Takashi Morii

Fluorescent biosensors to detect the bona fide events of biologically important molecules in living cells are increasingly demanded in the field of molecular cell biology. Recent advances in the development of fluorescent biosensors have made an outstanding contribution to elucidating not only the roles of individual biomolecules, but also the dynamic intracellular relationships between these molecules. However, rational design strategies of fluorescent biosensors are not as mature as they look.

ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSequence-specific DNA binding by a geometrically constrained peptide dimerTakashi Morii, Masatoshi Simomura, Shinji Morimoto, and Isao SaitoCite this: J. Am. Chem. Soc. 1993, 115, 3, 1150–1151Publication Date (Print):February 1, 1993Publication History Published online1 May 2002Published inissue 1 February 1993https://pubs.acs.org/doi/10.1021/ja00056a050https://doi.org/10.1021/ja00056a050research-articleACS PublicationsRequest reuse permissionsArticle

An intracellular second messenger d-myo-inositol-1,4,5-trisphosphate (IP3) is a key biological signaling molecule that controls the cellular Ca2+ concentration. We report the preparation and evaluation of a functionalized protein-based sensor for IP3 by exploring the selective IP3 binding properties of pleckstrin homology (PH) domain. Signal transduction is imparted to the protein by mutation of proximal residues to cysteine and then alkylation of the active site by various fluorophore derivativ

Peptide dimers of the basic leucine zipper protein with non-native monomer arrangements were synthesized by using C2 chiral templates as a synthetic dimerization module. The amino acid sequence of the peptide is derived from the DNA contact region of the basic leucine zipper protein GCN4. These peptide dimers are designed to possess different geometrical constraints from that of native GCN4 with respect to the orientation of two DNA-contacting peptides. Peptide dimers constrained at the 6th posi

In native systems, scaffolding proteins play important roles in assembling proteins into complexes to transduce signals. This concept is yet to be applied to the assembly of functional transmembrane protein complexes in artificial systems. To address this issue, DNA origami has the potential to serve as scaffolds that arrange proteins at specific positions in complexes. Herein, we report that Kir3 K⁺ channel proteins are assembled through zinc-finger protein (ZFP)-adaptors at specific

DNA is an attractive molecular building block to construct nanoscale structures for a variety of applications. In addition to their structure and function, modification the DNA nanostructures by other molecules opens almost unlimited possibilities for producing functional DNA-based architectures. Among the molecules to functionalize DNA nanostructures, proteins are one of the most attractive candidates due to their vast functional variations. DNA nanostructures loaded with various types of prote

A recently described three-dimensional structure of the ribosome provides a sense of remarkable diversity of RNA-protein complexes. We have designed a new class of scaffold for artificial receptors, in which a short peptide and RNA with a randomized nucleotide region form a stable and specific complex. The randomized nucleotide region was placed next to the HIV-1 Rev response element to enable the formation of "ribonucleopeptide" pools in the presence of the Rev peptide. In vitro selection of RN

A series of short peptides derived from the basic region of the basic leucine zipper protein GCN4 were synthesized to study the cooperative DNA binding to direct repeat sequences. A modified lysine residue bearing an adamantyl group at the ε-amino group was incorporated at the N-terminal position, and β-cyclodextrin was attached at the C-terminal cysteine residue of the parent basic region peptide. The resulting peptide G2AdCd possesses both host and guest molecules in the same peptide chain. DN