Visualizing the whispering gallery modes in a cylindrical optical microcavity.

Whispering gallery modes in cylindrical integrated optics microcavities have, for what is to our knowledge the first time, been mapped with a photon scanning tunneling microscope. Optical images were obtained with a spatial resolution of 50 nm. By combination of information on the spatial optical distributions with wavelength-dependent measurements, an unexpectedly rich variety of intracavity phenomena, such as polarization conversion and interference of copropagating and counterpropagating modes, could be directly observed.

Protein translocation across the bacterial cytoplasmic membrane.

About 25% to 30% of the bacterial proteins function in the cell envelope or outside of the cell. These proteins are synthesized in the cytosol, and the vast majority is recognized as a ribosome-bound nascent chain by the signal recognition particle (SRP) or by the secretion-dedicated chaperone SecB. Subsequently, they are targeted to the Sec translocase in the cytoplasmic membrane, a multimeric membrane protein complex composed of a highly conserved protein-conducting channel, SecYEG, and a peripherally bound ribosome or ATP-dependent motor protein SecA.

Quasi interference of perpendicularly polarized guided modes observed with a photon scanning tunneling microscope.

The simultaneous detection of TE- as well as TM-polarized light with a photon scanning tunneling microscope leads to a quasi-interference pattern of these mutually perpendicular polarized fields. This interference pattern has been observed in the optical field distribution as a function of both position and wavelength. Comparison of experimental data with simulations confirms the interference of mutually orthogonal fields.

Direct observation of chaperone-induced changes in a protein folding pathway.

How chaperone interactions affect protein folding pathways is a central problem in biology. With the use of optical tweezers and all-atom molecular dynamics simulations, we studied the effect of chaperone SecB on the folding and unfolding pathways of maltose binding protein (MBP) at the single-molecule level. In the absence of SecB, we find that the MBP polypeptide first collapses into a molten globulelike compacted state and then folds into a stable core structure onto which several alpha helices are finally wrapped.

Integrated optical microcavities for enhanced evanescent-wave spectroscopy.

The use of integrated optical microcavities (MCs) for enhanced optical spectroscopy and sensing is investigated. The MC sustains high- Q whispering-gallery modes, in which the energy of the optical field can be efficiently stored. The resulting enhanced field can be used to probe fluorescent molecules in the cladding of the MC.

Sensor based on an integrated optical microcavity.

A novel integrated optical sensor based on a cylindrical microcavity (MC) is proposed. A MC sustains so-called whispering-gallery modes (WGMs), in which the energy of the optical field can be efficiently stored. By monitoring the scattering intensity from the MC, one can detect minute changes in the refractive index of the WGM, for instance, as a result of analyte adsorption.

LmrR is a transcriptional repressor of expression of the multidrug ABC transporter LmrCD in Lactococcus lactis.

LmrCD is an ABC-type multidrug transporter in Lactococcus lactis. LmrR encodes a putative transcriptional regulator. In a DeltalmrR strain, lmrCD is up-regulated.

Structural stability of GlcV, the nucleotide binding domain of the glucose ABC transporter of Sulfolobus solfataricus.

GlcV is the nucleotide binding domain of the ABC-type glucose transporter of the hyperthermoacidophile Sulfolobus solfataricus. GlcV consists of two domains, an N-terminal domain containing the typical nucleotide binding-fold and a C-terminal beta-barrel domain with unknown function. The unfolding and structural stability of the wild-type (wt) protein and three mutants that are blocked at different steps in the ATP hydrolytic cycle were studied.

Membrane protein insertion and secretion in bacteria.

Export of secretory proteins across and insertion of membrane proteins into the cytoplasmic membrane of Escherichia coli and other bacteria is mediated by the enzyme complex translocase. The last decade has seen a major advance in the understanding of the mechanism of these processes. A large part of this progress can be attributed to the development of general and powerful methods to study the translocase activity in vitro.

Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane--distinct translocases and mechanisms.

In bacteria, two major pathways exist to secrete proteins across the cytoplasmic membrane. The general Secretion route, termed Sec-pathway, catalyzes the transmembrane translocation of proteins in their unfolded conformation, whereupon they fold into their native structure at the trans-side of the membrane. The Twin-arginine translocation pathway, termed Tat-pathway, catalyses the translocation of secretory proteins in their folded state.

NisC, the cyclase of the lantibiotic nisin, can catalyze cyclization of designed nonlantibiotic peptides.

Nisin is a pentacyclic peptide antibiotic active against Gram-positive bacteria. Its thioether rings are formed by two enzymatic steps: nisin dehydratase (NisB)-mediated dehydration of serines and threonines followed by nisin cyclase (NisC)-catalyzed enantioselective coupling of cysteines to the formed dehydroresidues. Here, we report the in vivo activity of NisC to cyclize a wide array of unrelated and designed peptides that were fused to the nisin leader peptide.

Distribution and physiology of ABC-type transporters contributing to multidrug resistance in bacteria.

Membrane proteins responsible for the active efflux of structurally and functionally unrelated drugs were first characterized in higher eukaryotes. To date, a vast number of transporters contributing to multidrug resistance (MDR transporters) have been reported for a large variety of organisms. Predictions about the functions of genes in the growing number of sequenced genomes indicate that MDR transporters are ubiquitous in nature.

The active protein-conducting channel of Escherichia coli contains an apolar patch.

Protein translocation across the cytoplasmic membrane of Escherichia coli is mediated by translocase, a complex of a protein-conducting channel, SecYEG, and a peripheral motor domain, SecA. SecYEG has been proposed to constitute an aqueous path for proteins to pass the membrane in an unfolded state. To probe the solvation state of the active channel, the polarity sensitive fluorophore N-((2-(iodoacetoxy)ethyl)-N-methyl) amino-7-nitrobenz-2-oxa-1,3-diazole was introduced at specific positions in the C-terminal region of the secretory protein proOmpA.

Densely integrated microring resonator based photonic devices for use in access networks.

Two reconfigurable optical add-drop multiplexers, operating in the second or third telecom window, as well as a 1x4x4 reconfigurable lambda-router operating in the second telecom window, are demonstrated. The devices have a footprint less than 2 mm(2) and are based on thermally tunable vertically coupled microring resonators fabricated in Si(3)N(4)/SiO(2).

Bacterial sec-translocase unfolds and translocates a class of folded protein domains.

It is generally assumed that preprotein substrates must be presented in an unfolded state to the bacterial Sec-translocase in order to be translocated. Here, we have examined the ability of the Sec-translocase to translocate folded preproteins. Tightly folded human cardiac Ig-like domain I27 fused to the C terminus of proOmpA is translocated efficiently by the Sec-translocase and the translocation kinetics are determined by the extent of folding of the titin I27 domain.

Dissection and modulation of the four distinct activities of nisin by mutagenesis of rings A and B and by C-terminal truncation.

Nisin A is a pentacyclic antibiotic peptide produced by various Lactococcus lactis strains. Nisin displays four different activities: (i) it autoinduces its own synthesis; (ii) it inhibits the growth of target bacteria by membrane pore formation; (iii) it inhibits bacterial growth by interfering with cell wall synthesis; and, in addition, (iv) it inhibits the outgrowth of spores. Here we investigate the structural requirements and relevance of the N-terminal thioether rings of nisin by randomization of the ring A and B positions.

Grading of dysplasia in Barrett's oesophagus: substantial interobserver variation between general and gastrointestinal pathologists.

Aims: To determine interobserver variation in grading of dysplasia in Barrett's oesophagus (BO) between non-expert general pathologists and expert gastrointestinal pathologists on the one hand and between expert pathologists on the other hand.

Methods And Results: In this prospective multicentre study, non-expert and expert pathologists graded biopsy specimens of 920 patients with endoscopic BO, which were blindly reviewed by one member of a panel of expert pathologists (panel experts) and by a second panel expert in case of disagreement on dysplasia grade. Agreement between two of three pathologists was established as the final diagnosis.

Pushing, pulling and trapping--modes of motor protein supported protein translocation.

Protein translocation across the cellular membranes is an ubiquitous and crucial activity of cells. This process is mediated by translocases that consist of a protein conducting channel and an associated motor protein. Motor proteins interact with protein substrates and utilize the free energy of ATP binding and hydrolysis for protein unfolding, translocation and unbinding.

Identification of a system required for the functional surface localization of sugar binding proteins with class III signal peptides in Sulfolobus solfataricus.

The hyperthermophilic archaeon Sulfolobus solfataricus contains an unusual large number of sugar binding proteins that are synthesized as precursors with a class III signal peptide. Such signal peptides are commonly used to direct archaeal flagellin subunits or bacterial (pseudo)pilins into extracellular macromolecular surface appendages. Likewise, S.

Arginine 357 of SecY is needed for SecA-dependent initiation of preprotein translocation.

The Escherichia coli SecYEG complex forms a transmembrane channel for both protein export and membrane protein insertion. Secretory proteins and large periplasmic domains of membrane proteins require for translocation in addition the SecA ATPase. The conserved arginine 357 of SecY is essential for a yet unidentified step in the SecA catalytic cycle.

Flagellar motility and structure in the hyperthermoacidophilic archaeon Sulfolobus solfataricus.

Flagellation in archaea is widespread and is involved in swimming motility. Here, we demonstrate that the structural flagellin gene from the crenarchaeaon Sulfolobus solfataricus is highly expressed in stationary-phase-grown cells and under unfavorable nutritional conditions. A mutant in a flagellar auxiliary gene, flaJ, was found to be nonmotile.

Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1.

The ABC protein ABCE1, formerly named RNase L inhibitor RLI1, is one of the most conserved proteins in evolution and is expressed in all organisms except eubacteria. Because of its fundamental role in translation initiation and/or ribosome biosynthesis, ABCE1 is essential for life. Its molecular mechanism has, however, not been elucidated.

Production of dehydroamino acid-containing peptides by Lactococcus lactis.

Nisin is a pentacyclic peptide antibiotic produced by some Lactococcus lactis strains. Nisin contains dehydroresidues and thioether rings that are posttranslationally introduced by a membrane-associated enzyme complex, composed of a serine and threonine dehydratase NisB and the cyclase NisC. In addition, the transporter NisT is necessary for export of the modified peptide.

Genome sequencing and analysis of the versatile cell factory Aspergillus niger CBS 513.88.

The filamentous fungus Aspergillus niger is widely exploited by the fermentation industry for the production of enzymes and organic acids, particularly citric acid. We sequenced the 33.9-megabase genome of A.