Characteristics of Chitosan Films with the Bioactive Substances-Caffeine and Propolis.

Chitosan is a natural and biodegradable polymer with promising potential for biomedical applications. This study concerns the production of chitosan-based materials for future use in the medical industry. Bioactive substances-caffeine and ethanolic propolis extract (EEP)-were incorporated into a chitosan matrix to increase the bioactivity of the obtained films and improve their mechanical properties.

Application of 3D Scanning Method to Assess Mounting Holes' Shape Instability of Pinewood.

Swelling and shrinkage anisotropy affect the susceptibility to an assembly of wooden elements by changing designed clearances or interference fits. This work described the new method to measure mounting holes' moisture-induced shape instability and its verification using three sets of twin samples made of Scots pinewood. Each set of samples contained a pair with different grain patterns.

Chemical Composition and Related Properties of Lime ( Mill.) Bark and Wood as Affected by Tree Growth Conditions.

Mill. is a favourite tree used in urban spaces. For this reason, it is important to know its sensitivity to environmental stress, which is particularly burdensome for vegetation in urban spaces.

Effects of Harvest Maturity on the Chemical and Energetic Properties of Corn Stover Biomass Combustion.

Over the last decade, there has been increased interest in applying biomass as a raw material for producing biofuels used for thermochemical conversions. Extensive use of biomass could lead to controversial competition for arable land, water, and food; therefore, only waste materials and agricultural by-products and residues should be used to produce biofuels. One suitable by-product of agricultural production is crop residue from the harvest of maize for grain (corn stover).

Moisture-Dependent Strength Properties of Thermally-Modified Wood in Compression.

European ash ( L.) is one of the species commonly used for wood thermal modification that improves its performance. The presented research aimed to investigate a moisture-dependent strength anisotropy of thermally-modified European ash in compression.

Discrete interactions between bacteriophage T7 primase-helicase and DNA polymerase drive the formation of a priming complex containing two copies of DNA polymerase.

Replisomes are multiprotein complexes that coordinate the synthesis of leading and lagging DNA strands to increase the replication efficiency and reduce DNA strand breaks caused by stalling of replication forks. The bacteriophage T7 replisome is an economical machine that requires only four proteins for processive, coupled synthesis of two DNA strands. Here we characterize a complex between T7 primase-helicase and DNA polymerase on DNA that was trapped during the initiation of Okazaki fragment synthesis from an RNA primer.

ATP hydrolysis by RAD50 protein switches MRE11 enzyme from endonuclease to exonuclease.

MRE11-RAD50 is a key early response protein for processing DNA ends of broken chromosomes for repair, yet how RAD50 nucleotide dynamics regulate MRE11 nuclease activity is poorly understood. We report here that ATP binding and ATP hydrolysis cause a striking butterfly-like opening and closing of the RAD50 subunits, and each structural state has a dramatic functional effect on MRE11. RAD50-MRE11 has an extended conformation in solution when MRE11 is an active nuclease.

Conformational trapping of mismatch recognition complex MSH2/MSH3 on repair-resistant DNA loops.

Insertion and deletion of small heteroduplex loops are common mutations in DNA, but why some loops are prone to mutation and others are efficiently repaired is unknown. Here we report that the mismatch recognition complex, MSH2/MSH3, discriminates between a repair-competent and a repair-resistant loop by sensing the conformational dynamics of their junctions. MSH2/MSH3 binds, bends, and dissociates from repair-competent loops to signal downstream repair.

Clamping the Mec1/ATR checkpoint kinase into action.

The yeast checkpoint protein kinase Mec1, the ortholog of human ATR, is the essential upstream regulator of the cell cycle checkpoint in response to DNA damage and to stalling of DNA replication forks. The activity of Mec1/ATR is not directly regulated by the DNA substrates that signal checkpoint activation. Rather the signal appears to be transduced to Mec1 by factors that interact with the signaling DNA substrates.

Analysis of protein-DNA interactions using surface plasmon resonance.

Protein-DNA interactions are required for access and protection of the genetic information within the cell. Historically these interactions have been studied using genetic, biochemical, and structural methods resulting in qualitative or semiquantitative interaction data. In the future the focus will be on high quality quantitative data to model a huge number of interactions forming a specific network in system biology approaches.

The checkpoint clamp activates Mec1 kinase during initiation of the DNA damage checkpoint.

Yeast Mec1/Ddc2 protein kinase, the ortholog of human ATR/ATRIP, plays a central role in the DNA damage checkpoint. The PCNA-like clamp Rad17/Mec3/Ddc1 (the 9-1-1 complex in human) and its loader Rad24-RFC are also essential components of this signal transduction pathway. Here we have studied the role of the clamp in regulating Mec1, and we delineate how the signal generated by DNA lesions is transduced to the Rad53 effector kinase.

Cluster of DnaA boxes involved in regulation of Streptomyces chromosome replication: from in silico to in vivo studies.

In Streptomyces coelicolor, replication is initiated by the DnaA protein in the centrally located oriC region and proceeds bidirectionally until the replication forks reach the ends of the linear chromosome. We identified three clusters of DnaA boxes (H69, H24, and D78) which are in a relatively short segment of the chromosome centered on the oriC region. Of the clusters analyzed, D78 exhibited the highest affinity for the DnaA protein; the affinity of DnaA for the D78 cluster was about eightfold higher than the affinity for oriC.

Replication protein A directs loading of the DNA damage checkpoint clamp to 5'-DNA junctions.

The heterotrimeric checkpoint clamp comprises the Saccharomyces cerevisiae Rad17, Mec3, and Ddc1 subunits (Rad17/3/1, the 9-1-1 complex in humans). This DNA damage response factor is loaded onto DNA by the Rad24-RFC (replication factor C-like complex with Rad24) clamp loader and ATP. Although Rad24-RFC alone does not bind to naked partial double-stranded DNA, coating of the single strand with single-stranded DNA-binding protein RPA (replication protein A) causes binding of Rad24-RFC via interactions with RPA.

Overproduction and purification of RFC-related clamp loaders and PCNA-related clamps from Saccharomyces cerevisiae.

The replication clamp PCNA and its loader RFC (Replication Factor C) are central factors required for processive replication and coordinated DNA repair. Recently, several additional related clamp loaders have been identified. These alternative clamp loaders contain the small Rfc2-5 subunits of RFC, but replace the large Rfc1 subunit by a pathway-specific alternative large subunit, Rad24 for the DNA damage checkpoint, Ctf18 for the establishment of sister chromatid cohesion, and Elg1 for a general function in chromosome stability.

Function of Rad17/Mec3/Ddc1 and its partial complexes in the DNA damage checkpoint.

The Saccharomyces cerevisiae heterotrimeric checkpoint clamp consisting of the Rad17, Mec3, and Ddc1 subunits (Rad17/3/1, the 9-1-1 complex in humans) is an early response factor to DNA damage in a signal transduction pathway leading to the activation of the checkpoint system and eventually to cell cycle arrest. These subunits show structural similarities with the replication clamp PCNA and indeed, it was demonstrated in vitro that Rad17/3/1 could be loaded onto DNA by checkpoint specific clamp loader Rad24-RFC, analogous to the PCNA-RFC clamp-clamp loader system. We have studied the interactions between the checkpoint clamp subunits and the activity of partial clamp complexes.

Proliferating cell nuclear antigen promotes translesion synthesis by DNA polymerase zeta.

DNA polymerase zeta (Pol zeta), a heterodimer of Rev3 and Rev7, is essential for DNA damage provoked mutagenesis in eukaryotes. DNA polymerases that function in a processive complex with the replication clamp proliferating cell nuclear antigen (PCNA) have been shown to possess a close match to the consensus PCNA-binding motif QxxLxxFF. This consensus motif is lacking in either subunit of Pol zeta, yet its activity is stimulated by PCNA.

Architecture of bacterial replication initiation complexes: orisomes from four unrelated bacteria.

Bacterial chromosome replication is mediated by single initiator protein, DnaA, that interacts specifically with multiple DnaA boxes located within the origin (oriC). We compared the architecture of the DnaA-origin complexes of evolutionarily distantly related eubacteria: two Gram-negative organisms, Escherichia coli and Helicobacter pylori, and two Gram-positive organisms, Mycobacterium tuberculosis and Streptomyces coelicolor. Their origins vary in size (from approx.

The PCNA-RFC families of DNA clamps and clamp loaders.

The proliferating cell nuclear antigen PCNA functions at multiple levels in directing DNA metabolic pathways. Unbound to DNA, PCNA promotes localization of replication factors with a consensus PCNA-binding domain to replication factories. When bound to DNA, PCNA organizes various proteins involved in DNA replication, DNA repair, DNA modification, and chromatin modeling.

[Responsibilities of enterprises introducing new dangerous chemical substances and preparations].

The paper reviews the responsibilities of producers, importers and distributors set in a new Act of January 2001 on chemical substances and preparations (Off. J. 2001, No.

Requirement for ATP by the DNA damage checkpoint clamp loader.

The DNA damage clamp loader replication factor C (RFC-Rad24) consists of the Rad24 protein and the four small Rfc2-5 subunits of RFC. This complex loads the heterotrimeric DNA damage clamp consisting of Rad17, Mec3, and Ddc1 (Rad17/3/1) onto partial duplex DNA in an ATP-dependent manner. Interactions between the clamp loader and the clamp have been proposed to mirror those of the replication clamp loader RFC and the sliding clamp proliferating cell nuclear antigen (PCNA).

The mechanism of regulation of bacteriophage lambda pR promoter activity by Escherichia coli DnaA protein.

Apart from its function as an initiator of DNA replication, the Escherichia coli DnaA protein is also a specific transcription factor. It activates and represses a number of promoters. However, mechanisms of transcription stimulation by DnaA remained unknown.

Yeast Rad17/Mec3/Ddc1: a sliding clamp for the DNA damage checkpoint.

The Saccharomyces cerevisiae Rad24 and Rad17 checkpoint proteins are part of an early response to DNA damage in a signal transduction pathway leading to cell cycle arrest. Rad24 interacts with the four small subunits of replication factor C (RFC) to form the RFC-Rad24 complex. Rad17 forms a complex with Mec3 and Ddc1 (Rad1731) and shows structural similarities with the replication clamp PCNA.

Structural elements of the Streptomyces oriC region and their interactions with the DnaA protein.

Streptomycetes differ from other prokaryotic organisms in their mycelial life cycle and in possessing a large, linear, GC-rich chromosome. To deduce structural features of the Streptomyces origin of chromosomal replication, the oriC sequences of three Streptomyces species (S. antibioticus, S.