TY  - JOUR
A1  - Brixner, Tobias
A1  - Pawłowska, Monika
A1  - Goetz, Sebastian
A1  - Dreher, Christian
A1  - Wurdack, Matthias
A1  - Krauss, Enno
A1  - Razinskas, Gary
A1  - Geisler, Peter
A1  - Hecht, Bert
T1  - Shaping and spatiotemporal characterization of sub-10-fs pulses focused by a high-NA objective
N2  - We describe a setup consisting of a 4 f pulse shaper and a microscope with a high-NA objective lens and discuss the spects most relevant for an undistorted spatiotemporal profile of the focused beam. We demonstrate shaper-assisted pulse compression in focus to a sub-10-fs duration using phase-resolved interferometric spectral modulation (PRISM). We introduce a nanostructure-based method for sub-diffraction spatiotemporal characterization of strongly focused pulses. The distortions caused by optical aberrations and space–time coupling from the shaper can be reduced by careful setup design and alignment to about 10 nm in space and 1 fs in time.
KW  - Interference microscopy
KW  - Scanning microscopy
KW  - Subwavelength structures
KW  - nanostructures
KW  - Pulse shaping
KW  - Ultrafast measurements
Y1  - 2014
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-111120
ER  - 
TY  - JOUR
A1  - Kozjak‑Pavlovic, Vera
A1  - Ott, Christine
A1  - Utech, Mandy
A1  - Goetz, Monika
A1  - Rudel, Thomas
T1  - Requirements for the import of neisserial Omp85 into the outer membrane of human mitochondria
JF  - Bioscience Reports
N2  - β-Barrel proteins are present only in the outer membranes of Gram-negative bacteria, chloroplasts and mitochondria. Fungal mitochondria were shown to readily import and assemble bacterial β-barrel proteins, but human mitochondria exhibit certain selectivity. Whereas enterobacterial β-barrel proteins are not imported, neisserial ones are. Of those, solely neisserial Omp85 is integrated into the outer membrane of mitochondria. In this study, we wanted to identify the signal that targets neisserial β-barrel proteins to mitochondria. We exchanged parts of neisserial Omp85 and PorB with their Escherichia coli homologues BamA and OmpC. For PorB, we could show that its C-terminal quarter can direct OmpC to mitochondria. In the case of Omp85, we could identify several amino acids of the C-terminal β-sorting signal as crucial for mitochondrial targeting. Additionally, we found that at least two POTRA (polypeptide-transport associated) domains and not only the β-sorting signal of Omp85 are needed for its membrane integration and function in human mitochondria. We conclude that the signal that directs neisserial β-barrel proteins to mitochondria is not conserved between these proteins. Furthermore, a linear mitochondrial targeting signal probably does not exist. It is possible that the secondary structure of β-barrel proteins plays a role in directing these proteins to mitochondria.
KW  - β-barrel
KW  - mitochondrion
KW  - Omp85
KW  - PorB
KW  - POTRA domain
Y1  - 2013
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-96381
ER  -