Publications by authors named "Naohiko Yokota"
Abi-1 is an adaptor protein for Abelson kinase (c-Abl), and Abi-1 promotes the Abl-mediated phosphorylation of Mammalian Enabled (Mena) by binding both c-Abl and Mena. Here, we identified a new phosphorylation site (Y398) in the SH3 domain of Abi-1, and disruption of Y398, combined with the previously identified phosphorylation site Y213, significantly weakens the binding of Abi-1 to c-Abl. The SH3 domain of Abi-1 and the proline-rich domain of c-Abl are involved in this interaction.
View Article and Find Full Text PDFWe performed mass spectrometric imaging (MSI) to localize ginsenosides (Rb(1), Rb(2) or Rc, and Rf) in cross-sections of the Panax ginseng root at a resolution of 100 microm using matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS). Tandem mass spectrometry (MS/MS) of alkali metal-adducted ginsenoside ions revealed structural information of the corresponding saccharides and aglycone. MALDI-MSI confirmed that ginsenosides were located more in the cortex and the periderm than that in the medulla of a lateral root.
View Article and Find Full Text PDFReactive oxygen species (ROS) are implicated in plant innate immunity. NADPH oxidase (RBOH; for Respiratory Burst Oxidase Homolog) plays a central role in the oxidative burst, and EF-hand motifs in the N terminus of this protein suggest possible regulation by Ca(2+). However, regulatory mechanisms are largely unknown.
View Article and Find Full Text PDFArticle Synopsis
- Brassica self-incompatibility is regulated by the S-locus, which encodes proteins like SRK, SP11, and SLG that participate in recognizing self and nonself pollen grains.
- SP11 on pollen determines its S-haplotype, while SRK on stigma cells determines the stigma's S-haplotype specificity; their interaction is crucial for successful fertilization.
- Research shows a 60-kD protein on the stigma is a truncated form of SRK that also binds to SP11, indicating the importance of the membrane-anchored SRK in pollen recognition and specificity.
Article Synopsis
- A study explored a method to control the proofreading and polymerase activities of archaeal DNA polymerases, focusing on the family B DNA polymerase from Thermococcus kodakaraensis KOD1.
- Mutating a "unique loop" in the exonuclease domain resulted in significant changes in 3'-5' exonuclease activity among various H147 mutants, ranging from 9% to 276% compared to the wild-type enzyme.
- The crystal structure analysis of the H147E mutant revealed it maintains good PCR performance and fidelity, indicating that interactions between the unique loop and Thumb domain play a crucial role in shaping the enzyme's properties.