The Jurassic-Cretaceous transition of Southern Sweden—palynological and sedimentological interpretation

Palynological studies on the Vitab?ck Clay help resolve the position of the Jurassic-Cretaceous boundary in southern Sweden. Well-preserved assemblages of terrestrial pollen and spores, together with abundant algae (Botryococcus), and for the first time, dinoflagellates have been identified in the Vitab?ck Clay. A Berriasian age is corroborated for the Vitab?ck Clay based on the palynological data; the Jurassic-Cretaceous boundary being placed around the contact of this unit with the underlying “Nytorp Sand”. The terrestrial vegetation was dominated by coniferous forest with an understorey of ferns in a warm, temperate climate. The palynoflora shows compositional similarities to the Northern Chinese Floral Province and especially the Jehol Group. The majority of the Vitab?ck Clay represents a moderate-to low-energy paralic succession. However, the basal part of the unit incorporates anomalously coarse material of mixed terrestrial and marine origin. This sedimentary package is herein interpreted to represent tsunami deposits and is similar to coeval tsunami-related deposits in France.     

Temperature-scan cryocrystallography reveals reaction intermediates in bacteriophytochrome

Light is a fundamental signal that regulates important physiological processes such as development and circadian rhythm in living organisms. Phytochromes form a major family of photoreceptors responsible for red light perception in plants, fungi and bacteria. They undergo reversible photoconversion between red-absorbing (Pr) and far-red-absorbing (Pfr) states, thereby ultimately converting a light signal into a distinct biological signal that mediates subsequent cellular responses. Several structures of microbial phytochromes have been determined in their dark-adapted Pr or Pfr states. However, the structural nature of initial photochemical events has not been characterized by crystallography. Here we report the crystal structures of three intermediates in the photoreaction of Pseudomonas aeruginosa bacteriophytochrome (PaBphP). We used cryotrapping crystallography to capture intermediates, and followed structural changes by scanning the temperature at which the photoreaction proceeded. Light-induced conformational changes in PaBphP originate in ring D of the biliverdin (BV) chromophore, and E-to-Z isomerization about the C(15) = C(16) double bond between rings C and D is the initial photochemical event. As the chromophore relaxes, the twist of the C(15) methine bridge about its two dihedral angles is reversed. Structural changes extend further to rings B and A, and to the surrounding protein regions. These data indicate that absorption of a photon by the Pfr state of PaBphP converts a light signal into a structural signal via twisting and untwisting of the methine bridges in the linear tetrapyrrole within the confined protein cavity.     

Horizontal gene transfer from Eukarya to Bacteria and domain shuffling: the α-amylase model

-Amylases are present in all kingdoms of the living world. Despite strong conservation of the tertiary structure, only a few amino acids are conserved in interkingdom comparisons. Animal -amylases are characterized by several typical motifs and biochemical properties. A few cases of such -amylases have been previously reported in some eubacterial species. We screened the bacterial genomes available in the sequence databases for new occurrences of animal-like -amylases. Three novel cases were found, which belong to unrelated bacterial phyla: Chloroflexus aurantiacus, Microbulbifer degradans, and Thermobifida fusca. All the animal-like -amylases in Bacteria probably result from repeated horizontal gene transfer from animals. The M. degradans genome also contains bacterial-type and plant-type -amylases in addition to the animal-type one. Thus, this species exhibits -amylases of animal, plant, and bacterial origins. Moreover, the similarities in the extra C-terminal domains (different from both the -amylase domain C and the starch-binding domain), when present, also suggest interkingdom as well as intragenomic shuffling.Received 17 October 2003; accepted 6 November 2003