published
2012
Full Text
View/download PDF

36. Probing the Binding Interfaces of Histone-Aptamer by Photo Cross-Linking Mass Spectrometry

Author

Lu, Congcong, Tian, Shanshan, Zhai, Guijin, Yuan, Zuofei, Li, Yijun, He, Xiwen, Zhang, Yukui, and Zhang, Kai

Abstract

Histone proteins, which could interact with DNA, play important roles in the regulation of chromatin structures, transcription, and other DNA-based biological processes. Here, we developed a novel aptamer-based probe for the analysis of histone H4-aptamer interfaces. This probe contains a DNA sequence for specific recognition of histone H4, a biotin tag for affinity enrichment, an aryl azide photoactive group for cross-linking and a cleavable disulfide group to dissociate aptamer from labeled histones. We successfully achieved specific enrichment of histone H4 and further developed a new analysis strategy for histone-aptamer interaction by photo cross-linking mass spectrometry. The binding area of histone H4 to aptamer was investigated and discussed for the first time. This strategy exhibits great potential and might further contribute to the understanding of histone–DNA interaction patterns.

Published
2017
Full Text
View/download PDF

37. Systematic Proteome and Lysine Succinylome Analysis Reveals the Enhanced Cell Migration by Hyposuccinylation in Esophageal Squamous Cell Cancer

Author

Guo, Zhenchang, Pan, Feng, Peng, Liu, Tian, Shanshan, Jiao, Jiwei, Liao, Liandi, Lu, Congcong, Zhai, Guijin, Wu, Zhiyong, Dong, Hanyang, Xu, Xiue, Wu, Jianyi, Chen, Pu, Bai, Xue, Lin, Dechen, Xu, Liyan, Li, Enmin, and Zhang, Kai

Abstract

Esophageal squamous cell cancer (ESCC) is an aggressive malignancy with poor therapeutic outcomes. However, the alterations in proteins and post-translational modifications (PTMs) leading to the pathogenesis of ESCC remains unclear. Here, we provide the comprehensive characterization of the proteome, phosphorylome, lysine acetylome and succinylome for ESCC and matched control cells using quantitative proteomic approach. We identify abnormal protein and post-translational modification (PTM) pathways, including significantly downregulated lysine succinylation sites in cancer cells. Focusing on hyposuccinylation, we reveal that this altered PTM was enriched on enzymes of metabolic pathways inextricably linked with cancer metabolism. Importantly, ESCC malignant behaviors such as cell migration are inhibited once the level of succinylation was restored in vitroor in vivo. This effect was further verified by mutations to disrupt succinylation sites in candidate proteins. Meanwhile, we found that succinylation has a negative regulatory effect on histone methylation to promote cancer migration. Finally, hyposuccinylation is confirmed in primary ESCC specimens. Our findings together demonstrate that lysine succinylation may alter ESCC metabolism and migration, providing new insights into the functional significance of PTM in cancer biology.

Published
2021
Full Text
View/download PDF

38. Identification of dual histone modification-binding protein interaction by combining mass spectrometry and isothermal titration calorimetric analysis.

Author

Chen P, Guo Z, Chen C, Tian S, Bai X, Zhai G, Ma Z, Wu H, and Zhang K

Abstract

Histone posttranslational modifications (HPTMs) play important roles in eukaryotic transcriptional regulation. Recently, it has been suggested that combinatorial modification codes that comprise two or more HPTMs can recruit readers of HPTMs, performing complex regulation of gene expression. However, the characterization of the multiplex interactions remains challenging, especially for the molecular network of histone PTMs, readers and binding complexes. Here, we developed an integrated method that combines a peptide library, affinity enrichment, mass spectrometry (MS) and bioinformatics analysis for the identification of the interaction between HPTMs and their binding proteins. Five tandem-domain-reader proteins (BPTF, CBP, TAF1, TRIM24 and TRIM33) were designed and prepared as the enriched probes, and a group of histone peptides with multiple PTMs were synthesized as the target peptide library. First, the domain probes were used to pull down the PTM peptides from the library, and then the resulting product was characterized by MS. The binding interactions between PTM peptides and domains were further validated and measured by isothermal titration calorimetry analysis (ITC). Meanwhile, the binding proteins were enriched by domain probes and identified by HPLC-MS/MS. The interaction network of histone PTMs-readers-binding complexes was finally analyzed via informatics tools. Our results showed that the integrated approach combining MS analysis with ITC assay enables us to understand the interaction between the combinatorial HPTMs and reading domains. The identified network of "HPTMs-reader proteins-binding complexes" provided potential clues to reveal HPTM functions and their regulatory mechanisms., Competing Interests: The authors declare no conflicts of interest., (© 2020 Production and hosting by Elsevier B.V. on behalf of Cairo University.)

Published
2019
Full Text
View/download PDF

39. Development of a DNA-Templated Peptide Probe for Photoaffinity Labeling and Enrichment of the Histone Modification Reader Proteins.

Author

Bai X, Lu C, Jin J, Tian S, Guo Z, Chen P, Zhai G, Zheng S, He X, Fan E, Zhang Y, and Zhang K

Subjects
HeLa Cells, Humans, Lysine analysis, Methylation, Photochemical Processes, Protein Processing, Post-Translational, Proteomics methods, DNA chemistry, Histone Code, Histones chemistry, Peptides chemistry, Photoaffinity Labels chemistry
Abstract

Histone post-translational modifications (HPTMs) provide signal platforms to recruit proteins or protein complexes to regulate gene expression. Therefore, the identification of these recruited partners (readers) is essential to understand the underlying regulatory mechanisms. However, it is still a major challenge to profile these partners because their interactions with HPTMs are rather weak and highly dynamic. Herein we report the development of a HPTM dual probe based on DNA-templated technology and a photo-crosslinking method for the identification of HPTM readers. By using the trimethylation of histone H3 lysine 4, we demonstrated that this HPTM dual probe can be successfully utilized for labeling and enrichment of HPTM readers, as well as for the discovery of potential HPTM partners. This study describes the development of a new chemical proteomics tool for profiling HPTM readers and can be adapted for broad biomedical applications., (© 2016 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)

Published
2016
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results