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Increasing Scots pine (Pinus sylvestris L.) mortality has been recently observed in the dry inner valleys of the European Alps. Besides drought, infection with pine mistletoe (Viscum album ssp. austriacum) seems to play an important role in the mortality dynamics of Scots pines, but how mistletoes promote pine decline remains unclear. To verify whether pine mistletoe infection weakens the host via crown degradation, as observed for dwarf mistletoes, we studied the negative effects of pine mistletoe infestation on the photosynthetic tissues and branch growth of pairs of infested and non-infested branches. Pine mistletoe infection leads to crown degradation in its host by reducing the length, the radial increment, the ramification, the needle length and the number of needle years of the infested branches. This massive loss in photosynthetic tissue results in a reduction in primary production and a subsequent decrease in carbohydrate availability. The significant reduction in needle length due to mistletoe infection is an indication for a lower water and nutrient availability in infested branches. Thus, mistletoe infection might lead to a decrease in the availability of water and carbohydrates, the two most important growth factors, which are already shortened due to the chronic drought situation in the area. Therefore, pine mistletoe increases the risk of drought-induced mortality of its host when growing in a xeric environment.
C-terminal truncation of a metagenome-derived detergent protease for effective expression in E. coli
(2010)
Recently, a new alkaline protease named HP70 showing highest homology to extracellular serine proteases of Stenotrophomonas maltophilia and Xanthomonas campestris was found in the course of a metagenome screening for detergent proteases (Niehaus et al., submitted for publication). Attempts to efficiently express the enzyme in common expression hosts had failed. This study reports on the realization of overexpression in Escherichia coli after structural modification of HP70. Modelling of HP70 resulted in a two-domain structure, comprising the catalytic domain and a C-terminal domain which includes about 100 amino acids. On the basis of the modelled structure the enzyme was truncated by deletion of most of the C-terminal domain yielding HP70-C477.
This structural modification allowed effective expression of active enzyme using E. coli BL21-Gold as the host. Specific activity of HP70-C477 determined with suc-l-Ala-l-Ala-l-Pro-l-Phe-p-nitroanilide as the substrate was 30 ± 5 U/mg compared to 8 ± 1 U/mg of the native enzyme. HP70-C477 was most active at 40 °C and pH 7–11; these conditions are prerequisite for a potential application as detergent enzyme. Determination of kinetic parameters at 40 °C and pH = 9.5 resulted in KM = 0.23 ± 0.01 mM and kcat = 167.5 ± 3.6 s⁻¹. MS-analysis of peptide fragments obtained from incubation of HP70 and HP70-C477 with insulin B indicated that the C-terminal domain influences the cleavage preferences of the enzyme. Washing experiments confirmed the high potential of HP70-C477 as detergent protease.