• Title/Summary/Keyword: structural proteomics

Search Result 37, Processing Time 0.019 seconds

Structural insights into the transcription-independent apoptotic pathway of p53

  • Chi, Seung-Wook
    • BMB Reports
    • /
    • v.47 no.3
    • /
    • pp.167-172
    • /
    • 2014
  • Reactivating the p53 pathway in tumors is an important strategy for anticancer therapy. In response to diverse cellular stresses, the tumor suppressor p53 mediates apoptosis in a transcription-independent and transcription-dependent manner. Although extensive studies have focused on the transcription-dependent apoptotic pathway of p53, the transcription-independent apoptotic pathway of p53 has only recently been discovered. Molecular interactions between p53 and Bcl-2 family proteins in the mitochondria play an essential role in the transcription-independent apoptosis of p53. This review describes the structural basis for the transcription-independent apoptotic pathway of p53 and discusses its potential application to anticancer therapy.

Advances in Ion Mobility Spectrometry-Mass Spectrometry (IMS-MS)-Based Techniques for Elucidating Higher-Order Protein Structures

  • Seo, Jongcheol
    • Mass Spectrometry Letters
    • /
    • v.11 no.4
    • /
    • pp.65-70
    • /
    • 2020
  • Despite its great success in the field of proteomics, mass spectrometry has limited use for determining structural details of peptides, proteins, and their assemblies. Emerging ion mobility spectrometry-mass spectrometry has enabled us to explore the conformational space of protein ions in the gas phase, and further combinations with the gas-phase ion spectroscopy and the collision-induced unfolding have extended its abilities to elucidating the secondary structure and local details of conformational transitions. This review will provide a brief introduction to the combined approaches of IMS-MS with gas-phase ion infrared spectroscopy or collision-induced unfolding and their most recent results that successfully revealed higher-order structural details.

Computational Chemistry as a Key to Structural Bioinformatics

  • Kang, Young-Kee
    • Proceedings of the Korean Society for Bioinformatics Conference
    • /
    • 2000.11a
    • /
    • pp.32-34
    • /
    • 2000
  • Computational chemistry is a discipline using computational methods for the calculation of molecular structure, properties, and reaction or for the simulation of molecular behavior. Relating and turning the complexity of data from genomics, high-throughput screening, combinatorial chemical synthesis, gene-expression investigations, pharmacogenomics, and proteomics into useful information and knowledge is the primary goal of bioinformatics. In particular, the structure-based molecular design is one of essential fields in bioinformatics and it can be called as structural bioinformatics. Therefore, the conformational analysis for proteins and peptides using the techniques of computational chemistry is expected to play a role in structural bioinformatics. There are two major computational methods for conformational analysis of proteins and peptides; one is the molecular orbital (MO) method and the other is the force field (or empirical potential function) method. The MO method can be classified into ab initio and semiempirical methods, which have been applied to relatively small and large molecules, respectively. However, the improvement in computer hardwares and softwares enables us to use the ab initio MO method for relatively larger biomolecules with up to v100 atoms or ∼800 basis functions. In order to show how computational chemistry can be used in structural bioinformatics, 1 will present on (1) cis-trans isomerization of proline dipeptide and its derivatives, (2) positional preference of proline in ${\alpha}$-helices, and (3) conformations and activities of Arg-Gly-Asp-containing tetrapeptides.

  • PDF

A Novel Approach to Investigating Protein/Protein Interactions and Their Functions by TAP-Tagged Yeast Strains and its Application to Examine Yeast Transcription Machinery

  • Jung, Jun-Ho;Ahn, Yeh-Jin;Kang, Lin-Woo
    • Journal of Microbiology and Biotechnology
    • /
    • v.18 no.4
    • /
    • pp.631-638
    • /
    • 2008
  • Tandem affinity purification (TAP) method combined with LC-MS/MS is the most accurate and reliable way to study the interaction of proteins or proteomics in a genome-wide scale. For the first time, we used a TAP-tag as a mutagenic tool to disrupt protein interactions at the specific site. Although lots of commonly used mutational tools exist to study functions of a gene, such as deletional mutations and site-directed mutagenesis, each method has its own demerit. To test the usefulness of a TAP-tag as a mutagenic tool, we applied a TAP-tag to RNA polymerase II, which is the key enzyme of gene expression and is controlled by hundreds of transcription factors even to transcribe a gene. Our experiment is based on the hypothesis that there will be interrupted interactions between Pol II and transcription factors owing to the TAP-tag attached at the C-terminus of each subunit of Pol II, and the abnormality caused by interrupted protein interactions can be observed by measuring a cell-cycle of each yeast strain. From ten different TAP-tagged strains, Rpb7- and Rpb12-TAP-tagged strains show severe defects in growth rate and morphology. Without a heterodimer of Rpb4/Rpb7, only the ten subunits Pol II can conduct transcription normally, and there is no previously known function of Rpb7. The observed defect of the Rpb7-TAP-tagged strain shows that Rpb7 forms a complex with other proteins or compounds and the interruption of the interaction can interfere with the normal cell cycle and morphology of the cell and nucleus. This is a novel attempt to use a TAP-tag as a proteomic tool to study protein interactions.

Label-free quantitative proteomic analysis of Panax ginseng leaves upon exposure to heat stress

  • Kim, So Wun;Gupta, Ravi;Min, Cheol Woo;Lee, Seo Hyun;Cheon, Ye Eun;Meng, Qing Feng;Jang, Jeong Woo;Hong, Chi Eun;Lee, Ji Yoon;Jo, Ick Hyun;Kim, Sun Tae
    • Journal of Ginseng Research
    • /
    • v.43 no.1
    • /
    • pp.143-153
    • /
    • 2019
  • Background: Ginseng is one of the well-known medicinal plants, exhibiting diverse medicinal effects. Its roots possess anticancer and antiaging properties and are being used in the medical systems of East Asian countries. It is grown in low-light and low-temperature conditions, and its growth is strongly inhibited at temperatures above $25^{\circ}C$. However, the molecular responses of ginseng to heat stress are currently poorly understood, especially at the protein level. Methods: We used a shotgun proteomics approach to investigate the effect of heat stress on ginseng leaves. We monitored their photosynthetic efficiency to confirm physiological responses to a high-temperature stress. Results: The results showed a reduction in photosynthetic efficiency on heat treatment ($35^{\circ}C$) starting at 48 h. Label-free quantitative proteome analysis led to the identification of 3,332 proteins, of which 847 were differentially modulated in response to heat stress. The MapMan analysis showed that the proteins with increased abundance were mainly associated with antioxidant and translation-regulating activities, whereas the proteins related to the receptor and structural-binding activities exhibited decreased abundance. Several other proteins including chaperones, G-proteins, calcium-signaling proteins, transcription factors, and transfer/carrier proteins were specifically downregulated. Conclusion: These results increase our understanding of heat stress responses in the leaves of ginseng at the protein level, for the first time providing a resource for the scientific community.

Protein Ontology: Semantic Data Integration in Proteomics

  • Sidhu, Amandeep S.;Dillon, Tharam S.;Chang, Elizabeth;Sidhu, Baldev S.
    • Proceedings of the Korean Society for Bioinformatics Conference
    • /
    • 2005.09a
    • /
    • pp.388-391
    • /
    • 2005
  • The Protein Structural and Functional Conservation need a common language for data definition. With the help of common language provided by Protein Ontology the high level of sequence and functional conservation can be extended to all organisms with the likelihood that proteins that carry out core biological processes will again be probable orthologues. The structural and functional conservation in these proteins presents both opportunities and challenges. The main opportunity lies in the possibility of automated transfer of protein data annotations from experimentally traceable model organisms to a less traceable organism based on protein sequence similarity. Such information can be used to improve human health or agriculture. The challenge lies in using a common language to transfer protein data annotations among different species of organisms. First step in achieving this huge challenge is producing a structured, precisely defined common vocabulary using Protein Ontology. The Protein Ontology described in this paper covers the sequence, structure and biological roles of Protein Complexes in any organism.

  • PDF

Impact of glycosylation on the unimpaired functions of the sperm

  • Cheon, Yong-Pil;Kim, Chung-Hoon
    • Clinical and Experimental Reproductive Medicine
    • /
    • v.42 no.3
    • /
    • pp.77-85
    • /
    • 2015
  • One of the key factors of early development is the specification of competence between the oocyte and the sperm, which occurs during gametogenesis. However, the starting point, growth, and maturation for acquiring competence during spermatogenesis and oogenesis in mammals are very different. Spermatogenesis includes spermiogenesis, but such a metamorphosis is not observed during oogenesis. Glycosylation, a ubiquitous modification, is a preliminary requisite for distribution of the structural and functional components of spermatids for metamorphosis. In addition, glycosylation using epididymal or female genital secretory glycans is an important process for the sperm maturation, the acquisition of the potential for fertilization, and the acceleration of early embryo development. However, nonemzymatic unexpected covalent bonding of a carbohydrate and malglycosylation can result in falling fertility rates as shown in the diabetic male. So far, glycosylation during spermatogenesis and the dynamics of the plasma membrane in the process of capacitation and fertilization have been evaluated, and a powerful role of glycosylation in spermatogenesis and early development is also suggested by structural bioinformatics, functional genomics, and functional proteomics. Further understanding of glycosylation is needed to provide a better understanding of fertilization and embryo development and for the development of new diagnostic and therapeutic tools for infertility.

Identification of SUMOylated proteins in neuroblastoma cells after treatment with hydrogen peroxide or ascorbate

  • Grant, Melissa M.
    • BMB Reports
    • /
    • v.43 no.11
    • /
    • pp.720-725
    • /
    • 2010
  • The small ubiquitin-like modifier (SUMO) proteins have been implicated in the pathology of a number of diseases, including neurodegenerative diseases. The conjugation machinery for SUMOylation consists of a number of proteins which are redox sensitive. Here, under oxidative stress ($100{\mu}M$ hydrogen peroxide), antioxidant ($100{\mu}M$ ascorbate) or control conditions 169 proteins were identified by electospray ionisation fourier transform ion cyclotron resonance mass spectrometry. The majority of these proteins (70%) were found to contain SUMOylation consensus sequences. From the remaining proteins a small number (12%) were found to contain possible SUMO interacting motifs. The proteins identified included DNA and RNA binding proteins, structural proteins and proteasomal proteins. Several of the proteins identified under oxidative stress conditions had previously been identified as SUMOylated proteins, thus validating the method presented.

Differentiation of Glycan Diversity with Serial Affinity Column Set (SACS)

  • Shin, Jihoon;Cho, Wonryeon
    • Mass Spectrometry Letters
    • /
    • v.7 no.3
    • /
    • pp.74-78
    • /
    • 2016
  • Targeted glycoproteomics is an effective way to discover disease-associated glycoproteins in proteomics and serial affinity chromatography (SAC) using lectin and glycan-targeting antibodies shows glycan diversity on the captured glycoproteins. This study suggests a way to determine glycan heterogeneity and structural analysis on the post-translationally modified proteins through serial affinity column set (SACS) using four Lycopersicon esculentum lectin (LEL) columns. The great advantage of this method is that it differentiates between glycoproteins on the basis of their binding affinity. Through this study, some proteins were identified to have glycoforms with different affinity on a single glycoprotein. It will be particularly useful in determining biomarkers in which the disease-specific feature is a unique glycan, or a group of glycans.