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BmAbl1 Regulates Silk Protein Synthesis via Glutathione Metabolism in Bombyx mori
SIMPLE SUMMARY: Silk yield is the primary economic character in sericulture. During the past 5000 years of domestication, great effort has been made to increase cocoon shell weight (CSW). However, silk yield is a complex trait controlled by quantitative trait loci (QTLs). From these QTLs, BmAbl1 tyr...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9696079/ https://www.ncbi.nlm.nih.gov/pubmed/36354792 http://dx.doi.org/10.3390/insects13110967 |
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author | Qin, Sheng Sun, Lingling Zhang, Shu Sun, Xia Li, Muwang |
author_facet | Qin, Sheng Sun, Lingling Zhang, Shu Sun, Xia Li, Muwang |
author_sort | Qin, Sheng |
collection | PubMed |
description | SIMPLE SUMMARY: Silk yield is the primary economic character in sericulture. During the past 5000 years of domestication, great effort has been made to increase cocoon shell weight (CSW). However, silk yield is a complex trait controlled by quantitative trait loci (QTLs). From these QTLs, BmAbl1 tyrosine kinase, which is located at chromosome 1, is considered to be closely related to CSW. In our study, the functional loss of BmAbl1 led to altered glutathione metabolism, which ultimately affects the amino acid synthesis and metabolic pathway, impairing silk fibroin protein synthesis. We further investigated the role of BmAbl1 in regulating silk fibroin secretion. A new perspective was taken on factors affecting silk fibroin synthesis. This provides a new idea to improve silk fibroin yield. It lays the groundwork for improving silk yield in the future. ABSTRACT: Bombyx mori, domesticated from wild silkworms, is an economic insect that feeds on mulberry leaves and produces silk. In the current study, we demonstrated the contribution of BmAbl1 in silk protein synthesis. The inhibition and knockout of BmAbl1 can reduce the larva weight and CSW. The effect on CSW of BmAbl1 is not on the transcriptional level, but on the translational level. RNA-sequencing data suggested that amino acid synthesis and the metabolism process had a great difference between the BmAbl1(-) and Control strain, particularly glutathione metabolism. An abnormality in glutathione metabolism led to the reduction of free glycine and serine content, which are the main components of fibroin protein. Finally, fibroin protein synthesis has been reduced, including fibroin-heavy chain, fibroin-light chain, and p25 protein. This finding brought to light the role of BmAbl1 in the silk protein synthesis process. |
format | Online Article Text |
id | pubmed-9696079 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-96960792022-11-26 BmAbl1 Regulates Silk Protein Synthesis via Glutathione Metabolism in Bombyx mori Qin, Sheng Sun, Lingling Zhang, Shu Sun, Xia Li, Muwang Insects Article SIMPLE SUMMARY: Silk yield is the primary economic character in sericulture. During the past 5000 years of domestication, great effort has been made to increase cocoon shell weight (CSW). However, silk yield is a complex trait controlled by quantitative trait loci (QTLs). From these QTLs, BmAbl1 tyrosine kinase, which is located at chromosome 1, is considered to be closely related to CSW. In our study, the functional loss of BmAbl1 led to altered glutathione metabolism, which ultimately affects the amino acid synthesis and metabolic pathway, impairing silk fibroin protein synthesis. We further investigated the role of BmAbl1 in regulating silk fibroin secretion. A new perspective was taken on factors affecting silk fibroin synthesis. This provides a new idea to improve silk fibroin yield. It lays the groundwork for improving silk yield in the future. ABSTRACT: Bombyx mori, domesticated from wild silkworms, is an economic insect that feeds on mulberry leaves and produces silk. In the current study, we demonstrated the contribution of BmAbl1 in silk protein synthesis. The inhibition and knockout of BmAbl1 can reduce the larva weight and CSW. The effect on CSW of BmAbl1 is not on the transcriptional level, but on the translational level. RNA-sequencing data suggested that amino acid synthesis and the metabolism process had a great difference between the BmAbl1(-) and Control strain, particularly glutathione metabolism. An abnormality in glutathione metabolism led to the reduction of free glycine and serine content, which are the main components of fibroin protein. Finally, fibroin protein synthesis has been reduced, including fibroin-heavy chain, fibroin-light chain, and p25 protein. This finding brought to light the role of BmAbl1 in the silk protein synthesis process. MDPI 2022-10-22 /pmc/articles/PMC9696079/ /pubmed/36354792 http://dx.doi.org/10.3390/insects13110967 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Qin, Sheng Sun, Lingling Zhang, Shu Sun, Xia Li, Muwang BmAbl1 Regulates Silk Protein Synthesis via Glutathione Metabolism in Bombyx mori |
title | BmAbl1 Regulates Silk Protein Synthesis via Glutathione Metabolism in Bombyx mori |
title_full | BmAbl1 Regulates Silk Protein Synthesis via Glutathione Metabolism in Bombyx mori |
title_fullStr | BmAbl1 Regulates Silk Protein Synthesis via Glutathione Metabolism in Bombyx mori |
title_full_unstemmed | BmAbl1 Regulates Silk Protein Synthesis via Glutathione Metabolism in Bombyx mori |
title_short | BmAbl1 Regulates Silk Protein Synthesis via Glutathione Metabolism in Bombyx mori |
title_sort | bmabl1 regulates silk protein synthesis via glutathione metabolism in bombyx mori |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9696079/ https://www.ncbi.nlm.nih.gov/pubmed/36354792 http://dx.doi.org/10.3390/insects13110967 |
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