39 research outputs found
Isolation, crystallization, and investigation of ribosomal protein S8 complexed with specific fragments of rRNA of bacterial or archaeal origin. Biochemistry 66
Study of the nature of protein-rRNA complexes is a topical problem of modern molecular biology. Structural studies of rRNA-protein complexes are the most direct and precise method of analysis of these interactions. Because ribosomal proteins are most conservative during evolution, their complexes with specific RNA fragments provide an interesting model for studying RNA-protein interactions. Ribosomal protein S8 from E. coli plays a key role in assembling the small ribosomal subunit The major region of protein S8 binding on 16S rRNA was determined by partial hydrolysis with restric tion endonucleases The binding sites of protein S8 on 16S rRNA are similar in E. coli and T. thermophilus. It was shown that ACCELERATED PUBLICATION 0006 2979/01/6609 0948$25.00 ©2001 MAIK "Nauka / Interperiodica" * To whom correspondence should be addressed. Vol. 66, No. 9, 2001, pp. 948 953. Translated from Biokhimiya, Vol. 66, No. 9, 2001, pp. 1165 1171. Original Russian Text Copyright © 2001 Abstract-The core ribosomal protein S8 binds to the central domain of 16S rRNA independently of other ribosomal proteins and is required for assembling the 30S subunit. It has been shown with E. coli ribosomes that a short rRNA fragment restrict ed by nucleotides 588 602 and 636 651 is sufficient for strong and specific protein S8 binding. In this work, we studied the complexes formed by ribosomal protein S8 from Thermus thermophilus and Methanococcus jannaschii with short rRNA frag ments isolated from the same organisms. The dissociation constants of the complexes of protein S8 with rRNA fragments were determined. Based on the results of binding experiments, rRNA fragments of different length were designed and syn thesized in preparative amounts in vitro using T7 RNA polymerase. Stable S8-RNA complexes were crystallized. Crystals were obtained both for homologous bacterial and archaeal complexes and for hybrid complexes of archaeal protein with bac terial rRNA. Crystals of the complex of protein S8 from M. jannaschii with the 37 nucleotide rRNA fragment from the same organism suitable for X ray analysis were obtained
The Lie algebroid Poisson sigma model
The Poisson--Weil sigma model, worked out by us recently, stems from gauging
a Hamiltonian Lie group symmetry of the target space of the Poisson sigma
model. Upon gauge fixing of the BV master action, it yields interesting
topological field theories such as the 2--dimensional Donaldson-Witten
topological gauge theory and the gauged A topological sigma model. In this
paper, generalizing the above construction, we construct the Lie algebroid
Poisson sigma model. This is yielded by gauging a Hamiltonian Lie groupoid
symmetry of the Poisson sigma model target space. We use the BV quantization
approach in the AKSZ geometrical version to ensure consistent quantization and
target space covariance. The model has an extremely rich geometry and an
intricate BV cohomology, which are studied in detail.Comment: 52 pages, Late
Enantiosensitive Structure Determination by Photoelectron Scattering on Single Molecules
X-ray as well as electron diffraction are powerful tools for structure
determination of molecules. Electron diffraction methods yield
\r{A}ngstrom-resolution even when applied to large systems or systems involving
weak scatterers such as hydrogen atoms. For cases in which molecular crystals
cannot be obtained or the interaction-free molecular structure is to be
addressed, corresponding electron scattering approaches on gas-phase molecules
exist. Such studies on randomly oriented molecules, however, can only provide
information on interatomic distances, which is challenging to analyse in case
of overlapping distance parameters and they do not reveal the handedness of
chiral systems8. Here, we present a novel scheme to obtain information on the
structure, handedness and even detailed geometrical features of single
molecules in the gas phase. Using a loop-like analysis scheme employing input
from ab initio computations on the photoionization process, we are able to
deduce the three dimensional molecular structure with sensitivity to the
position individual atoms, as e.g. protons. To achieve this, we measure the
molecular frame diffraction pattern of core-shell photoelectrons in combination
with only two ionic fragments from a molecular Coulomb explosion. Our approach
is expected to be suitable for larger molecules, as well, since typical size
limitations regarding the structure determination by pure Coulomb explosion
imaging are overcome by measuring in addition the photoelectron in coincidence
with the ions. As the photoelectron interference pattern captures the molecular
structure at the instant of ionization, we anticipate our approach to allow for
tracking changes in the molecular structure on a femtosecond time scale by
applying a pump-probe scheme in the future
The transition probabilities from the ground state to the excited J = 0 ^1Σu^+ levels of H_2
Dieser Beitrag ist mit Zustimmung des Rechteinhabers aufgrund einer (DFG-geförderten) Allianz- bzw. Nationallizenz frei zugänglich. - This publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively
The transition probabilities from the ground state to the excited J 0 1Sigma u levels of H2 Measurements and ab initio quantum defect study
Dieser Beitrag ist mit Zustimmung des Rechteinhabers aufgrund einer (DFG-geförderten) Allianz- bzw. Nationallizenz frei zugänglich. - This publication is with permission of the rights owner freely accessible due to an Alliance licence and a national licence (funded by the DFG, German Research Foundation) respectively