The influence of temperature transfers on subsequent growth of the European peacock butterfly <Emphasis Type="Italic">Inachis io</Emphasis> (Lepidoptera,Nymphalidae)

The study addresses the effects of higher and lower temperatures experienced during the early stages of ontogeny on the parameters of the subsequent growth and development of the butterfly Inachis io. The caterpillars reared at a temperature of 22°С during instars I–III and then transferred to lower temperatures (16, 18, and 20°C) had higher instantaneous growth rates, larger body mass, and shorter duration of instars IV and V than the caterpillars that developed permanently at these lower temperatures. Vice versa, the caterpillars reared at 16°С during instars I–III and transferred to higher temperatures (18, 20, and 22°C) developed and grew slower than the caterpillars reared at these higher temperatures from the beginning. Possible physiological mechanisms underlying the observed phenomena and their ecological consequences are discussed. Our results are compared with the previously published data on fish—another group of ectothermic organisms, on which similar experiments have been carried out.     

Femtosecond Carotenoid to Retinal Energy Transfer in Xanthorhodopsin

Xanthorhodopsin of the extremely halophilic bacterium Salinibacter ruber represents a novel antenna system. It consists of a carbonyl carotenoid, salinixanthin, bound to a retinal protein that serves as a light-driven transmembrane proton pump similar to bacteriorhodopsin of archaea. Here we apply the femtosecond transient absorption technique to reveal the excited-state dynamics of salinixanthin both in solution and in xanthorhodopsin. The results not only disclose extremely fast energy transfer rates and pathways, they also reveal effects of the binding site on the excited-state properties of the carotenoid. We compared the excited-state dynamics of salinixanthin in xanthorhodopsin and in NaBH₄-treated xanthorhodopsin. The NaBH₄ treatment prevents energy transfer without perturbing the carotenoid binding site, and allows observation of changes in salinixanthin excited-state dynamics related to specific binding. The S₁ lifetimes of salinixanthin in untreated and NaBH₄-treated xanthorhodopsin were identical (3 ps), confirming the absence of the S₁-mediated energy transfer. The kinetics of salinixanthin S₂ decay probed in the near-infrared region demonstrated a change of the S₂ lifetime from 66 fs in untreated xanthorhodopsin to 110 fs in the NaBH₄-treated protein. This corresponds to a salinixanthin-retinal energy transfer time of 165 fs and an efficiency of 40%. In addition, binding of salinixanthin to xanthorhodopsin increases the population of the S^∗ state that decays in 6 ps predominantly to the ground state, but a small fraction (<10%) of the S^∗ state generates a triplet state.     

Photoperiod-temperature interaction--a new form of seasonal control of growth and development in insects and in particular carabid beetle, Amara communis (coleoptera: carabidae)

Amara communis larvae are found to develop significantly faster and have higher growth rate at short-day (12 h) as compared to long-day (22 h) photoperiods under all temperatures (16, 18, 20 and 22 degrees C) used. The coefficient of linear regression of larval development rate on temperature was significantly higher at short days than at long days. At that thermal developmental thresholds appeared similar at both photoperiods. Body weight of young beetles reared under different photoperiods was just the same. Thus, the photoperiodic effect does not simply accelerate or retard insect development, but modifies their thermal reaction norm. Under short days larval development becomes faster and more temperature dependent, which ensures the timely completion of the development at the end of summer. The analysis of data from literature allowed us to find photoperiodic modification of thermal requirements for development in 5 insect orders--Orthoptera, Heteroptera, Coleoptera, Lepidoptera, Diptera. Modification may result in significant changes in the slope of the regression line and hence in the sum of degree-days and thermal developmental threshold. Consequently, during summer under the influence of changing day-length the thermal requirements for development in many insects gradually vary, which may have adaptive significance. Thus, the photoperiodic modification of thermal reaction norm acts as a specific form of seasonal control of insect development.     

Removal and Reconstitution of the Carotenoid Antenna of Xanthorhodopsin

Salinixanthin, a C(40)-carotenoid acyl glycoside, serves as a light-harvesting antenna in the retinal-based proton pump xanthorhodopsin of Salinibacter ruber. In the crystallographic structure of this protein, the conjugated chain of salinixanthin is located at the protein-lipid boundary and interacts with residues of helices E and F. Its ring, with a 4-keto group, is rotated relative to the plane of the π-system of the carotenoid polyene chain and immobilized in a binding site near the β-ionone retinal ring. We show here that the carotenoid can be removed by oxidation with ammonium persulfate, with little effect on the other chromophore, retinal. The characteristic CD bands attributed to bound salinixanthin are now absent. The kinetics of the photocycle is only slightly perturbed, showing a 1.5-fold decrease in the overall turnover rate. The carotenoid-free protein can be reconstituted with salinixanthin extracted from the cell membrane of S. ruber. Reconstitution is accompanied by restoration of the characteristic vibronic structure of the absorption spectrum of the antenna carotenoid, its chirality, and the excited-state energy transfer to the retinal. Minor modification of salinixanthin, by reducing the carbonyl C=O double bond in the ring to a C-OH, suppresses its binding to the protein and eliminates the antenna function. This indicates that the presence of the 4-keto group is critical for carotenoid binding and efficient energy transfer.     

Arginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsin.

In wild-type bacteriorhodopsin light-induced proton release occurs before uptake at neutral pH. In contrast, in mutants in which R82 is replaced by a neutral residue (as in R82A and R82Q), only a small fraction of the protons is released before proton uptake at neutral pH; the major fraction is released after uptake. In R82Q the relative amounts of the two types of proton release, "early" (preceding proton uptake) and "late" (following proton uptake), are pH dependent. The main conclusions are that 1) R82 is not the normal light-driven proton release group; early proton release can be observed in the R82Q mutant at higher pH values, suggesting that the proton release group has not been eliminated. 2) R82 affects the pKa of the proton release group both in the unphotolyzed state of the pigment and during the photocycle. In the wild type (in 150 mM salt) the pKa of this group decreases from approximately 9.5 in the unphotolyzed pigment to approximately 5.8 in the M intermediate, leading to early proton release at neutral pH. In the R82 mutants the respective values of pKa of the proton release group in the unphotolyzed pigment and in M are approximately 8 and 7.5 in R82Q (in 1 M salt) and approximately 8 and 6.5 in R82K (in 150 mM KCl). Thus in R82Q the pKa of the proton release group does not decrease enough in the photocycle to allow early proton release from this group at neutral pH. 3) Early proton release in R82Q can be detected as a photocurrent signal that is kinetically distinct from those photocurrents that are due to proton movements from the Schiff base to D85 during M formation and from D96 to the Schiff base during the M-->N transition. 4) In R82Q, at neutral pH, proton uptake from the medium occurs during the formation of O. The proton is released during the O-->bacteriorhodopsin transition, probably from D85 because the normal proton release group cannot deprotonate at this pH. 5) The time constant of early proton release is increased from 85 microseconds in the wild type to 1 ms in R82Q (in 150 mM salt). This can be directly attributed to the increase in the pKa of the proton release group and also explains the uncoupling of proton release from M formation. 6) In the E204Q mutant only late proton release is observed at both neutral and alkaline pH, consistent with the idea that E204 is the proton release group. The proton release is concurrent with the O-->bacteriorhodopsin transition, as in R82Q at neutral pH.     

Alpha interferon interaction with opiate receptors in the rat brain

The preferential interactions of alpha-interferon (alpha-IFN) with delta and mu opiate receptors were studied. alpha-IFN (specific antiviral activity 2 X 10(3) U/mg protein) was shown to inhibit in the competitive manner 3H-naloxone and 3H-D-ala2, D-leu5-enkephalin (3H-DADL) specific binding to opiate receptor subpopulations. alpha-IFN was much more effective in decreasing 3H-DADL than 3H-naloxone binding in opiate receptors: K1 values averaged 160 +/- 30 and 1150 +/- 80 U/ml, respectively. IFN effective concentrations inhibiting 50% of 3H-naloxone opiate receptor binding in the absence or presence of 100 mmol/l NaCl were similar, and the "sodium shift" value was equal to 1. The independence of alpha-IFN activity of the presence of NA+ cations suggests the antagonist character of alpha-IFN interaction with opiate receptors. Thus, alpha-IFN employed appears to be an alpha-selective ligand displaying the in vitro properties of "pure" morphine antagonists.     

Effect ot thyroliberin on rat brain opiate receptors

The ability of thyroliberin to interact with opiate receptors of the rat midbrain and hypothalamus has been studied. It was shown by competitive displacement analysis that thyroliberin did not replace labeled opioid peptides in opiate receptor binding sites when added in vitro at concentrations of up to 10(-5) M. The specific binding of opioid peptides was increased by 10-20% in the presence of 10(-7)-10(-6) M thyroliberin. This effect was, probably, due to the rise in the affinity of high-affinity opiate receptors. At the same time the affinity of low-affinity binding sites was decreased. It is suggested that the antagonistic properties of thyroliberin are mediated by the modulation of the binding characteristics of enkephalin-low-affinity opiate receptors.     

Escherichia coli cells bearing a ribosomal ambiguity mutation in rpsD have a mutator phenotype that correlates with increased mistranslation

Escherichia coli cells bearing certain mutations in rpsD (coding for the 30S ribosomal protein S4) show a ribosomal ambiguity (Ram) phenotype characterized by increased translational error rates. Here we show that spontaneous mutagenesis increases in Ram cells bearing the rpsD14 allele, suggesting that the recently described translational stress-induced mutagenesis pathway is activated in Ram cells.     

Academician E. N. Pavlovskiĭ's parasitology school in the Zoological institute RAS

The first parasitological division in the Zoological Museum was created in 1924 by the initiative of E. N. Pavlovsky and A. A. Schtakelberg and originally had a named "The permanent commission on the study of malaria mosquitoes". In the process of reorganisation of the Zoological Museum into Zoological Institute in 1930, it was modified into the Department of Parasitology with the E. N. Pavlovsky as a head. In 1934-1935, two laboratories were formed within this department: the Laboratory arachno-entomology and Laboratory of parasitic worms. In subsequent history of ZIN, these parasitological laboratories existed at first as subdivisions of the Department of Parasitology and finally the they were reorganised into independent administrative divisions. The study of parasitic and blood-sucking arthropodes is concentrated in the Laboratory of Parasitology (the head Yu. S. Balashov). A creation of the most important concepts of ecological parasitology was taking place in the Zoological Institute in the middle of 30th. E. N. Pavlovsky for the first time had formulated the principle of an organism as an environment for parasites, the concept of communities of parasitic organisms (concept of parasitocoenosis), and the theory of natural focuses of transmissive diseases. In the process of development of these scientific generalisations, a scientific direction named "Academician E. N. Pavlovsky's school of thought in parasitology" was formed in the USSR in 40-50th. In the frame of this school of thought, the main tusks of the Laboratory of Parasitology ZIN are to work out fundamental problems in ecology, systematics and morphology of parasitic and blood-sucking ticks, mites and insects. Within the ecological parasitology, different aspects of host-parasite relationships are studied at organism and population levels. The main basis of systematics studies of parasitic arthropodes is a scientific collection including over 250,000 samples. Based on this material, 40 key books and monographs on the USSR's fauna were created. Over 20 doctors of science and 50 candidates of science have been prepared within the laboratory or under the promotion of its stuff during 70 years of the existence of the Laboratory of Parasitology.