The Lotus japonicus nucleoporin GLE1 is involved in symbiotic association with rhizobia.

Nucleoporins are components of the nuclear pore complexes, channels that regulate the transport of macromolecules between the nucleus and cytoplasm. The nucleoporin GLE1 (GLFG lethal1) functions in the export of messenger RNAs containing poly(A) tails from the nucleus into the cytoplasm. Here we investigated a mutant of the model legume Lotus japonicus that was defective in GLE1, which we designated Ljgle1. The growth of Ljgle1 was retarded under symbiotic association with rhizobia, and the nitrogen-fixation activities of the nodules were around one-third of those in the wild-type plant. The growth of Ljgle1 was not substantialy recovered by supplemention of combined nitrogen. Nodules formed on the Ljgle1 were smaller than those on the wild-type and colored faint pink. The numbers of infected cells of nodules on the Ljgle1 were smaller than on the wild-type plant, and the former cells remained undeveloped. Rhizobia in the cells of the Ljgle1 exhibited disordered forms, and the symbiosome membrane was closely attached to the bacterial membrane. These results indicate that GLE1 plays a distinct role in the symbiotic association between legumes and rhizobia.

[A case of tuberculous peritonitis in a hemodialysis patient revealed by severe diarrhea and stomachache].

A 53-year-old woman was admitted to our hospital due to abdominal pain, diarrhea, and shunt occlusion caused by dehydration. She had undergone hemodialysis due to diabetic nephropathy over a ten-year period. She was hospitalized again with fever and a persistent high serum CRP level. We started antibiotic administration using cefotiam hexetil hydrochloride because of ascites and peritoneum thickening observed by abdominal computed tomography. Although her symptoms, such as abdominal pain and diarrhea, improved after the administration of antibiotics, the ascites and the peritoneum thickening did not improve. On the fourth hospital day, we attempted ascites aspiration to investigate the etiology of the peritonitis. Cytological examination suggested tuberculous peritonitis because of predominant macrophage cell proliferation, a high level of ADA concentration, and a high level of CA125 of ascites. Although QuantiFERON-tuberculosis (QFT) and the Gaffky scale were negative, we started multidrug therapy (isoniazid + rifampicin + pyrazinamide + ethambutol) on the 20th hospital day. She was finally diagnosed as mycobacterium tuberculous peritonitis based on biopsy of the tissue of the ileum and the results of colonoscopy. Administration of antituberculosis chemotherapy improved abdominal fullness and ascites and the patient was discharged on the 97th hospital day. Moreover Kuno et al. reported that serum soluble interleukin-2 receptor(sIL-2R) and CA-125 levels can be used to monitor the response to anti-tuberculosis treatment. In this case, we use these markers to monitor the response to treatment. We experienced a case of tuberculous peritonitis undergoing hemodialysis. Tuberculosis should be suspected when patients undergoing dialysis have long-term fever of unknown etiology. There are many reports stating that the sensitivity and specificity of QuantiFERON-tuberculosis (QFT) and sputum culture are low in latent tuberculosis infection of dialysis patients. Accordingly it is necessary to diagnose mycobacterium tuberculous peritonitis comprehensively by the clinical symptoms and image analysis.

Modulation of cellulase activity by charged lipid bilayers with different acyl chain properties for efficient hydrolysis of ionic liquid-pretreated cellulose.

The stability of cellulase activity in the presence of ionic liquids (ILs) is critical for the enzymatic hydrolysis of insoluble cellulose pretreated with ILs. In this work, cellulase was incorporated in the liposomes composed of negatively charged 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (POPG) and zwitterionic phosphatidylcholines (PCs) with different length and degree of unsaturation of the acyl chains. The liposomal cellulase-catalyzed reaction was performed at 45°C in the acetate buffer solution (pH 4.8) with 2.0g/L CC31 as cellulosic substrate. The crystallinity of CC31 was reduced by treating with 1-butyl-3-methylimidazolium chloride ([Bmim]Cl) at 120°C for 30min. The liposomal cellulase continuously catalyzed hydrolysis of the pretreated CC31 for 48h producing glucose in the presence of 15wt% [Bmim]Cl. The charged lipid membranes were interactive with [Bmim](+), as elucidated by the [Bmim]Cl-induced alterations in fluorescence polarization of the membrane-embedded 1,6-diphenyl-1,3,5-hexatriene (DPH) molecules. The charged membranes offered the microenvironment where inhibitory effects of [Bmim]Cl on the cellulase activity was relieved. The maximum glucose productivity GP of 10.8 mmol-glucose/(hmol-lipid) was obtained at the reaction time of 48h with the cellulase incorporated in the liposomes ([lipid]=5.0mM) composed of 50mol% POPG and 1,2-dilauroyl-sn-glycero-3-phosohocholine (DLPC) with relatively short and saturated acyl chains.

Gold single-crystal electrode surface modified with self-assembled monolayers for electron tunneling with bilirubin oxidase.

Using Au(111) and Au(100) single-crystal electrodes modified with self-assembled monolayers (SAMs), the direct electron transfer reaction of bilirubin oxidase (BOD) adsorbed onto their surfaces was investigated. The BOD adsorbed onto the Au(111), Au(100) and gold /mica electrodes, and the BOD adsorbed onto Au(111) electrodes modified with C(3)-SO(3)H and C(n)-COOH (n = 2, 5 and 7), showed the electrocatalytic currents of dioxygen reduction based on the direct electron transfer reaction. The BOD adsorbed onto Au(111) electrodes modified with C(6)-NH(2), C(6)-OH and C(5)-CH(3) did not show any electrocatalytic current. Negatively charged electrode surfaces can give a suitable molecular orientation for the direct electron transfer of BOD. The k degrees values evaluated by an analysis of the steady-state voltammogram with a simulated fitting method did not depend on the crystal structure of the gold electrode surface. Using a C(n)-COOH (n = 2, 5, 7) modified Au(111) electrode, the k degrees values decreased with an increasing alkyl chain length of C(n)-COOH. Based on the k degrees values obtained from the C(n)-COOH (n = 2, 5, 7) modified Au(111) electrodes, the electron tunneling distance was evaluated. The average distance between the type 1 Cu site of BOD and the outside of the BOD protein structure was evaluated to be 17 (+/-2) A.