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Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica
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| Zeitschriftentitel: | Microbiology |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Microbiology, 151, 2005, 9, S. 3107-3115 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Microbiology Society
|
| Schlagwörter: |
| author_facet |
van der Giezen, Mark León-Avila, Gloria Tovar, Jorge van der Giezen, Mark León-Avila, Gloria Tovar, Jorge |
|---|---|
| author |
van der Giezen, Mark León-Avila, Gloria Tovar, Jorge |
| spellingShingle |
van der Giezen, Mark León-Avila, Gloria Tovar, Jorge Microbiology Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica Microbiology |
| author_sort |
van der giezen, mark |
| spelling |
van der Giezen, Mark León-Avila, Gloria Tovar, Jorge 1350-0872 1465-2080 Microbiology Society Microbiology http://dx.doi.org/10.1099/mic.0.28068-0 <jats:p><jats:italic>Entamoeba histolytica</jats:italic>is the causative agent of amoebiasis, a poverty-related disease that kills an estimated 100 000 people each year.<jats:italic>E. histolytica</jats:italic>does not contain ‘standard mitochondria’, but harbours mitochondrial remnant organelles called mitosomes. These organelles are characterized by the presence of mitochondrial chaperonin Cpn60, but little else is known about the functions and molecular composition of mitosomes. In this study, a gene encoding molecular chaperonin Cpn10 – the functional partner of Cpn60 – was cloned, and its structure and expression were characterized, as well as the cellular localization of its encoded protein. The 5′ untranslated region of the gene contains all of the structural promoter elements required for transcription in this organism. The amoebic Cpn10, like Cpn60, is not significantly upregulated upon heat-shock treatment. Computer-assisted protein modelling, and specific antibodies against Cpn10 and Cpn60, suggest that both proteins interact with each other, and that they function in the same intracellular compartment. Thus,<jats:italic>E. histolytica</jats:italic>appears to have retained at least two of the key molecular components required for the refolding of imported mitosomal proteins.</jats:p> Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica Microbiology |
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| title |
Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica |
| title_unstemmed |
Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica |
| title_full |
Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica |
| title_fullStr |
Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica |
| title_full_unstemmed |
Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica |
| title_short |
Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica |
| title_sort |
characterization of chaperonin 10 (cpn10) from the intestinal human pathogen entamoeba histolytica |
| topic |
Microbiology |
| url |
http://dx.doi.org/10.1099/mic.0.28068-0 |
| publishDate |
2005 |
| physical |
3107-3115 |
| description |
<jats:p><jats:italic>Entamoeba histolytica</jats:italic>is the causative agent of amoebiasis, a poverty-related disease that kills an estimated 100 000 people each year.<jats:italic>E. histolytica</jats:italic>does not contain ‘standard mitochondria’, but harbours mitochondrial remnant organelles called mitosomes. These organelles are characterized by the presence of mitochondrial chaperonin Cpn60, but little else is known about the functions and molecular composition of mitosomes. In this study, a gene encoding molecular chaperonin Cpn10 – the functional partner of Cpn60 – was cloned, and its structure and expression were characterized, as well as the cellular localization of its encoded protein. The 5′ untranslated region of the gene contains all of the structural promoter elements required for transcription in this organism. The amoebic Cpn10, like Cpn60, is not significantly upregulated upon heat-shock treatment. Computer-assisted protein modelling, and specific antibodies against Cpn10 and Cpn60, suggest that both proteins interact with each other, and that they function in the same intracellular compartment. Thus,<jats:italic>E. histolytica</jats:italic>appears to have retained at least two of the key molecular components required for the refolding of imported mitosomal proteins.</jats:p> |
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| author | van der Giezen, Mark, León-Avila, Gloria, Tovar, Jorge |
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| description | <jats:p><jats:italic>Entamoeba histolytica</jats:italic>is the causative agent of amoebiasis, a poverty-related disease that kills an estimated 100 000 people each year.<jats:italic>E. histolytica</jats:italic>does not contain ‘standard mitochondria’, but harbours mitochondrial remnant organelles called mitosomes. These organelles are characterized by the presence of mitochondrial chaperonin Cpn60, but little else is known about the functions and molecular composition of mitosomes. In this study, a gene encoding molecular chaperonin Cpn10 – the functional partner of Cpn60 – was cloned, and its structure and expression were characterized, as well as the cellular localization of its encoded protein. The 5′ untranslated region of the gene contains all of the structural promoter elements required for transcription in this organism. The amoebic Cpn10, like Cpn60, is not significantly upregulated upon heat-shock treatment. Computer-assisted protein modelling, and specific antibodies against Cpn10 and Cpn60, suggest that both proteins interact with each other, and that they function in the same intracellular compartment. Thus,<jats:italic>E. histolytica</jats:italic>appears to have retained at least two of the key molecular components required for the refolding of imported mitosomal proteins.</jats:p> |
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| spelling | van der Giezen, Mark León-Avila, Gloria Tovar, Jorge 1350-0872 1465-2080 Microbiology Society Microbiology http://dx.doi.org/10.1099/mic.0.28068-0 <jats:p><jats:italic>Entamoeba histolytica</jats:italic>is the causative agent of amoebiasis, a poverty-related disease that kills an estimated 100 000 people each year.<jats:italic>E. histolytica</jats:italic>does not contain ‘standard mitochondria’, but harbours mitochondrial remnant organelles called mitosomes. These organelles are characterized by the presence of mitochondrial chaperonin Cpn60, but little else is known about the functions and molecular composition of mitosomes. In this study, a gene encoding molecular chaperonin Cpn10 – the functional partner of Cpn60 – was cloned, and its structure and expression were characterized, as well as the cellular localization of its encoded protein. The 5′ untranslated region of the gene contains all of the structural promoter elements required for transcription in this organism. The amoebic Cpn10, like Cpn60, is not significantly upregulated upon heat-shock treatment. Computer-assisted protein modelling, and specific antibodies against Cpn10 and Cpn60, suggest that both proteins interact with each other, and that they function in the same intracellular compartment. Thus,<jats:italic>E. histolytica</jats:italic>appears to have retained at least two of the key molecular components required for the refolding of imported mitosomal proteins.</jats:p> Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica Microbiology |
| spellingShingle | van der Giezen, Mark, León-Avila, Gloria, Tovar, Jorge, Microbiology, Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica, Microbiology |
| title | Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica |
| title_full | Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica |
| title_fullStr | Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica |
| title_full_unstemmed | Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica |
| title_short | Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica |
| title_sort | characterization of chaperonin 10 (cpn10) from the intestinal human pathogen entamoeba histolytica |
| title_unstemmed | Characterization of chaperonin 10 (Cpn10) from the intestinal human pathogen Entamoeba histolytica |
| topic | Microbiology |
| url | http://dx.doi.org/10.1099/mic.0.28068-0 |