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Traditionally, the durability of timber is determined in laboratory decay tests or ground contact field tests. Since it is commonly accepted that results from those tests are not directly transferable to less severe above-ground exposures, this study aimed at assessing alternative durability measures related to the moisture performance of wood. Results from above-ground tests including continuous wood moisture monitoring were analyzed. Decay ratings determined in double-layer field tests were compared with time of wetness, and temperature- and moisture-induced dose according to a dose-response model for above-ground decay. Significant differences between European wood species were found in façade, decking, sandwich, lap-joint, and double-layer tests with respect to their moisture performance. It is concluded that for many wood-based products intended for above-ground use, a combination of short-term laboratory decay tests and mid-term moisture performance field tests may serve as time-saving alternative to long-term decay tests in the field. [ABSTRACT FROM AUTHOR]

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Ribosomes synthesizing inner membrane proteins in Escherichia coli are targeted to the membrane by the signal recognition particle (SRP) pathway. By rapid kinetic analysis we show that after initial binding to the ribosome, SRP undergoes dynamic fluctuations in search of additional interactions. Non-translating ribosomes, or ribosomes synthesizing non-membrane proteins, do not provide these contacts, allowing SRPs to dissociate rapidly. A nascent peptide in the exit tunnel stabilizes SRPs in a standby state. Binding to the emerging signal-anchor sequence (SAS) of a nascent membrane protein halts the fluctuations of SRP, resulting in complex stabilization and recruitment of the SRP receptor. We propose a kinetic model where SRP rapidly scans all ribosomes until it encounters a ribosome exposing an SAS. Binding to the SAS switches SRP into the targeting mode, in which dissociation is slow and docking of the SRP receptor is accelerated. [ABSTRACT FROM AUTHOR]

Ribosomes synthesizing inner membrane proteins in Escherichia coli are targeted to the translocon in the plasma membrane by the signal recognition particle (SRP) and the SRP receptor, FtsY. Here we show using a purified system that membrane targeting does not require an exposed signal-anchor sequence, as SRP-dependent targeting takes place with ribosomes containing short nascent peptides, with or without a signal-anchor sequence, within the peptide exit tunnel. Signaling from inside the tunnel involves ribosomal protein L23, which constitutes part of the SRP binding site. When nascent peptides emerge from the ribosome, the targeting complex is maintained with ribosomes exposing a signal-anchor sequence, whereas ribosomes exposing other sequences are released. These results indicate that ribosome–nascent chain complexes containing any nascent peptide within the exit tunnel can enter the SRP targeting pathway to be sorted at the membrane into ribosome-nascent chain complexes that synthesize either membrane or cytosolic proteins. [ABSTRACT FROM AUTHOR]