Building a platform for predicting functions of serine protease-related proteins in Drosophila melanogaster and other insects. (December 2018)
- Record Type:
- Journal Article
- Title:
- Building a platform for predicting functions of serine protease-related proteins in Drosophila melanogaster and other insects. (December 2018)
- Main Title:
- Building a platform for predicting functions of serine protease-related proteins in Drosophila melanogaster and other insects
- Authors:
- Cao, Xiaolong
Jiang, Haobo - Abstract:
- Abstract: Serine proteases (SPs) and serine protease homologs (SPHs) play essential roles in insect physiological processes including digestion, defense and development. Studies of insect genomes, transcriptomes and proteomes have generated a vast amount of information on these proteins, dwarfing the biological data acquired from a few model species. The large number and high diversity of homologous sequences makes it a challenge to use the limited functional information for making predictions across a broad taxonomic group of insects. In this work, we have extensively updated the framework of knowledge on the SP-related proteins in Drosophila melanogaster by identifying 52 new SPs/SPHs, classifying the 257 proteins into four groups (CLIP, gut, single- and multi-domain SPs/SPHs), and detecting inherent connections among phylogenetic relationships, genomic locations and expression profiles for 99 of the genes. Information on the existence of specific proteins in eggs, larvae, pupae and adults is presented to facilitate future research. More importantly, we have developed an approach to reveal close homologous or orthologous relationships among SPs/SPHs from D. melanogaster, Anopheles gambiae, Apis mellifera, Manduca sexta, and Tribolium castaneum thus inspiring functional studies in these and other holometabolous insects. This approach is useful for tackling similar problems on large and diverse protein families in other groups of organisms. Graphical abstract: Highlights:Abstract: Serine proteases (SPs) and serine protease homologs (SPHs) play essential roles in insect physiological processes including digestion, defense and development. Studies of insect genomes, transcriptomes and proteomes have generated a vast amount of information on these proteins, dwarfing the biological data acquired from a few model species. The large number and high diversity of homologous sequences makes it a challenge to use the limited functional information for making predictions across a broad taxonomic group of insects. In this work, we have extensively updated the framework of knowledge on the SP-related proteins in Drosophila melanogaster by identifying 52 new SPs/SPHs, classifying the 257 proteins into four groups (CLIP, gut, single- and multi-domain SPs/SPHs), and detecting inherent connections among phylogenetic relationships, genomic locations and expression profiles for 99 of the genes. Information on the existence of specific proteins in eggs, larvae, pupae and adults is presented to facilitate future research. More importantly, we have developed an approach to reveal close homologous or orthologous relationships among SPs/SPHs from D. melanogaster, Anopheles gambiae, Apis mellifera, Manduca sexta, and Tribolium castaneum thus inspiring functional studies in these and other holometabolous insects. This approach is useful for tackling similar problems on large and diverse protein families in other groups of organisms. Graphical abstract: Highlights: Extensively updated knowledge on serine protease-related proteins in the fruit fly, honey bee, and flour beetle. Inner links detected among phylogenetic relationships, genomic locations and expression profiles for 99 of the fly genes. Putative orthologous relationships revealed among S1A members from the five holometabolous insects. Physiological roles predicted on the basis of orthologous relationships and functional data. … (more)
- Is Part Of:
- Insect biochemistry and molecular biology. Volume 103(2018)
- Journal:
- Insect biochemistry and molecular biology
- Issue:
- Volume 103(2018)
- Issue Display:
- Volume 103, Issue 2018 (2018)
- Year:
- 2018
- Volume:
- 103
- Issue:
- 2018
- Issue Sort Value:
- 2018-0103-2018-0000
- Page Start:
- 53
- Page End:
- 69
- Publication Date:
- 2018-12
- Subjects:
- Phylogenetic analysis -- Gene duplication -- Chromosomal location -- Insect immunity -- Expression profiling -- Hemolymph protein -- Clip domain -- Serine protease cascade
SP serine protease -- SPH (non-catalytic) serine protease homolog -- PD SP catalytic domain -- PLD protease-like domain in SPH -- CLIP clip-domain SP or SPH -- GP and GPH gut serine protease and gut serine protease homolog -- CUB a domain in complement 1r/s, uegf and bmp1 -- FPKM fragments per kilobase of transcript per million mapped reads -- G-C-T-E group-chromosome-tree-expression -- Gd a domain in Drosophilagastrulation defective -- LDL low-density lipoprotein receptor class A repeat -- LFQ label-free quantification -- PO and proPO phenoloxidase and its proenzyme -- PAP proPO activating protease -- SEA a domain in sperm protein, enterokinase and agrin -- SRA sequence read archive -- TSP thrombospondin
Insect biochemistry -- Periodicals
Insects -- Physiology -- Periodicals
Insects -- Molecular aspects -- Periodicals
Biochemistry -- Periodicals
Insectes -- Biochimie -- Périodiques
Insectes -- Composition -- Périodiques
Insectes -- Physiologie -- Périodiques
Insectes -- Aspect moléculaire -- Périodiques
Biochimie -- Périodiques
Biochemistry
Insect biochemistry
Insects -- Molecular aspects
Insects -- Physiology
Periodicals
572.8157 - Journal URLs:
- http://www.sciencedirect.com/science/journal/09651748 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.ibmb.2018.10.006 ↗
- Languages:
- English
- ISSNs:
- 0965-1748
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 4516.852000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 8753.xml