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Temporal regulation of proteome profile in the fruit fly, Drosophila melanogaster

Background. Diurnal rhythms of protein synthesis controlled by the biological clock underlie the rhythmic physiology in the fruit fly, Drosophila melanogaster. In this study, we conducted a proteome-wide investigation of rhythmic protein accumulation in D. melanogaster. Materials and Methods. Total...

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Autores principales: Subramanian, Perumal, Jayapalan, Jaime J., Abdul-Rahman, Puteri S., Arumugam, Manjula, Hashim, Onn H.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: PeerJ Inc. 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4888302/
https://www.ncbi.nlm.nih.gov/pubmed/27257555
http://dx.doi.org/10.7717/peerj.2080
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author Subramanian, Perumal
Jayapalan, Jaime J.
Abdul-Rahman, Puteri S.
Arumugam, Manjula
Hashim, Onn H.
author_facet Subramanian, Perumal
Jayapalan, Jaime J.
Abdul-Rahman, Puteri S.
Arumugam, Manjula
Hashim, Onn H.
author_sort Subramanian, Perumal
collection PubMed
description Background. Diurnal rhythms of protein synthesis controlled by the biological clock underlie the rhythmic physiology in the fruit fly, Drosophila melanogaster. In this study, we conducted a proteome-wide investigation of rhythmic protein accumulation in D. melanogaster. Materials and Methods. Total protein collected from fly samples harvested at 4 h intervals over the 24 h period were subjected to two-dimensional gel electrophoresis, trypsin digestion and MS/MS analysis. Protein spots/clusters were identified with MASCOT search engine and Swiss-Prot database. Expression of proteins was documented as percentage of volume contribution using the Image Master 2D Platinum software. Results. A total of 124 protein spots/clusters were identified using MS/MS analysis. Significant variation in the expression of 88 proteins over the 24-h period was observed. A relatively higher number of proteins was upregulated during the night compared to the daytime. The complexity of temporal regulation of the D. melanogaster proteome was further reflected from functional annotations of the differently expressed proteins, with those that were upregulated at night being restricted to the heat shock proteins and proteins involved in metabolism, muscle activity, protein synthesis/folding/degradation and apoptosis, whilst those that were overexpressed in the daytime were apparently involved in metabolism, muscle activity, ion-channel/cellular transport, protein synthesis/folding/degradation, redox homeostasis, development and transcription. Conclusion. Our data suggests that a wide range of proteins synthesized by the fruit fly, D. melanogaster, is under the regulation of the biological clock.
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spelling pubmed-48883022016-06-02 Temporal regulation of proteome profile in the fruit fly, Drosophila melanogaster Subramanian, Perumal Jayapalan, Jaime J. Abdul-Rahman, Puteri S. Arumugam, Manjula Hashim, Onn H. PeerJ Biochemistry Background. Diurnal rhythms of protein synthesis controlled by the biological clock underlie the rhythmic physiology in the fruit fly, Drosophila melanogaster. In this study, we conducted a proteome-wide investigation of rhythmic protein accumulation in D. melanogaster. Materials and Methods. Total protein collected from fly samples harvested at 4 h intervals over the 24 h period were subjected to two-dimensional gel electrophoresis, trypsin digestion and MS/MS analysis. Protein spots/clusters were identified with MASCOT search engine and Swiss-Prot database. Expression of proteins was documented as percentage of volume contribution using the Image Master 2D Platinum software. Results. A total of 124 protein spots/clusters were identified using MS/MS analysis. Significant variation in the expression of 88 proteins over the 24-h period was observed. A relatively higher number of proteins was upregulated during the night compared to the daytime. The complexity of temporal regulation of the D. melanogaster proteome was further reflected from functional annotations of the differently expressed proteins, with those that were upregulated at night being restricted to the heat shock proteins and proteins involved in metabolism, muscle activity, protein synthesis/folding/degradation and apoptosis, whilst those that were overexpressed in the daytime were apparently involved in metabolism, muscle activity, ion-channel/cellular transport, protein synthesis/folding/degradation, redox homeostasis, development and transcription. Conclusion. Our data suggests that a wide range of proteins synthesized by the fruit fly, D. melanogaster, is under the regulation of the biological clock. PeerJ Inc. 2016-05-24 /pmc/articles/PMC4888302/ /pubmed/27257555 http://dx.doi.org/10.7717/peerj.2080 Text en ©2016 Subramanian et al. http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) , which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ) and either DOI or URL of the article must be cited.
spellingShingle Biochemistry
Subramanian, Perumal
Jayapalan, Jaime J.
Abdul-Rahman, Puteri S.
Arumugam, Manjula
Hashim, Onn H.
Temporal regulation of proteome profile in the fruit fly, Drosophila melanogaster
title Temporal regulation of proteome profile in the fruit fly, Drosophila melanogaster
title_full Temporal regulation of proteome profile in the fruit fly, Drosophila melanogaster
title_fullStr Temporal regulation of proteome profile in the fruit fly, Drosophila melanogaster
title_full_unstemmed Temporal regulation of proteome profile in the fruit fly, Drosophila melanogaster
title_short Temporal regulation of proteome profile in the fruit fly, Drosophila melanogaster
title_sort temporal regulation of proteome profile in the fruit fly, drosophila melanogaster
topic Biochemistry
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4888302/
https://www.ncbi.nlm.nih.gov/pubmed/27257555
http://dx.doi.org/10.7717/peerj.2080
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