Identification of the glutamine residue that may be involved in the transglutaminase-mediated intramolecular crosslinking of carp and walleye pollack myosin |
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| Authors: | Hisanori Nozawa Mai Ezou |
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| Institution: | (1) Faculty of Fisheries Sciences, Hokkaido University, Hakodate Hokkaido, 041-8611, Japan |
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| Abstract: | In order to elucidate the molecular mechanism of transglutaminase-mediated myosin crosslinking, a fluorescent monodansylcadaverine
(MDC) was incorporated into carp Cyprinus carpio myosin and the reactive Gln residues were analyzed by cyanogen bromide cleavage. The fluorescence was predominantly detected
in a 10.5 kDa BrCN fragment, assumed to be located in subfragment 2 of the myosin heavy chain. Furthermore, lysyl endopeptidase
digestion of the 10.5 kDa fragment revealed that MDC was specifically incorporated into the 520th Gln residue of the subfragment
2 domain. When meat paste prepared from frozen walleye pollack (Theragra chalcogramma) surimi was incubated with MDC, the fluorescence was mostly observed in a 16 kDa BrCN fragment and also slightly detected
in other three bands. By digesting the 16 kDa fragment with lysyl endopeptidase, it was elucidated that MDC was incorporated
specifically into Gln-520 of myosin subfragment 2, as also detected in carp. This domain around Gln-520 is likely to be a
critical region for the formation of myosin heavy chain dimers that both fish species have in common. In walleye pollack,
other reactive Gln residues are presumed to exist at the C-terminus of the light meromyosin. This slight difference may have
a significant effect on the capacity of myosin to form tetramers or even larger multimers. |
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