Chemical stability and aggregation activity of assembly pheromone of argasid ticks and its synthetic purine analogues were studied during long-lasting storage at room temperature as the potential components of attractant/acaricide mixtures. Guanine spherules from dry excreta of Omithodoros moubata Murray, 1877 were very stable in their chemical composition and did not suffer from purine degradation. However, an intensive purine conversion into uric acid occurred in samples of the fluid of the excreta of Argas persicus (Oken, 1818) and to a lesser extent also in an artificial mixture of synthetic guanine, xanthine and hypoxanthine in saline. The presence of bacteria Bacillus sp. and the moulds Talaromyces flavus (syn. Pénicillium dangeardii) and Aspergillus carbonarius, isolated from some samples, might explain the enzymic degradation of purines. The suspension of guanine hydrochloride in saline or in saline with ethanol (1 : 1 v/v) as a potential acaricide solvent, and with diatomaceous earth as the pheromone carrier, was very stable and no guanine degradation occurred. This proved to be suitable for potential use mixed with acaricides for tick control. The assembly of A. persicus males, on most of the substrates tested, was very high up to day 77 of experiment but decreased significantly on day 114-119 in samples of synthetic analogue of assembly pheromone variant 1 in which the absolute amount of guanine in solutions strongly decreased or disappeared completely.
Many RNA recognition motif (RRM)-containing proteins are known to exist in chloroplasts. Major members of the RRM protein family, which are chloroplast ribonucleoproteins (cpRNPs), have been investigated in seed plants, including tobacco and Arabidopsis thaliana, but never in early land plants, such as bryophytes. In this study, we surveyed RRM proteins encoded in the moss Physcomitrella patens genome and predicted 25 putative chloroplast RRM proteins. Among them, two RRM-containing proteins, PpRBP2a and PpRBP2b, resembled cpRNPs and were thus referred to as cpRNP-like proteins. However, knockout mutants of either one or two PpRBP2 genes exhibited a wild type-like phenotype. Unlike Arabidopsis cpRNPs, the levels of mRNA accumulation in chloroplasts were not affected in the PpRBP2 knockout mutants. In addition, the efficiency of RNA editing was also not altered in the mutants. This suggests that PpRBP2a and 2b may be functionally distinct from Arabidopsis cpRNPs., H. Uchiyama, M. Ichinose, M. Sugita., and Obsahuje bibliografické odkazy