Nucleotide sequences of serine tRNAs from Bacillus subtilis.

Three B. subitilis serine tRNAs were sequenced including modified nucleosides. All the serine tRNAs contained 1-methyl-adenosine in the D-loop. As other characteristic modified nucleosides, 5-methoxyuridine was found in the first letter of the anticodon in the tRNA(UGA).     

Biosynthesis of Xyloglucan in Suspension-Cultured Soybean Cells. Synthesis of Xyloglucan from UDP-Glucose and UDP-Xylose in the Cell-Free System

When UDP-[¹⁴C]glucose or UDP-[¹⁴C]xylose was incubated witha particulate fraction from soybean cells, radioactive polymerswere synthesized. On digestion with Aspergillus oryzae enzymes,these polymers gave ¹⁴C-monosaccharides and a ¹⁴C-disaccharidewith chromatographic and electrophoretic mobilities indistinguishablefrom those of authentic isoprimeverose (6-O--D-xylopyranosyl-D-glucopyranose).The disaccharide consisted of xylose and glucose, and the latterwas located at the reducing end. Evidence that the disaccharideis isoprimeverose was provided by methylation analysis. Hydrolysisof the methylated disaccharide yielded 2,3,4-tri-O-methyl-D-xyloseand 2,3,4-tri-O-methyl-D-glucose. Thus, incorporation of radioactivityinto isoprimeverose, the smallest structural unit of xyloglucan,suggests that xyloglucan is synthesized in vitro from UDP-glucoseand UDP-xylose. (Received November 20, 1980; Accepted February 14, 1981)     

Biosynthesis of Xyloglucan in Suspension-cultured Soybean Cells. Evidence that the Enzyme System of Xyloglucan Synthesis does not Contain {beta}-1,4-Glucan 4-{beta}-D-Glucosyltransferase Activity (EC 2.4.1.12)

Xyloglucan 4-ß-D-glucosyltransferase, an enzyme responsiblefor the formation of the xyloglucan backbone, in a particulatepreparation of soybean cells has been compared with ß-1,4-glucan4-ß-D-glucosyltransferase of the same origin. Thefollowing observations indicate that the enzyme system of xyloglucansynthesis does not contain ß-1,4-glucan 4-ß-D-glucosyltransferaseactivity, although both enzymes transfer the glucosyl residuefrom UDP-glucose to form the ß-1,4-glucosidic linkage:1. The incorporation of [¹⁴C]glucose into xyloglucan dependedon the presence of UDP-xylose in the incubation mixture. 2.No measurable amount of radioactivity was incorporated fromUDP-[¹⁴C]xylose into the cello-oligosaccharides, although theincorporation of [¹⁴C]xylose into xyloglucan depended on thepresence of UDP-glucose in the incubation mixture (Hayashi andMatsuda 1981b). 3. The activity of xyloglucan 4-ß-D-glucosyltransferasewas stimulated more strongly by Mn²⁺ than by Mg²⁺, whereas Mg²⁺was the most active stimulator for the activity of ß-1,4-glucan4-ß-D-glucosyltransferase. 4. An addition of GDP-glucose(100 µM) to the incubation mixture inhibited the activityof xyloglucan 4-ß-D-glucosyltransferase by 17%, whereasthe activity of ß-1,4-glucan 4-ß-D-glucosyltransferasewas inhibited 56% under the same conditions. 5. Irpex exo-cellulasedid not hydrolyze the xyloglucan synthesized in vitro. 6. Theß-1,4-glucan synthesized in vitro was not a branchedxyloglucan because it gave no 2,3-di-O-methyl glucose derivativeon methylation analysis. 7. Pulse-chase experiments indicatedthat the ß-1,4-glucan was not transformed into thexyloglucan. The subcellular distribution of the xyloglucan synthase, however,was similar to that of the ß-1,4-glucan synthase (Golgi-located1,4-ß-D-glucan 4-ß-D-glucosyltransferase).Thus, it appears that the latter enzyme is located at a siteclose to xyloglucan synthase and is set aside for the assemblyof these polysaccharides into the plant cell surface. (Received May 21, 1981; Accepted October 13, 1981)     

Degradation of Xyloglucan by Wall-bound Enzymes from Soybean Tissue I. Occurrence of Xyloglucan-degrading Enzymes in Soybean Cell Wall

An enzyme preparation that catalyzes the degradation of xyloglucanwas obtained by extraction of the cell walls of soybean hypocotylswith a buffer containing 1.0 M NaCl. The enzyme preparationwas shown to catalyze two-step degradation of xyloglucan. Thepolysaccharide was first degraded into comparatively large fragments,which were then further degraded into monosaccharides. In orderto elucidate the mode of degradation of the xyloglucan duringcell growth, the activities of xyloglucandegrading enzymes ofsoybean-hypocotyl segments were assayed at different stagesof elongation. The total activities of the degrading enzymeswere lower in the elongating regions than in the non-elongatingregions. However, high levels of endo-ß-l,4-glucanasewere found in the elongating regions. These results suggestthat xyloglucan is hydrolyzed by endo-ß-1,4-glucanaseinto comparatively large fragments at the initial stage of growthand the resulting fragments are further degraded into monosaccharidesduring cell elongation. (Received May 20, 1981; Accepted August 8, 1981)     

An unusual fluorescence spectrum of a protein proteinase inhibitor, Streptomyces subtilisin inhibitor.

Streptomyces subtilisin inhibitor, a dimeric protein proteinase inhibitor isolated in crystalline form by Murae et al. in 1972, contains three tyrosine and one tryptophan residues per monomer unit and has unusual fluorescence properties. When excited at 280 nm, it shows a characteristic fluorescence spectrum having a peak at 307 nm and a shoulder near 340 nm, a feature which has been recognized only for a very few cases in proteins containing both tryosine and tryptophan residues. When excited at 295 nm, at which tryrosine scarcely absorbs, the inhibitor shows an emission spectrum with a peak at 340 nm characteristic of a tryptophan residue. The emission with a peak at 307 nm is considered to arise from the tryrosine residues. The tryptophan quantum yield of Streptomyces subtilisin inhibitor excited at 295 nm is very small, indicating that the tryptophan florescence is strongly quenched in the native state of the inhibitor. Below pH 4 the peak of the fluorescence spectrum of the inhibitor excited at 280 nm shifts toward 340-350 nm with a concomitant increase in the quantum yield. The structural change induced by low pH seems to release the tryptophan fluorescence from the quenching.     

A Geometry-Based Multiple Testing Correction for Contingency Tables by Truncated Normal Distribution

Statistics in Biosciences - Inference procedure is a critical step of experimental researches to draw scientific conclusions especially in multiple testing. The false positive rate increases unless...     

Intrapopulation genetic variation in the level and rhythm of daily activity in Drosophila immigrans

Genetic diversity within a population, such as polymorphisms and personality, is considered to improve population performance because such intraspecific variations have the potential to alleviate the competition for a limited resource or the risk of predation and sexual harassment at a population level. Variation in the level and rhythm of daily activity in a population could also affect population performance by directly altering ecological, social, and sexual interactions among individuals. However, it remains to be elucidated whether such intra‐population variation in the level and rhythms of daily activity exists in a natural population. Here, we investigated the genetic variation in daily activity within a single natural population of Drosophila immigrans. We established 21 isofemale lines from a single natural population and measured larval activity level and the level and daily pattern of adult activity over a 24 hr period. Larval activity level significantly varied among isofemale lines. Likewise, the activity level in the adult stage significantly varied among lines. The significant variation was also found in the daily pattern of adult activity; some lines showed greater activity level in the daytime, and others showed greater activity level in the night. Our results consistently suggest that there is a genetic variation in behavioral activity in a natural population, probably contributing to shaping the population performance.