Mediator structure and conformation change

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Genome Sequence and Comparative Genomics Analysis of a Vibrio cholerae O1 Strain Isolated from a Cholera Patient in Malaysia

The genome sequence analysis of a clinical Vibrio cholerae VC35 strain from an outbreak case in Malaysia indicates multiple genes involved in host adaptation and a novel Na⁺-driven multidrug efflux pump-coding gene in the genome of Vibrio cholerae with the highest similarity to VMA_001754 of Vibrio mimicus VMA223.     

Cytological and mapping analysis of a novel male sterile type resulting from spontaneous floral organ homeotic conversion in marigold (<Emphasis Type="Italic">Tagetes erecta</Emphasis> L.)

A male sterile line was isolated in marigold (Tagetes erecta L.) and cytological analysis determined this to be a novel genic male sterility trait (Tems). Through the use of amplified fragment length polymorphisms (AFLPs) and bulked segregant analysis (BSA), tightly linked markers of Tems were identified with a view towards a map-based cloning strategy. It was found that spontaneous homeotic conversion of floral organs was the underlying cause of the male sterility in this marigold line. Thus, petals of male sterile plants resembled sepal-like structures and the stamens were partially converted to styles, although without the full characteristics or function of the true style organs. We have constructed a fine marker-based map for the Tems gene. This is intended to provide a tool for marker assisted selection (MAS) strategies in hybrid breeding and map-based cloning strategies for the male sterility locus. We discuss the significance of this spontaneously derived genic male sterility trait relating to the homeotic conversion of floral organs in marigold.     

A NEW RHEOCRICOTOPUS THIENEMANN & HARNISCHIA (DIPTERA: CHIRONOMIDAE) FROM TAIWAN PROVINCE CHINA

Abstract  Rheocricotopus (Psilocricotopus) taiwanensis sp. n. from Taiwan, China, is described as male imagines. The species is allied to R. (P.) chalybeatus (Edwards) but it is easily separated from the latter in lacking setae in all reins, much lower AR and more pronounced crista dorsalis in gonostylus. The genus is new to Taiwan Province, China. The specimen is deposited at the Department of Biology, Nankai University, Tianjin.     

A cytogenetic characterization comparing a rat 6TG-resistant strain and 6TG-sensitive clones

Summary A 8.3 /ml 6-thioguanine (6TG)-resistant strain was isolated from a rat tetraploid cell line by step-by-step selection in 6TG-medium. In the 6TG-resistant cell population 51% of the cells were tetraploid and 35% of the cells were hypertetraploid, i.e., one chromosome more than a tetraploid. The 6TG-resistant strain grew very well in RPMI 1640 medium with intervals of three days between subcultures. The 6TG-resistant cells all have a homogeneously staining region (HSRs) in one of the X chromosomes which do not stain after chromosome C-banding. They also possess a higher NORs activity and much lower frequency of sister chromatid exchanges (SCE). When the 6TG-resistant RCT cells were subcultured in 6TG-free medium for three days, their SCE frequency did not change. 5-bromodeoxyuridine (BrdU) significantly suppressed the NORs activity for both 6TG-resistant cells and 6TG-sensitive cells (P<0.001).Abbreviations 6TG 6-thioguanine - HSRs homogeneously staining region - NORs nucleolar organizer region - SCE sister chromatid exchange - BrdU 5-bromodeoxyuridine - HPRT Hypoxanthine phosphoribosyl transferase     

Purification and Characterization of a Substrate-Size-Recognizing Metalloendopeptidase from Streptococcus cremoris H61

During the ripening of Gouda-type cheese, two kinds of endopeptidases were found to participate in the degradation of αs1-CN(f1-23), a specific product from αs1-casein hydrolyzed by chymosin. One of the endopeptidases, lactic acid bacteria endopeptidase (LEP-II), which can recognize the size of its substrates, has already been purified and characterized (T. R. Yan, N. Azuma, S. Kaminogawa, and K. Yamauchi, Eur. J. Biochem. 163:259-265, 1987). The other endopeptidase, LEP-I, was purified to homogeneity by conventional chromatographic techniques from Streptococcus cremoris H61. The enzyme appeared to be monomeric, with an apparent molecular weight of 98,000, and its isoelectric point was 5.1. For the hydrolysis of αs1-CN(f1-23), the enzyme had an optimum pH and temperature of 7.0 to 7.5 and 40°C, respectively. Its activity was inhibited by such chelating agents as EDTA and 1,10-phenanthrolin, and it could be fully reactivated by Mn²⁺. Inhibitors specific for serine and thiol proteases had no effect on the protease activity. The enzyme showed a high affinity toward the Glu-Asn peptide bond of αs1-CN(f1-23) and αs1-CN(f91-100) but showed no hydrolysis activity toward αs1-CN(f1-52), αs1-CN(61-122), αs1-CN(136-196), αs1-casein, β-casein, κ-casein, α-lactalbumin, and β-lactoglobulin. The K_m and V_max of LEP-I for αs1-CN(f1-23) were 14.2 pM and 139 U, respectively.