• Title/Summary/Keyword: interaction protein

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Protein-Protein Interaction between Poly(A) Polymerase and Cyclophilin A in Chemotactic Cells

  • Choi, Hyun-Sook;Kim, Hana;Lee, Changgook;Kim, Youngmi;Lee, Younghoon
    • Bulletin of the Korean Chemical Society
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    • v.35 no.1
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    • pp.83-86
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    • 2014
  • Poly(A) polymerase (PAP) play an essential role for maturation of mRNA by adding the adenylate residues at the 3' end. PAP functions are regulated through protein-protein interaction at its C-terminal region. In this study, cyclophilin A (CypA), a member of the peptidyl-prolyl cis-trans isomerase family, was identified as a partner protein interacting with the C-terminal region PAP. The interaction between PAP and CypA was inhibited by the immunosuppressive drug cyclosporine A. Deletion analysis revealed that the N-terminal 56 residues of CypA are sufficient for the interaction with PAP. Interestingly, we observed that PAP and CypA colocalize in the nucleus during SDF-1-induced chemotaxis, implying that CypA could be involved in the regulation of polyadenylation by PAP in the chemotactic cells.

Interaction of a 22 kDa Peptidyl Prolyl cis/trans Isomerase with the Heat Shock Protein DnaK in Vibrio anguillarum

  • Kang, Dong Seop;Moon, Soo Young;Cho, Hwa Jin;Lee, Jong Min;Kong, In-Soo
    • Journal of Microbiology and Biotechnology
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    • v.27 no.3
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    • pp.644-647
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    • 2017
  • Peptidyl prolyl cis/trans isomerases (PPIases) catalyze the cis/trans isomerization of peptidyl-prolyl peptide bonds preceding prolines. We investigated the protein-protein interaction between a 22 kDa PPIase (VaFKBP22, an FK506-binding protein) and the molecular chaperone DnaK derived from Vibrio anguillarum O1 (VaDnaK) using GST pull-down assays and a bacterial two-hybrid system for in vivo and in vitro studies, respectively. Furthermore, we analyzed the three-dimensional structure of the protein-protein interaction. Based on our results, VaFKBP22 appears to act as a cochaperone of VaDnaK, and contributes to protein folding and stabilization via its peptidyl-prolyl cis/trans isomerization activity.

Interaction of the Bacteriophage P2 Tin Protein and Bacteriophage T4 gp32 Protein Inhibites Growth of Bacteriophage T4

  • Jin, Hee-Kyung;Kim, Min-Jung;Park, Chan-Hee;Park, Jung-Chan;Myung, Hee-Joon
    • Journal of Microbiology and Biotechnology
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    • v.11 no.4
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    • pp.724-726
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    • 2001
  • The growth of baceriophage T4 is inhibited by the presence of the tin gene product o bacteriophage P2. The interaction between purified Tin and gp32 proteins was observed using coimmunoprecipitation experiments. The in vivo interaction was confirmed by yeast two-hybrid experiments. A deletion analysis showed that the Asp 163 region of gp32 to DNA substrates was not affected by the presence of Tin, Thus, it would appear that the inhibition of 4 growth by Tin was due to a protein-protein interaction rather than affecting the DNA-binding ability of gp32.

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A New Approach to Find Orthologous Proteins Using Sequence and Protein-Protein Interaction Similarity

  • Kim, Min-Kyung;Seol, Young-Joo;Park, Hyun-Seok;Jang, Seung-Hwan;Shin, Hang-Cheol;Cho, Kwang-Hwi
    • Genomics & Informatics
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    • v.7 no.3
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    • pp.141-147
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    • 2009
  • Developed proteome-scale ortholog and paralog prediction methods are mainly based on sequence similarity. However, it is known that even the closest BLAST hit often does not mean the closest neighbor. For this reason, we added conserved interaction information to find orthologs. We propose a genome-scale, automated ortholog prediction method, named OrthoInterBlast. The method is based on both sequence and interaction similarity. When we applied this method to fly and yeast, 17% of the ortholog candidates were different compared with the results of Inparanoid. By adding protein-protein interaction information, proteins that have low sequence similarity still can be selected as orthologs, which can not be easily detected by sequence homology alone.

Protein-Protein Interaction Prediction using Interaction Significance Matrix (상호작용 중요도 행렬을 이용한 단백질-단백질 상호작용 예측)

  • Jang, Woo-Hyuk;Jung, Suk-Hoon;Jung, Hwie-Sung;Hyun, Bo-Ra;Han, Dong-Soo
    • Journal of KIISE:Software and Applications
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    • v.36 no.10
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    • pp.851-860
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    • 2009
  • Recently, among the computational methods of protein-protein interaction prediction, vast amounts of domain based methods originated from domain-domain relation consideration have been developed. However, it is true that multi domains collaboration is avowedly ignored because of computational complexity. In this paper, we implemented a protein interaction prediction system based the Interaction Significance matrix, which quantified an influence of domain combination pair on a protein interaction. Unlike conventional domain combination methods, IS matrix contains weighted domain combinations and domain combination pair power, which mean possibilities of domain collaboration and being the main body on a protein interaction. About 63% of sensitivity and 94% of specificity were measured when we use interaction data from DIP, IntAct and Pfam-A as a domain database. In addition, prediction accuracy gradually increased by growth of learning set size, The prediction software and learning data are currently available on the web site.

Web-Based Computational System for Protein-Protein Interaction Inference

  • Kim, Ki-Bong
    • Journal of Information Processing Systems
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    • v.8 no.3
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    • pp.459-470
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    • 2012
  • Recently, high-throughput technologies such as the two-hybrid system, protein chip, Mass Spectrometry, and the phage display have furnished a lot of data on protein-protein interactions (PPIs), but the data has not been accurate so far and the quantity has also been limited. In this respect, computational techniques for the prediction and validation of PPIs have been developed. However, existing computational methods do not take into account the fact that a PPI is actually originated from the interactions of domains that each protein contains. So, in this work, the information on domain modules of individual proteins has been employed in order to find out the protein interaction relationship. The system developed here, WASPI (Web-based Assistant System for Protein-protein interaction Inference), has been implemented to provide many functional insights into the protein interactions and their domains. To achieve those objectives, several preprocessing steps have been taken. First, the domain module information of interacting proteins was extracted by taking advantage of the InterPro database, which includes protein families, domains, and functional sites. The InterProScan program was used in this preprocess. Second, the homology comparison with the GO (Gene Ontology) and COG (Clusters of Orthologous Groups) with an E-value of $10^{-5}$, $10^{-3}$ respectively, was employed to obtain the information on the function and annotation of each interacting protein of a secondary PPI database in the WASPI. The BLAST program was utilized for the homology comparison.

Protein-Protein Interaction Reliability Enhancement System based on Feature Selection and Classification Technique (특징 추출과 분석 기법에 기반한 단백질 상호작용 데이터 신뢰도 향상 시스템)

  • Lee, Min-Su;Park, Seung-Soo;Lee, Sang-Ho;Yong, Hwan-Seung;Kang, Sung-Hee
    • The KIPS Transactions:PartB
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    • v.13B no.7 s.110
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    • pp.679-688
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    • 2006
  • Protein-protein interaction data obtained from high-throughput experiments includes high false positives. In this paper, we introduce a new protein-protein interaction reliability verification system. The proposed system integrates various biological features related with protein-protein interactions, and then selects the most relevant and informative features among them using a feature selection method. To assess the reliability of each protein-protein interaction data, the system construct a classifier that can distinguish true interacting protein pairs from noisy protein-protein interaction data based on the selected biological evidences using a classification technique. Since the performance of feature selection methods and classification techniques depends heavily upon characteristics of data, we performed rigorous comparative analysis of various feature selection methods and classification techniques to obtain optimal performance of our system. Experimental results show that the combination of feature selection method and classification algorithms provide very powerful tools in distinguishing true interacting protein pairs from noisy protein-protein interaction dataset. Also, we investigated the effects on performances of feature selection methods and classification techniques in the proposed protein interaction verification system.

Protein Interaction Possibility Ranking Method based on Domain Combination (도메인 조합 기반 단백질 상호작용 가능성 순위 부여 기법)

  • Han Dong-Soo;Kim Hong-Song;Jong Woo-Hyuk;Lee Sung-Doke
    • Journal of KIISE:Computing Practices and Letters
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    • v.11 no.5
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    • pp.427-435
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    • 2005
  • With the accumulation of protein and its related data on the Internet, many domain based computational techniques to predict protein interactions have been developed. However, most of the techniques still have many limitations to be used in real fields. They usually suffer from a low accuracy problem in prediction and do not provide any interaction possibility ranking method for multiple protein pairs. In this paper, we reevaluate a domain combination based protein interaction prediction method and develop an interaction possibility ranking method for multiple protein pairs. Probability equations are devised and proposed in the framework of domain combination based protein interaction prediction method. Using the ranking method, one can discern which protein pair is more probable to interact with each other than other protein pairs in multiple protein pairs. In the validation of the ranking method, we revealed that there exist some correlations between the interacting probability and the precision of the prediction in case of the protein pair group having the matching PIP(Primary Interaction Probability) values in the interacting or non interacting PIP distributions.

Computational approaches for prediction of protein-protein interaction between Foot-and-mouth disease virus and Sus scrofa based on RNA-Seq

  • Park, Tamina;Kang, Myung-gyun;Nah, Jinju;Ryoo, Soyoon;Wee, Sunghwan;Baek, Seung-hwa;Ku, Bokkyung;Oh, Yeonsu;Cho, Ho-seong;Park, Daeui
    • Korean Journal of Veterinary Service
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    • v.42 no.2
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    • pp.73-83
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    • 2019
  • Foot-and-Mouth Disease (FMD) is a highly contagious trans-boundary viral disease caused by FMD virus, which causes huge economic losses. FMDV infects cloven hoofed (two-toed) mammals such as cattle, sheep, goats, pigs and various wildlife species. To control the FMDV, it is necessary to understand the life cycle and the pathogenesis of FMDV in host. Especially, the protein-protein interaction between FMDV and host will help to understand the survival cycle of viruses in host cell and establish new therapeutic strategies. However, the computational approach for protein-protein interaction between FMDV and pig hosts have not been applied to studies of the onset mechanism of FMDV. In the present work, we have performed the prediction of the pig's proteins which interact with FMDV based on RNA-Seq data, protein sequence, and structure information. After identifying the virus-host interaction, we looked for meaningful pathways and anticipated changes in the host caused by infection with FMDV. A total of 78 proteins of pig were predicted as interacting with FMDV. The 156 interactions include 94 interactions predicted by sequence-based method and the 62 interactions predicted by structure-based method using domain information. The protein interaction network contained integrin as well as STYK1, VTCN1, IDO1, CDH3, SLA-DQB1, FER, and FGFR2 which were related to the up-regulation of inflammation and the down-regulation of cell adhesion and host defense systems such as macrophage and leukocytes. These results provide clues to the knowledge and mechanism of how FMDV affects the host cell.

Construction of a Protein-Protein Interaction Network for Chronic Myelocytic Leukemia and Pathway Prediction of Molecular Complexes

  • Zhou, Chao;Teng, Wen-Jing;Yang, Jing;Hu, Zhen-Bo;Wang, Cong-Cong;Qin, Bao-Ning;Lv, Qing-Liang;Liu, Ze-Wang;Sun, Chang-Gang
    • Asian Pacific Journal of Cancer Prevention
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    • v.15 no.13
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    • pp.5325-5330
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    • 2014
  • Background: Chronic myelocytic leukemia is a disease that threatens both adults and children. Great progress has been achieved in treatment but protein-protein interaction networks underlining chronic myelocytic leukemia are less known. Objective: To develop a protein-protein interaction network for chronic myelocytic leukemia based on gene expression and to predict biological pathways underlying molecular complexes in the network. Materials and Methods: Genes involved in chronic myelocytic leukemia were selected from OMIM database. Literature mining was performed by Agilent Literature Search plugin and a protein-protein interaction network of chronic myelocytic leukemia was established by Cytoscape. The molecular complexes in the network were detected by Clusterviz plugin and pathway enrichment of molecular complexes were performed by DAVID online. Results and Discussion: There are seventy-nine chronic myelocytic leukemia genes in the Mendelian Inheritance In Man Database. The protein-protein interaction network of chronic myelocytic leukemia contained 638 nodes, 1830 edges and perhaps 5 molecular complexes. Among them, complex 1 is involved in pathways that are related to cytokine secretion, cytokine-receptor binding, cytokine receptor signaling, while complex 3 is related to biological behavior of tumors which can provide the bioinformatic foundation for further understanding the mechanisms of chronic myelocytic leukemia.