The mitogen-activated protein kinase kinase kinase 3 (MEKK3) is a member of the MAP kinase family whose cellular activity is elevated in response to growth factors, oxidative stress, and hyperosmolar conditions. MEKK3 regulates MKK3 and MKK5/6/7. MEKK3 is involved distinctively in the signal pathway for blocking cell proliferation and cell cycle progression, contradictory to the biological responses commonly associated with other members of MEKKs. Based information concerning the substrate specificity of serum- and glucocorticoid-induced kinase 1 (SGK1), R-x-R-x-x-(S/T)-phi, where phi indicates a hydrophobic amino acid, two putative phosphorylation sites (Ser(166) and Ser(337)) were found in MEKK3. It was shown that the recombinant MEKK3 protein and fluorescein-labeled MEKK3 peptides (FITC-(159)epRsRhlSVi(168) and FITC-(330)dpRgRlpSAd(339)) are phosphorylated by SGK1 in vitro. It was also observed that the intrinsic kinase activity of MEKK3 on Ser(189) of MKK3 (equivalent to Ser(207) of MKK6) decreased along with phosphorylation of Ser(166) and Ser(337) in MEKK3 in vitro and in vivo. Therefore, it is suggested that SGK1 inhibits MEKK3-MKK3/6 signal transduction by phosphorylation of MEKK3.

A novel active-matrix organic light-emitting-diode (AMOLED) display employing a new current-mirror pixel circuit, which requires four-poly-Si TFTs and one-capacitor and no additional signal lines, has been proposed and sucessfully fabricated. The experimental results show that a new current mirror can considerably compensate luminance non-uniformity and scale down a data current more than a conventional current-mirror circuit in order to reduce the pixel charging time and increase the minimum data current. Compared with a conventional two-TFT pixel, the luminance non-uniformity induced by the grain boundaries of poly-Si TFTs can be decreased considerably from 41% to 9.1%. FIGURE 1 -The serial-current-mirror pixel circuit and timing diagram, T3 and T4, are paired by a serial-mirror type.

e Here, we present the high-quality draft genome sequence of the agar-degrading marine gammaproteobacterium Alteromonadaceae sp. strain G7, which was isolated from coastal seawater to be utilized as a bioresource for production of agar-derived biofuels. The 3.91-Mb genome contains a number of genes encoding algal polysaccharide-degrading enzymes such as agarases and sulfatases.

An agar-degrading bacterium, designated as strain G7(T), was isolated from a coastal seawater sample from Gaya Island (Gayado in Korean), Republic of Korea. The isolated strain G7(T) is gram-negative, rod shaped, aerobic, non-motile, and non-pigmented. A similarity search based on its 16S rRNA gene sequence revealed that it shares 95.5%, 90.6%, and 90.0% similarity with the 16S rRNA gene sequences of Catenovulum agarivorans YM01(T), Algicola sagamiensis, and Bowmanella pacifica W3-3A(T), respectively. Phylogenetic analyses demonstrated that strain G7(T) formed a distinct monophyletic clade closely related to species of the family Alteromonadaceae in the Alteromonas-like Gammaproteobacteria. The G+C content of strain G7(T) was 41.12 mol%. The DNA-DNA hybridization value between strain G7(T) and the phylogenetically closest strain YM01(T) was 19.63%. The genomes of G7(T) and YM01(T) had an average ANIb value of 70.00%. The predominant isoprenoid quinone of this particular strain was ubiquinone-8, whereas that of C. agarivorans YM01(T) was menaquinone-7. The major fatty acids of strain G7(T) were Iso-C15:0(41.47%), Anteiso-C15:0(22.99%), and C16:1ω7c/iso-C15:02-OH (8.85%), which were quite different from those of YM01(T). Comparison of the phenotypic characteristics related to carbon utilization, enzyme production, and susceptibility to antibiotics also demonstrated that strain G7(T) is distinct from C. agarivorans YM01T. Based on its phenotypic, chemotaxonomic, and phylogenetic distinctiveness, strain G7(T) was considered a novel genus and species in the Gammaproteobacteria, for which the name Gayadomonas joobiniege gen. nov. sp. nov. (ATCC BAA-2321 = DSM25250(T) = KCTC23721(T)) is proposed.

DagA, a β-agarase, was produced by cultivating a recombinant Streptomyces lividans in a glucose medium or a mixed-sugar medium simulating microalgae hydrolysate. The optimum composition of the glucose medium was identified as 25 g/l glucose, 10 g/l yeast extract, and 5 g/l MgCl2·6H2O. With this, a DagA activity of 7.26 U/ml could be obtained. When a mixedsugar medium containing 25 g/l of sugars was used, a DagA activity of 4.81 U/ml was obtained with very low substrate utilization efficiency owing to the catabolic repression of glucose against the other sugars. When glucose and galactose were removed from the medium, an unexpectedly high DagA activity of about 8.7 U/ml was obtained, even though a smaller amount of sugars was used. It is recommended for better substrate utilization and process economics that glucose and galactose be eliminated from the medium, by being consumed by some other useful applications, before the production of DagA.