Synergistic effect of estrogen and androgen on induction of uterine thymidine kinase activities in immature rats

Estrdiol-17β induced a significant increase in the uterine thymidine kinase activity with a characteristic isozyme pattern 30 h after injection into immature rats. Testosterone propionate also revealed a similar increase. Following combined injection of estradiol-17β and testosterone propionate, the overall and separate isozyme activities of thymidine kinase increased to nearly the total amount of those when each hormone was injected separately.     

Search for translation arrest peptides encoded upstream of genes for components of protein localization pathways

Regulatory nascent peptides participate in the regulation of cellular functions by the mechanisms involving regulated translation arrest. A class of them in bacteria, called monitoring substrates, feedback-regulates the expression of a specific component of protein localization machinery. Three monitoring substrates, SecM, MifM and VemP have previously been identified. Here, we attempt at identifying additional arrest peptides in bacteria. Our bioinformatic searches over more than 400 bacterial genomic sequences for proteins that have the common characteristic features shared by the known monitoring substrates and subsequent in vitro and in vivo characterization of the highlighted sequences allowed the identification of three arrest peptides termed ApcA, ApdA and ApdP. ApcA and ApdA homologs are conserved among a subset of actinobacteria, whereas ApdP has homologs in a subset of α-proteobacteria. We demonstrate that these arrest peptides, in their ribosome-tethered nascent states, inhibit peptidyl transfer. The elongation arrest occurs at a specific codon near the 3′ end of the coding region, in a manner depending on the amino acid sequence of the nascent chain. Interestingly, the arrest sequences of ApcA, ApdA and ApdP share a sequence R-A-P-G/P that is essential for the elongation arrest.     

Antifouling Brominated Diterpenoids from Japanese Marine Red Alga Laurencia venusta Yamada

The marine red algal genus Laurencia has abundant halogenated secondary metabolites, which exhibit novel structural types and possess various unique biological potentials, including antifouling activity. In this study, we report the isolation, structure elucidation, and antifouling activities of two novel brominated diterpenoids, aplysin-20 aldehyde ( 1 ), 13-dehydroxyisoaplysin-20 ( 2 ), and its congeners. We screened marine red alga Laurencia venusta Yamada for their antifouling activity against the mussel Mytilus galloprovincialis. Ethyl acetate extracts of L. venusta from Hiroshima and Chiba, Japan, were isolated and purified, and the compound structures were identified using 1D and 2D NMR, HR-APCI-MS, IR, and chemical synthesis. Seven secondary metabolites were identified, and their antifouling activities were evaluated. Compounds 1 , 2 , and aplysin-20 ( 3 ) exhibited strong activities against M. galloprovincialis. Therefore, these compounds can be explored as natural antifouling drugs.     

Targeting of Chrolamphenicol Acetyltransferase to Human Immunodeficiency Virus Particles via Vpr and Vpx

Vpr and Vpx are the auxiliary proteins of human immunodeficiency viruses (HIVs) selectively incorporated into mature viral particles. We showed that the bacterial chloramphenicol acetyltransferase (CAT) fused to the N-terminus of HIV-1 Vpr, HIV-2 Vpr, or HIV-2 Vpx was incorporated into mature virions in a type-selective manner. By using chimeric proteins between HIV-1 Vpr and HIV-2 Vpx, we found that the N-terminal side of these proteins was mainly important for type-selective virion incorporation. The C-terminal arginine-rich region of HIV-1 Vpr was also found to transport CAT fusion proteins into virions but without any type selectivity. Furthermore, the corresponding regions of HIV-2 Vpr and HIV-2 Vpx had no such activity. This region of HIV-1 Vpr may interact nonspecifically with viral genomic RNA. Collectively, Vpr and Vpx may provide a means to introduce foreign proteins and other molecules into HIV virions for therapeutic purposes.