A photocytes-associated fatty acid-binding protein from the light organ of adult Taiwanese firefly, Luciola cerata.
BACKGROUND: Intracellular fatty acid-binding proteins (FABPs) are considered to be an important energy source supplier in lipid metabolism; however, they have never been reported in any bioluminescent tissue before. In this study, we determined the structural and functional characteristics of a nove...
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doaj-ae8dec118cc448ecbb53f22f0150eac62020-11-25T02:39:29ZengPublic Library of Science (PLoS)PLoS ONE1932-62032011-01-01612e2957610.1371/journal.pone.0029576A photocytes-associated fatty acid-binding protein from the light organ of adult Taiwanese firefly, Luciola cerata.King-Siang GohChia-Wei LiBACKGROUND: Intracellular fatty acid-binding proteins (FABPs) are considered to be an important energy source supplier in lipid metabolism; however, they have never been reported in any bioluminescent tissue before. In this study, we determined the structural and functional characteristics of a novel FABP (lcFABP) from the light organ of adult Taiwanese firefly, Luciola cerata, and showed anatomical association of lcFABP with photocytes. PRINCIPAL FINDINGS: Our results demonstrated the primary structure of lcFABP deduced from the cDNA clone of light organ shares structural homologies with other insect and human FABPs. In vitro binding assay indicated the recombinant lcFABP binds saturated long chain fatty acids (C₁₄-C₁₈) more strongly than other fatty acids and firefly luciferin. In addition, tissue distribution screening assay using a rabbit antiserum specifically against the N-terminal sequence of lcFABP confirmed the light organ-specific expression of lcFABP. In the light organ, the lcFABP constituted about 15% of total soluble proteins, and was detected in both cytosol and nucleus of photocytes. CONCLUSIONS: The specific localization of abundant lcFABP in the light organ suggests that sustained bioluminescent flashes in the light organ might be a high energy demanding process. In photocytes, lcFABP might play a key role in providing long chain fatty acids to peroxisomes for the luciferase-catalyzed long chain acyl-CoA synthetic reaction.http://europepmc.org/articles/PMC3248459?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
King-Siang Goh Chia-Wei Li |
spellingShingle |
King-Siang Goh Chia-Wei Li A photocytes-associated fatty acid-binding protein from the light organ of adult Taiwanese firefly, Luciola cerata. PLoS ONE |
author_facet |
King-Siang Goh Chia-Wei Li |
author_sort |
King-Siang Goh |
title |
A photocytes-associated fatty acid-binding protein from the light organ of adult Taiwanese firefly, Luciola cerata. |
title_short |
A photocytes-associated fatty acid-binding protein from the light organ of adult Taiwanese firefly, Luciola cerata. |
title_full |
A photocytes-associated fatty acid-binding protein from the light organ of adult Taiwanese firefly, Luciola cerata. |
title_fullStr |
A photocytes-associated fatty acid-binding protein from the light organ of adult Taiwanese firefly, Luciola cerata. |
title_full_unstemmed |
A photocytes-associated fatty acid-binding protein from the light organ of adult Taiwanese firefly, Luciola cerata. |
title_sort |
photocytes-associated fatty acid-binding protein from the light organ of adult taiwanese firefly, luciola cerata. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2011-01-01 |
description |
BACKGROUND: Intracellular fatty acid-binding proteins (FABPs) are considered to be an important energy source supplier in lipid metabolism; however, they have never been reported in any bioluminescent tissue before. In this study, we determined the structural and functional characteristics of a novel FABP (lcFABP) from the light organ of adult Taiwanese firefly, Luciola cerata, and showed anatomical association of lcFABP with photocytes. PRINCIPAL FINDINGS: Our results demonstrated the primary structure of lcFABP deduced from the cDNA clone of light organ shares structural homologies with other insect and human FABPs. In vitro binding assay indicated the recombinant lcFABP binds saturated long chain fatty acids (C₁₄-C₁₈) more strongly than other fatty acids and firefly luciferin. In addition, tissue distribution screening assay using a rabbit antiserum specifically against the N-terminal sequence of lcFABP confirmed the light organ-specific expression of lcFABP. In the light organ, the lcFABP constituted about 15% of total soluble proteins, and was detected in both cytosol and nucleus of photocytes. CONCLUSIONS: The specific localization of abundant lcFABP in the light organ suggests that sustained bioluminescent flashes in the light organ might be a high energy demanding process. In photocytes, lcFABP might play a key role in providing long chain fatty acids to peroxisomes for the luciferase-catalyzed long chain acyl-CoA synthetic reaction. |
url |
http://europepmc.org/articles/PMC3248459?pdf=render |
work_keys_str_mv |
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