Differential Scanning Calorimetry of Light Meromyosin Fragments Having Various Lengths of Carp Fast Skeletal Muscle Isoforms.
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概要
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Various recombinant light meromyosin (LMM) fragments were prepared from cDNAs encoding the 10°C and 30°C types of myosin heavy chain isoforms predominantly expressed in fast skeletal muscles of the 10°C-and 30°C-acclimated carp, respectively. These included three kinds of quarter fragments, 1/4-, 2/4-, and 4/4-quarter, composed of residues 1-130, 131-270, and 401-563 from the N-terminus, respectively, as well as three halves, N-, M-, and C-half fragments, containing residues 1-301, 131-400, and 302-563, respectively, and 69K fragments of residues 1-525. Unfortunately, in spite of extensive efforts, the 3/4-quarter fragment was not expressed for both 10°C and 30°C types in our expression system using Escherichia coli. All the LMM fragments except for the 10-and 30-2/4 quarters for the 10°C and 30°C types, respectively, exhibited a typical pattern of α-helix in CD spectrometry. When these were subjected to differential scanning calorimetry (DSC), 30°C-type LMM fragments were all found to be more thermostable than the 10°C-type counterparts. To identify amino acid substitutions responsible for different thermostabilities between the 10°C- and 30°C-type LMMs, six mutant proteins were prepared, mainly focusing on substitutions in the C-terminal half of LMM, and subjected to DSC and CD analyses. For three mutants in which two residues of the 10°C type were replaced by those of the 30°C type, 10-S355T/T361A, 10-M415L/L417V, and 10-S535A/ H536Q, the endothermic peaks in DSC increased by 1.4-2.0°C from that of the original 10°C type. The Tm values for two single-residue substitutions, 10-H449R and 10-T491I, shifted 0.8 and 1.3°C higher than that for the 10°C-type LMM, respectively, whereas the last mutant, 10-G61V, showed no change in thermostability. The finding that the difference in Tm values for major endothermic peaks from the 10-69K and 30-69K fragments was 4.6°C, which roughly corresponds to that between the original 10°C and 30°C types, suggested that the eight substitutions located in the C-terminal region of the 69K fragments (residues 302-525) are major candidates for the residues responsible for the difference in thermostability between the 10°C- and 30°C-type LMMs.
- 社団法人 日本生化学会の論文
著者
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Kakinuma Makoto
Laboratory Of Aquatic Molecular Biology And Biotechnology Graduate School Of Agricultural And Life S
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MAEDA Kayo
The Institute of Physical and Chemical Research (RIKEN)
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Doi Yukio
Department Of Agricultural Chemistry Faculty Of Agriculture Shinshu University
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Nakaya Misako
Laboratory Of Aquatic Molecular Biology And Biotechnology Graduate School Of Agricultural And Life S
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Fukushima Hideto
Laboratory Of Aquatic Molecular Biology And Biotechnology Graduate School Of Agricultural And Life S
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Watabe Shugo
Laboratory Of Aquatic Molecular Bilhogy And Biotechnology Graduate School Of Agricultural And Life S
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Hatanaka Akimasa
Laboratory Of Aquatic Molecular Biology And Biotechnology Graduate School Of Agricultural And Life S
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Ooi Tatsuo
Department Of Food Science Kyoto Women's Unversity
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Nakaya Misako
Laboratory of Aquatic Molecular Biology and Biotechnology, Graduate School of Agricultural and Life Science, The University of Tokyo
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Doi Yukio
Department of Food Science, Kyoto Women's Univesity
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