کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2819035 1569899 2009 10 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Myosin heavy chain genes expressed in juvenile and adult silver carp Hypopthalmichthys molitrix: Novel fast-type myosin heavy chain genes of silver carp
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی ژنتیک
پیش نمایش صفحه اول مقاله
Myosin heavy chain genes expressed in juvenile and adult silver carp Hypopthalmichthys molitrix: Novel fast-type myosin heavy chain genes of silver carp
چکیده انگلیسی

Silver carp Hypopthalmichthys molitrix is eurythermal temperate fish, whose muscle is considered to express several types of myosin heavy chain (MYH) genes at different stages of its growth and to adjust to the environmental temperature. In this study, MYH genes expressed in the muscles of juvenile and adult silver carp were investigated. Five types of MYH cDNA clone were isolated from silver carp (H. molitrix) by RACE strategy using a set of fast-type MYH specific primers, and termed scMYHF1, scMYHF2, scMYHF3, scMYHF4 and scMYHF5 in the order of their abundance in cDNA libraries constructed from fast skeletal muscles of adult silver carp. scMYHF1, scMYHF3 and scMYHF5 showed high nucleotide sequence identities of 96, 98 and 96% to gcMYHF30, gcMYHF10 and gcMYHFI, respectively, that encode MYHs predominantly expressed in fast skeletal muscle of grass carp (Ctenopharyngodon idella) acclimated to 30, 10 and 20 °C, respectively. scMYHF2 and scMYHF4 showed a high identity to A4-type MYH from rock cod (Notothenia coriiceps) slow skeletal muscle. Phylogenetic analysis demonstrated that scMYHF1 and scMYHF5 were monophyletic with fish adult fast-type MYHs, whereas scMYHF2 and scMYHF4 formed a cluster with fish slow-like fast-type MYH, and scMYHF3 did with fish embryonic fast-type MYHs. Interestingly, juvenile silver carp predominantly expressed scMYHF3 irrespective of acclimation temperatures at 10, 18 or 26 °C. The comparison among scMYHF1, scMYHF2 and scMYHF3 in the deduced amino acid sequence revealed that the putative binding sites for ATP, actin, and essential and regulatory light chains in myosin subfragment-1 (S1) have high identities with each other (81–100%). However, their loop-1 and loop-2 regions in S1 were highly variable, suggesting their different functions. The deduced amino acid sequences of myosin subfragment-2 and L-meromyosin showed high identities of 90–91% and 86–90%, respectively, among the above three scMYHs.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Gene - Volume 432, Issues 1–2, 1 March 2009, Pages 102–111
نویسندگان
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