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Logo of bmcgenoBioMed Centralsearchsubmit a manuscriptregisterthis articleBMC Genomics
 
BMC Genomics. 2009; 10: 117.
Published online Mar 19, 2009. doi:  10.1186/1471-2164-10-117
PMCID: PMC2674065
Analysis of tarantula skeletal muscle protein sequences and identification of transcriptional isoforms
Jingui Zhu,#1,3 Yongqiao Sun,#1,3 Fa-Qing Zhao,2 Jun Yu,1 Roger Craig,corresponding author2 and Songnian Hucorresponding author1
1Key laboratory of Genome Sciences and Information, Beijing Institute of Genomics, Chinese Academy of Sciences, Beijing, PR China
2University of Massachusetts Medical School, Worcester, MA, USA
3The Graduate University of Chinese Academy of Sciences, Beijing, PR China
corresponding authorCorresponding author.
#Contributed equally.
Jingui Zhu: osmanthusz/at/gmail.com; Yongqiao Sun: sunyq/at/big.ac.cn; Fa-Qing Zhao: fa-qing.zhao/at/umassmed.edu; Jun Yu: junyu/at/big.ac.cn; Roger Craig: roger.craig/at/umassmed.edu; Songnian Hu: husn/at/big.ac.cn
Received October 27, 2008; Accepted March 19, 2009.
Abstract
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.
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