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In silico Identification of Novel Chitinase-Like Proteins in the Silkworm, Bombyx mori, Genome
In insects, chitinases participate in the periodic shedding of old exoskeletons and the turnover of peritrophic membranes. Chitinase family members have been identified in dozens of species, including Tribolium castaneum, Drosophila melanogaster, and Anopheles gambiae. In this study, nine chitinases...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
University of Wisconsin Library
2012
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3646613/ https://www.ncbi.nlm.nih.gov/pubmed/23461297 http://dx.doi.org/10.1673/031.012.15001 |
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author | Pan, Ye Lü, Peng Wang, Yong Yin, Lijing Ma, Hexiang Ma, Guohong Chen, Keping He, Yuanqing |
author_facet | Pan, Ye Lü, Peng Wang, Yong Yin, Lijing Ma, Hexiang Ma, Guohong Chen, Keping He, Yuanqing |
author_sort | Pan, Ye |
collection | PubMed |
description | In insects, chitinases participate in the periodic shedding of old exoskeletons and the turnover of peritrophic membranes. Chitinase family members have been identified in dozens of species, including Tribolium castaneum, Drosophila melanogaster, and Anopheles gambiae. In this study, nine chitinases and three hypothetical chitinases have been identified in Bombyx mori L. (Lepidoptera: Bombycidae) through genome-wide searching. Phylogenetic analyses revealed that seven of them belong to the seven chitinase groups, respectively. BmCht25 and BmCht26 could not be grouped into the known chitinase groups, and might belong to two new groups of the chitinase family. BmCht10, BmCht25, and BmIDGF have glutamate amino acid substitutions in the active catalytic domain. Only BmCht5 and BmCht10 contain CBD domain and PEST sequences (rich in proline, glutamic acid, serine, and threonine). BmCht5 and BmCht26 are located on chromosome 7, and others (BmCht6, BmCht7, BmCht10, BmCht11, BmCht20, BmIDGF) are located on separate chromosomes of Bombyx mori, respectively. The present study provides important background information for future studies using Bombyx mori as a model organism for insect development and virus and host interaction. |
format | Online Article Text |
id | pubmed-3646613 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2012 |
publisher | University of Wisconsin Library |
record_format | MEDLINE/PubMed |
spelling | pubmed-36466132013-05-09 In silico Identification of Novel Chitinase-Like Proteins in the Silkworm, Bombyx mori, Genome Pan, Ye Lü, Peng Wang, Yong Yin, Lijing Ma, Hexiang Ma, Guohong Chen, Keping He, Yuanqing J Insect Sci Article In insects, chitinases participate in the periodic shedding of old exoskeletons and the turnover of peritrophic membranes. Chitinase family members have been identified in dozens of species, including Tribolium castaneum, Drosophila melanogaster, and Anopheles gambiae. In this study, nine chitinases and three hypothetical chitinases have been identified in Bombyx mori L. (Lepidoptera: Bombycidae) through genome-wide searching. Phylogenetic analyses revealed that seven of them belong to the seven chitinase groups, respectively. BmCht25 and BmCht26 could not be grouped into the known chitinase groups, and might belong to two new groups of the chitinase family. BmCht10, BmCht25, and BmIDGF have glutamate amino acid substitutions in the active catalytic domain. Only BmCht5 and BmCht10 contain CBD domain and PEST sequences (rich in proline, glutamic acid, serine, and threonine). BmCht5 and BmCht26 are located on chromosome 7, and others (BmCht6, BmCht7, BmCht10, BmCht11, BmCht20, BmIDGF) are located on separate chromosomes of Bombyx mori, respectively. The present study provides important background information for future studies using Bombyx mori as a model organism for insect development and virus and host interaction. University of Wisconsin Library 2012-12-27 /pmc/articles/PMC3646613/ /pubmed/23461297 http://dx.doi.org/10.1673/031.012.15001 Text en © 2012 http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Article Pan, Ye Lü, Peng Wang, Yong Yin, Lijing Ma, Hexiang Ma, Guohong Chen, Keping He, Yuanqing In silico Identification of Novel Chitinase-Like Proteins in the Silkworm, Bombyx mori, Genome |
title |
In silico Identification of Novel Chitinase-Like Proteins in the Silkworm, Bombyx mori, Genome |
title_full |
In silico Identification of Novel Chitinase-Like Proteins in the Silkworm, Bombyx mori, Genome |
title_fullStr |
In silico Identification of Novel Chitinase-Like Proteins in the Silkworm, Bombyx mori, Genome |
title_full_unstemmed |
In silico Identification of Novel Chitinase-Like Proteins in the Silkworm, Bombyx mori, Genome |
title_short |
In silico Identification of Novel Chitinase-Like Proteins in the Silkworm, Bombyx mori, Genome |
title_sort | in silico identification of novel chitinase-like proteins in the silkworm, bombyx mori, genome |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3646613/ https://www.ncbi.nlm.nih.gov/pubmed/23461297 http://dx.doi.org/10.1673/031.012.15001 |
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