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Analysis of tarantula skeletal muscle protein sequences and identification of transcriptional isoforms
BACKGROUND: Tarantula has been used as a model system for studying skeletal muscle structure and function, yet data on the genes expressed in tarantula muscle are lacking. RESULTS: We constructed a cDNA library from Aphonopelma sp. (Tarantula) skeletal muscle and got 2507 high-quality 5'ESTs (e...
Autores principales: | , , , , , |
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Formato: | Texto |
Lenguaje: | English |
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BioMed Central
2009
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2674065/ https://www.ncbi.nlm.nih.gov/pubmed/19298669 http://dx.doi.org/10.1186/1471-2164-10-117 |
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author | Zhu, Jingui Sun, Yongqiao Zhao, Fa-Qing Yu, Jun Craig, Roger Hu, Songnian |
author_facet | Zhu, Jingui Sun, Yongqiao Zhao, Fa-Qing Yu, Jun Craig, Roger Hu, Songnian |
author_sort | Zhu, Jingui |
collection | PubMed |
description | BACKGROUND: Tarantula has been used as a model system for studying skeletal muscle structure and function, yet data on the genes expressed in tarantula muscle are lacking. RESULTS: We constructed a cDNA library from Aphonopelma sp. (Tarantula) skeletal muscle and got 2507 high-quality 5'ESTs (expressed sequence tags) from randomly picked clones. EST analysis showed 305 unigenes, among which 81 had more than 2 ESTs. Twenty abundant unigenes had matches to skeletal muscle-related genes including actin, myosin, tropomyosin, troponin-I, T and C, paramyosin, muscle LIM protein, muscle protein 20, a-actinin and tandem Ig/Fn motifs (found in giant sarcomere-related proteins). Matches to myosin light chain kinase and calponin were also identified. These results support the existence of both actin-linked and myosin-linked regulation in tarantula skeletal muscle. We have predicted full-length as well as partial cDNA sequences both experimentally and computationally for myosin heavy and light chains, actin, tropomyosin, and troponin-I, T and C, and have deduced the putative peptides. A preliminary analysis of the structural and functional properties was also carried out. Sequence similarities suggested multiple isoforms of most myofibrillar proteins, supporting the generality of multiple isoforms known from previous muscle sequence studies. This may be related to a mix of muscle fiber types. CONCLUSION: The present study serves as a basis for defining the transcriptome of tarantula skeletal muscle, for future in vitro expression of tarantula proteins, and for interpreting structural and functional observations in this model species. |
format | Text |
id | pubmed-2674065 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2009 |
publisher | BioMed Central |
record_format | MEDLINE/PubMed |
spelling | pubmed-26740652009-04-28 Analysis of tarantula skeletal muscle protein sequences and identification of transcriptional isoforms Zhu, Jingui Sun, Yongqiao Zhao, Fa-Qing Yu, Jun Craig, Roger Hu, Songnian BMC Genomics Research Article BACKGROUND: Tarantula has been used as a model system for studying skeletal muscle structure and function, yet data on the genes expressed in tarantula muscle are lacking. RESULTS: We constructed a cDNA library from Aphonopelma sp. (Tarantula) skeletal muscle and got 2507 high-quality 5'ESTs (expressed sequence tags) from randomly picked clones. EST analysis showed 305 unigenes, among which 81 had more than 2 ESTs. Twenty abundant unigenes had matches to skeletal muscle-related genes including actin, myosin, tropomyosin, troponin-I, T and C, paramyosin, muscle LIM protein, muscle protein 20, a-actinin and tandem Ig/Fn motifs (found in giant sarcomere-related proteins). Matches to myosin light chain kinase and calponin were also identified. These results support the existence of both actin-linked and myosin-linked regulation in tarantula skeletal muscle. We have predicted full-length as well as partial cDNA sequences both experimentally and computationally for myosin heavy and light chains, actin, tropomyosin, and troponin-I, T and C, and have deduced the putative peptides. A preliminary analysis of the structural and functional properties was also carried out. Sequence similarities suggested multiple isoforms of most myofibrillar proteins, supporting the generality of multiple isoforms known from previous muscle sequence studies. This may be related to a mix of muscle fiber types. CONCLUSION: The present study serves as a basis for defining the transcriptome of tarantula skeletal muscle, for future in vitro expression of tarantula proteins, and for interpreting structural and functional observations in this model species. BioMed Central 2009-03-19 /pmc/articles/PMC2674065/ /pubmed/19298669 http://dx.doi.org/10.1186/1471-2164-10-117 Text en Copyright © 2009 Zhu et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Research Article Zhu, Jingui Sun, Yongqiao Zhao, Fa-Qing Yu, Jun Craig, Roger Hu, Songnian Analysis of tarantula skeletal muscle protein sequences and identification of transcriptional isoforms |
title | Analysis of tarantula skeletal muscle protein sequences and identification of transcriptional isoforms |
title_full | Analysis of tarantula skeletal muscle protein sequences and identification of transcriptional isoforms |
title_fullStr | Analysis of tarantula skeletal muscle protein sequences and identification of transcriptional isoforms |
title_full_unstemmed | Analysis of tarantula skeletal muscle protein sequences and identification of transcriptional isoforms |
title_short | Analysis of tarantula skeletal muscle protein sequences and identification of transcriptional isoforms |
title_sort | analysis of tarantula skeletal muscle protein sequences and identification of transcriptional isoforms |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2674065/ https://www.ncbi.nlm.nih.gov/pubmed/19298669 http://dx.doi.org/10.1186/1471-2164-10-117 |
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