Exposure assessment for nitrogen oxides and carbon monoxide in German hard coal mining.

OBJECTIVE: The exposure situation of German hard coal miners with respect to the components nitrogen monoxide and nitrogen dioxide. Carbon monoxide was measured additionally and the results are displayed but not discussed in detail in this paper. The data were used to estimate personal long-term exposures in an inception cohort. METHODS: For all three components, time weighted 8-h shift values were determined for typical groups of coalminers according to the European measurement standard. An expert panel from the coal mining company made an effort to estimate major potential changes in the exposure situation. RESULTS: The main sources of nitrogen oxides and carbon monoxide in hard coal mining were the diesel engines. Blasting fumes contributed only to a lesser degree and with different exposure characteristics, e.g. much reduced NO(2) levels compared to the mines' rear areas. As rough 8 h-shift averages describing the current exposure situation, we found 1.35 ppm NO and 0.21 ppm NO(2) for the diesel engine drivers. Blasting specialists were more difficult to evaluate but rough 8 h-shift averages of 0.84 ppm NO and 0.014 ppm NO(2) could be estimated from our measurement series. By applying these data and the estimates of experts about the retrospective exposure situation to a cohort of 1,369 coalminers, we derived mean (max) cumulative exposures in ppm x number of shifts of 1,748 (5,928) for NO and 19.6 (1,013) for NO(2) when summarizing over the follow-up period from 1974 until 1998. CONCLUSIONS: Especially for the diesel engine drivers, exposure can be regarded as rather high, in particular, when compared to recommended limits by SCOEL and MAK, though the exposures have been in line with the enforced German occupational exposure limits. Whether this exposure situation has caused adverse health effects will be investigated epidemiologically.

A new structural motif in the left terminal domain of large viroids identified by covariation analysis.

Sequence alignment of non-hammerhead viroids (Pospiviroidae) reveals that they can be divided into large and small viroids. Covariation analysis of these groups provides evidence for a rod-like secondary structure, but also for two proposed suboptimal structures, namely hairpin I and a bifurcation in the left terminus of large viroids. The strongest covariation within the branched T1 domain of all large Pospiviroidae indicates a new tertiary interaction, resulting in a double-pseudoknot within the (+) strand or an additional hairpin in the (-) strand. The structural element is expected to play a role in the viroid's life cycle.

The GTP-dependent restriction enzyme McrBC from Escherichia coli forms high-molecular mass complexes with DNA and produces a cleavage pattern with a characteristic 10-base pair repeat.

The GTP-dependent restriction enzyme McrBC consists of two polypeptides: one (McrB) that is responsible for GTP binding and hydrolysis as well as DNA binding and another (McrC) that is responsible for DNA cleavage. It recognizes two methylated or hemimethylated RC sites (R(m)C) at a distance of approximately 30 to more than 2000 base pairs and cleaves the DNA close to one of the two R(m)C sites. This process is strictly coupled to GTP hydrolysis and involves the formation of high-molecular mass complexes. We show here using footprinting techniques, surface plasmon resonance, and scanning force microscopy experiments that in the absence of McrC, McrB binds to a single R(m)C site. If a second R(m)C site is present on the DNA, it is occupied independently by McrB. Whereas the DNA-binding domain of McrB forms 1:1 complexes with each R(m)C site and shows a clear footprint on both R(m)C sites, full-length McrB forms complexes with a stoichiometry of at least 4:1 at each R(m)C site, resulting in a slightly more extended footprint. In the presence of McrC, McrB forms high-molecular mass complexes of unknown stoichiometry, which are considerably larger than the complexes formed with McrB alone. In these complexes and when GTP is present, the DNA is cleaved next to one of the R(m)C sites at distances differing by one to five helical turns, suggesting that in the McrBC-DNA complex only a few topologically well-defined phosphodiester bonds of the DNA are accessible for the nucleolytic center of McrC.