All line up together! A new concept for the alignment and assembly of conjugated polymers through the action of supramolecular bundling (“aligner”) molecules is inspired by actin‐filament bundling proteins. The approach provides a general means of preparing complex, ordered assemblies of conjugated polymers.

We have found that s-SPG and curdlan are capable of wrapping SWNTs and the “periodical” helical structure is created, reflecting the helical nature of the SPG main-chain, on the SWNTs surface. The novel SWNTs/β-1,3-glucan composites were characterized by TEM and AFM, which consistently support the view that these β-1,3-glucans wrap SWNTs, creating a helical higher-order structure.

The obligate intracellular parasitic bacteria rickettsiae are more closely related to mitochondria than any other microbes investigated to date. A rickettsial putative peptidase (RPP) was found to resemble the ␣ and ␤ subunits of mitochondrial processing peptidase (MPP), which cleaves the transport signal sequences of mitochondrial preproteins. RPP showed completely conserved zinc-binding and catalytic residues compared with ␤-MPP but barely contained any of the glycine-rich loop region characteristic of ␣-MPP. When the biochemical activity of RPP purified from a recombinant source was analyzed, RPP specifically hydrolyzed basic peptides and presequence peptides with frequent cleavage at their MPP-processing sites. Moreover, RPP appeared to activate yeast ␤-MPP so that it processed preproteins with shorter presequences. Thus, RPP behaves as a bifunctional protein that could act as a basic peptide peptidase and a somewhat regulatory protein for other protein activities in rickettsiae. These are the first biological and enzymological studies to report that a protein from a parasitic microorganism can cleave the signal sequences of proteins targeted to mitochondria.The endosymbiont hypothesis for the origin of mitochondria in eukaryotes is now widely accepted, accompanied by a growing interest in evolution as entire genomic sequences are revealed from various organisms. According to this hypothesis, a free-living bacterium as an organelle progenitor once entered an anaerobic organism, which is thought to be an archaebacterial ancestor, and established a constitutive endosymbiotic relationship with the host cells, mainly to supply ATP (7,11,17). Modern mitochondria originated when the parasitic invader lost most of its own genome and began to depend on nuclearly encoded proteins for its biogenesis, although it retained control of the eukaryotic cell viability via metabolic and apoptotic pathways.Most mitochondrial proteins are encoded in the nucleus and synthesized by cytoplasmic ribosomes as preproteins with Nterminal presequences that are required for targeting to mitochondria (3, 12). These preproteins are unfolded and imported into the mitochondrial matrix across the double membrane through protein translocation machinery comprising a translocase on the outer mitochondrial membrane and a translocase on the inner mitochondrial membrane (20,24,26,27). Finally, the presequences are cleaved by a matrix-located metalloendopeptidase, i.e., mitochondrial processing peptidase (MPP) (10, 13, 16). Overall, this proteolytic processing is involved in maturation of the mitochondrial proteins and is essential for eukaryotic cell viability from unicellular (30) to multicellular (22) organisms. Therefore, the ␣ and ␤ subunits of MPP (␣-and ␤-MPP, respectively) tightly regulate the protease action and specifically cleave the preproteins.The genome sequences of the obligate intracellular parasitic bacteria rickettsiae (the agents that cause typhus) reveal gene profiles strikingly similar to those of mitochondria (2,18,23). Among ...

In Reihe aufstellen! Ein neues Konzept für das Ausrichten und Organisieren konjugierter Polymere durch die Wirkung supramolekularer bündelnder Moleküle („Ausrichtermoleküle“) wird vorgestellt, das von Actinfilamente bündelnden Proteinen inspiriert ist. Der Ansatz bietet einen allgemeinen Zugang zum Aufbau komplexer, geordneter Ensembles konjugierter Polymere.

Synthetische bündelnde Moleküle überführen in Lösung konjugierte Polymere in geordnete supramolekulare Ensembles. Der Ansatz ist inspiriert durch Actinfilamente bündelnde Proteine. In der Zuschrift auf S. 1578 ff. schildern M. Takeuchi, S. Shinkai et al., wie die Verwendung dieser “Ausrichtermoleküle” herkömmliche Techniken ergänzt und eine neue Möglichkeit bietet, komplexe, definiert angeordnete Ensembles konjugierter Polymere zu erzeugen, wie sie im Titelbild gezeigt sind.