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Prediction of localization and interactions of apoptotic proteins
During apoptosis several mitochondrial proteins are released. Some of them participate in caspase-independent nuclear DNA degradation, especially apoptosis-inducing factor (AIF) and endonuclease G (endoG). Another interesting protein, which was expected to act similarly as AIF due to the high sequen...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
Publicado: |
BioMed Central
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2714591/ https://www.ncbi.nlm.nih.gov/pubmed/19580669 http://dx.doi.org/10.1186/1423-0127-16-59 |
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author | Vařecha, Miroslav Zimmermann, Michal Amrichová, Jana Ulman, Vladimír Matula, Pavel Kozubek, Michal |
author_facet | Vařecha, Miroslav Zimmermann, Michal Amrichová, Jana Ulman, Vladimír Matula, Pavel Kozubek, Michal |
author_sort | Vařecha, Miroslav |
collection | PubMed |
description | During apoptosis several mitochondrial proteins are released. Some of them participate in caspase-independent nuclear DNA degradation, especially apoptosis-inducing factor (AIF) and endonuclease G (endoG). Another interesting protein, which was expected to act similarly as AIF due to the high sequence homology with AIF is AIF-homologous mitochondrion-associated inducer of death (AMID). We studied the structure, cellular localization, and interactions of several proteins in silico and also in cells using fluorescent microscopy. We found the AMID protein to be cytoplasmic, most probably incorporated into the cytoplasmic side of the lipid membranes. Bioinformatic predictions were conducted to analyze the interactions of the studied proteins with each other and with other possible partners. We conducted molecular modeling of proteins with unknown 3D structures. These models were then refined by MolProbity server and employed in molecular docking simulations of interactions. Our results show data acquired using a combination of modern in silico methods and image analysis to understand the localization, interactions and functions of proteins AMID, AIF, endonuclease G, and other apoptosis-related proteins. |
format | Text |
id | pubmed-2714591 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-27145912009-07-24 Prediction of localization and interactions of apoptotic proteins Vařecha, Miroslav Zimmermann, Michal Amrichová, Jana Ulman, Vladimír Matula, Pavel Kozubek, Michal J Biomed Sci Research During apoptosis several mitochondrial proteins are released. Some of them participate in caspase-independent nuclear DNA degradation, especially apoptosis-inducing factor (AIF) and endonuclease G (endoG). Another interesting protein, which was expected to act similarly as AIF due to the high sequence homology with AIF is AIF-homologous mitochondrion-associated inducer of death (AMID). We studied the structure, cellular localization, and interactions of several proteins in silico and also in cells using fluorescent microscopy. We found the AMID protein to be cytoplasmic, most probably incorporated into the cytoplasmic side of the lipid membranes. Bioinformatic predictions were conducted to analyze the interactions of the studied proteins with each other and with other possible partners. We conducted molecular modeling of proteins with unknown 3D structures. These models were then refined by MolProbity server and employed in molecular docking simulations of interactions. Our results show data acquired using a combination of modern in silico methods and image analysis to understand the localization, interactions and functions of proteins AMID, AIF, endonuclease G, and other apoptosis-related proteins. BioMed Central 2009-07-06 /pmc/articles/PMC2714591/ /pubmed/19580669 http://dx.doi.org/10.1186/1423-0127-16-59 Text en Copyright © 2009 Vařecha et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Vařecha, Miroslav Zimmermann, Michal Amrichová, Jana Ulman, Vladimír Matula, Pavel Kozubek, Michal Prediction of localization and interactions of apoptotic proteins |
title | Prediction of localization and interactions of apoptotic proteins |
title_full | Prediction of localization and interactions of apoptotic proteins |
title_fullStr | Prediction of localization and interactions of apoptotic proteins |
title_full_unstemmed | Prediction of localization and interactions of apoptotic proteins |
title_short | Prediction of localization and interactions of apoptotic proteins |
title_sort | prediction of localization and interactions of apoptotic proteins |
topic | Research |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2714591/ https://www.ncbi.nlm.nih.gov/pubmed/19580669 http://dx.doi.org/10.1186/1423-0127-16-59 |
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