Publications by authors named "Kengo Nakano"

Article Synopsis
  • Understanding how microplastics behave in oceans is key to tackling marine plastic pollution, especially since the deep seafloor is a major accumulation area for them.
  • A study in Sagami Bay revealed that the deepest parts of the ocean had a higher density of microplastics than previously seen, showing significant differences in the types and shapes of plastic found there compared to shallower areas.
  • The research indicates that microplastics from the surface layer sink to the abyssal plains, while those from land sources settle in shallower depths and are moved deeper by underwater currents.
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In order to determine the amino-terminal sequence requirements for protein N-myristoylation, site-directed mutagenesis of the N-terminal region was performed using tumor necrosis factor (TNF) mutants as model substrate proteins. Subsequently, the susceptibility of these mutants to protein N-myristoylation was evaluated by metabolic labeling in an in vitro translation system using rabbit reticulocyte lysate. A TNF mutant having the sequence MGAAAAAAAA at its N-terminus was used as the starting sequence to identify elements critical for protein N-myristoylation.

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To detect the posttranslational N-myristoylation of caspase substrates, the susceptibility of the newly exposed N-terminus of known caspase substrates to protein N-myristoylation was evaluated by in vivo metabolic labeling with [(3)H]myristic acid in transfected cells using a fusion protein in which the query sequence was fused to a model protein. As a result, it was found that the N-terminal nine residues of the newly exposed N-terminus of the caspase-cleavage product of cytoskeletal actin efficiently direct the protein N-myristoylation. Metabolic labeling of COS-1 cells transiently transfected with cDNA coding for full-length truncated actin (tActin) revealed the efficient incorporation of [(3)H]myristic acid into this molecule.

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