Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions
Abstract Background Enolase (2-Phospho-D-glycerate hydrolase; EC 4.2.1.11) is one of the glycolytic enzymes, whose levels are highly elevated in malaria parasite infected red blood cells. In several organisms, enolases have been shown to have diverse non glycolytic (moonlighting) biological function...
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ftdoajarticles:oai:doaj.org/article:e54ecc90df214d148e3987d7f5c71f73 2023-05-15T15:15:50+02:00 Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions Jarori Gotam K Vora Hardeep K Pal-Bhowmick Ipsita 2007-04-01T00:00:00Z https://doi.org/10.1186/1475-2875-6-45 https://doaj.org/article/e54ecc90df214d148e3987d7f5c71f73 EN eng BMC http://www.malariajournal.com/content/6/1/45 https://doaj.org/toc/1475-2875 doi:10.1186/1475-2875-6-45 1475-2875 https://doaj.org/article/e54ecc90df214d148e3987d7f5c71f73 Malaria Journal, Vol 6, Iss 1, p 45 (2007) Arctic medicine. Tropical medicine RC955-962 Infectious and parasitic diseases RC109-216 article 2007 ftdoajarticles https://doi.org/10.1186/1475-2875-6-45 2022-12-31T03:16:50Z Abstract Background Enolase (2-Phospho-D-glycerate hydrolase; EC 4.2.1.11) is one of the glycolytic enzymes, whose levels are highly elevated in malaria parasite infected red blood cells. In several organisms, enolases have been shown to have diverse non glycolytic (moonlighting) biological functions. As functional diversity of a protein would require diverse sub-cellular localization, the possibility of involvement of Plasmodium enolase in moonlighting functions was examined by investigating its sub-cellular distribution in the murine malarial parasite, Plasmodium yoelii . Methods Cellular extracts of P. yoelii were fractionated in to soluble (cytosolic) and particulate (membranes, nuclear and cytoskeletal) fractions and were analysed by one and two-dimensional gel electrophoresis. These were probed by Western blotting using antibodies raised against recombinant Plasmodium falciparum enolase. Immunofluorescence assay was used for in situ localization. Fe +3 based metal affinity chromatography was used to isolate the phospho-proteome fraction from P. yoelii extracts. Results Apart from the expected presence of enolase in cytosol, this enzyme was also found to be associated with membranes, nuclei and cytoskeletal fractions. Nuclear presence was also confirmed by in situ immunofluorescence. Five different post translationally modified isoforms of enolase could be identified, of which at least three were due to the phosphorylation of the native form. in situ phosphorylation of enolase was also evident from the presence of enolase in purified phosphor-proteome of P. yoelli . Different sub-cellular fractions showed different isoform profiles. Conclusion Association of enolase with nuclei, cell membranes and cytoskeletal elements suggests non-glycolytic functions for this enzyme in P. yoelii . Sub-cellular fraction specific isoform profiles indicate the importance of post-translational modifications in diverse localization of enolase in P. yoelii . Further, it is suggested that post-translational modifications of ... Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic Malaria Journal 6 1 45 |
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Arctic medicine. Tropical medicine RC955-962 Infectious and parasitic diseases RC109-216 |
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Arctic medicine. Tropical medicine RC955-962 Infectious and parasitic diseases RC109-216 Jarori Gotam K Vora Hardeep K Pal-Bhowmick Ipsita Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions |
topic_facet |
Arctic medicine. Tropical medicine RC955-962 Infectious and parasitic diseases RC109-216 |
description |
Abstract Background Enolase (2-Phospho-D-glycerate hydrolase; EC 4.2.1.11) is one of the glycolytic enzymes, whose levels are highly elevated in malaria parasite infected red blood cells. In several organisms, enolases have been shown to have diverse non glycolytic (moonlighting) biological functions. As functional diversity of a protein would require diverse sub-cellular localization, the possibility of involvement of Plasmodium enolase in moonlighting functions was examined by investigating its sub-cellular distribution in the murine malarial parasite, Plasmodium yoelii . Methods Cellular extracts of P. yoelii were fractionated in to soluble (cytosolic) and particulate (membranes, nuclear and cytoskeletal) fractions and were analysed by one and two-dimensional gel electrophoresis. These were probed by Western blotting using antibodies raised against recombinant Plasmodium falciparum enolase. Immunofluorescence assay was used for in situ localization. Fe +3 based metal affinity chromatography was used to isolate the phospho-proteome fraction from P. yoelii extracts. Results Apart from the expected presence of enolase in cytosol, this enzyme was also found to be associated with membranes, nuclei and cytoskeletal fractions. Nuclear presence was also confirmed by in situ immunofluorescence. Five different post translationally modified isoforms of enolase could be identified, of which at least three were due to the phosphorylation of the native form. in situ phosphorylation of enolase was also evident from the presence of enolase in purified phosphor-proteome of P. yoelli . Different sub-cellular fractions showed different isoform profiles. Conclusion Association of enolase with nuclei, cell membranes and cytoskeletal elements suggests non-glycolytic functions for this enzyme in P. yoelii . Sub-cellular fraction specific isoform profiles indicate the importance of post-translational modifications in diverse localization of enolase in P. yoelii . Further, it is suggested that post-translational modifications of ... |
format |
Article in Journal/Newspaper |
author |
Jarori Gotam K Vora Hardeep K Pal-Bhowmick Ipsita |
author_facet |
Jarori Gotam K Vora Hardeep K Pal-Bhowmick Ipsita |
author_sort |
Jarori Gotam K |
title |
Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions |
title_short |
Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions |
title_full |
Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions |
title_fullStr |
Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions |
title_full_unstemmed |
Sub-cellular localization and post-translational modifications of the Plasmodium yoelii enolase suggest moonlighting functions |
title_sort |
sub-cellular localization and post-translational modifications of the plasmodium yoelii enolase suggest moonlighting functions |
publisher |
BMC |
publishDate |
2007 |
url |
https://doi.org/10.1186/1475-2875-6-45 https://doaj.org/article/e54ecc90df214d148e3987d7f5c71f73 |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
Malaria Journal, Vol 6, Iss 1, p 45 (2007) |
op_relation |
http://www.malariajournal.com/content/6/1/45 https://doaj.org/toc/1475-2875 doi:10.1186/1475-2875-6-45 1475-2875 https://doaj.org/article/e54ecc90df214d148e3987d7f5c71f73 |
op_doi |
https://doi.org/10.1186/1475-2875-6-45 |
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Malaria Journal |
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6 |
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1 |
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45 |
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1766346171459043328 |