Regimes of atomic diffraction: Raman versus Bragg diffraction in retroreflective geometries

We provide a comprehensive study of atomic Raman and Bragg diffraction when coupling to a pair of counterpropagating light gratings (double diffraction) or to a single one (single diffraction) and discuss the transition from one case to the other in a retroreflective geometry as the Doppler detuning changes. In contrast to single diffraction, double Raman loses its advantage of high diffraction efficiency for short pulses and has to be performed in a Bragg-type regime. Moreover, the structure of double diffraction leads to further limitations for broad momentum distributions on the efficiency of mirror pulses, making the use of (ultra) cold ensembles essential for high diffraction efficiency.Comment: 16 pages, 14 figure

Atomic Raman scattering: Third-order diffraction in a double geometry

In a retroreflective scheme atomic Raman diffraction adopts some of the properties of Bragg diffraction due to additional couplings to off-resonant momenta. As a consequence, double Raman diffraction has to be performed in a Bragg-type regime. Taking advantage of this regime, double Raman allows for resonant higher-order diffraction. We study theoretically the case of third-order diffraction and compare it to first order as well as a sequence of first-order pulses giving rise to the same momentum transfer as the third-order pulse. In fact, third-order diffraction constitutes a competitive tool for the diffraction of ultracold atoms and interferometry based on large momentum transfer since it allows to reduce the complexity of the experiment as well as the total duration of the diffraction process compared to a sequence.Comment: 10 pages, 13 figure

Posttranslational protein transport in yeast reconstituted with a purified complex of Sec proteins and Kar2p

AbstractWe have reproduced the posttranslational mode of protein translocation across the endoplasmic reticulum membrane with reconstituted proteoliposomes containing a purified complex of seven yeast proteins. This Sec complex includes a heterotrimeric Sec61p complex, homologous to that in mammals, as well as all other membrane proteins found in genetic screens for translocation components. Efficient posttranslational translocation also requires the addition of lumenal Kar2p(BIP) and ATP. The trimeric Sec61p complex also exists as a separate entity that, in contrast with the large Sec complex, is associated with membrane-bound ribosomes. We therefore hypothesize that distinct membrane protein complexes function in co- and posttranslational translocation pathways

NDC1: a crucial membrane-integral nucleoporin of metazoan nuclear pore complexes

POM121 and gp210 were, until this point, the only known membrane-integral nucleoporins (Nups) of vertebrates and, thus, the only candidate anchors for nuclear pore complexes (NPCs) within the nuclear membrane. In an accompanying study (see Stavru et al. on p. 477 of this issue), we provided evidence that NPCs can exist independently of POM121 and gp210, and we predicted that vertebrate NPCs contain additional membrane-integral constituents. We identify such an additional membrane protein in the NPCs of mammals, frogs, insects, and nematodes as the orthologue to yeast Ndc1p/Cut11p. Human NDC1 (hNDC1) likely possesses six transmembrane segments, and it is located at the nuclear pore wall. Depletion of hNDC1 from human HeLa cells interferes with the assembly of phenylalanine-glycine repeat Nups into NPCs. The loss of NDC1 function in Caenorhabditis elegans also causes severe NPC defects and very high larval and embryonic mortality. However, it is not ultimately lethal. Instead, homozygous NDC1-deficient worms can be propagated. This indicates that none of the membrane-integral Nups is universally essential for NPC assembly, and suggests that NPC biogenesis is an extremely fault-tolerant process

Bragg-diffraction-induced imperfections of the signal in retroreflective atom interferometers

We present a detailed study of the effects of imperfect atom-optical manipulation in Bragg-based light-pulse atom interferometers. Off-resonant higher-order diffraction leads to population loss, spurious interferometer paths, and diffraction phases. In a path-dependent formalism, we study numerically various effects and analyze the interference signal caused by an external phase or gravity. We compare first-order single and double Bragg diffraction in retroreflective setups. In double Bragg diffraction, phase imperfections lead to a beating due to three-path interference. Some effects of diffraction phases can be avoided by adding the population of the outer exit ports of double diffraction

Structure and biosynthesis of the signal-sequence receptor

The signal-sequence receptor (SSR) has previously been shown to be a component of the environment which nascent polypeptides meet on passage through the endoplasmic reticulum (ER) membrane. We report here on the primary structure of the SSR as deduced from cDNA clones and from direct protein sequencing. The glycoprotein is synthesized with a cleavable amino-terminal signal sequence and contains only one classical membrane-spanning segment. Its insertion into the ER membrane during biosynthesis depends on the function of the signal-recognition particle. SSR shows a remarkable charge distribution with the amino terminus being highly negatively charged, and the cytoplasmic carboxyl terminus positively charged. The SSR can be phosphorylated in its cytoplasmic tail both in intact cells and in a cell-free system, suggesting a regulation of its function. The localization of the protein in the ER membrane was confirmed by immunofluorescence microscopy

Atomic Raman scattering: Third-order diffraction in a double geometry

In a retroreflective scheme with an atom initially at rest, atomic Raman diffraction adopts some of the properties of Bragg diffraction due to additional couplings to off-resonant momenta. As a consequence, double Raman diffraction has to be performed in a Bragg-type regime, where the pulse duration is sufficiently long to suppress diffraction into spurious orders. Taking advantage of this regime, double Raman allows for resonant higher-order diffraction. We study theoretically the case of third-order diffraction and compare it to first order as well as a sequence of first-order Raman pulses giving rise to the same momentum transfer as the third-order pulse. Moreover, we demonstrate that interferometry is possible, and we investigate amplitude and contrast of a third-order double Raman Mach-Zehnder interferometer. In fact, third-order diffraction constitutes a competitive tool for the diffraction of ultracold atoms and interferometry based on large momentum transfer since it allows one to reduce the complexity of the experiment as well as the total duration of the diffraction process compared to a sequence, at the cost of higher pulse intensities

The Signal Sequence Receptor Has a Second Subunit and IsPart of a Translocation Complex in the Endoplasmic Reticulum as Probed by Bifunctional Reagents

Bifunctional cross-linking reagents were used to probe the protein environment in the ER membrane of the signal sequence receptor (SSR), a 34-kD integral membrane glycoprotein (Wiedmann, M., T. V. Kurzchalia, E. Hartmarm, and T. A. Rapoport. 1987. Nature [Lond.]. 328:830-833). The proximity of several polypeptides was demonstrated. A 22-kD glycoprotein was identified tightly bound to the 34-kD SSR even after membrane solubilization. The 34-kD polypeptide, now termed otSSR, and the 22-kD polypeptide, the #SSR, represent a heterodimer. We report on the sequence of the/3SSR, its membrane topology, and on the mechanism of its integration into the membrane. Cross-linking also produced dimers of the a-subunit of the SSR indicating that oligomers of the SSR exist in the ER membrane. Various bifunctional cross-linking reagents were used to study the relation to ER membrane proteins of nascent chains of preprolactin and/3-1actamase at different stages of their translocation through the membrane. The predominant cross-linked products obtained in high yields contained the aSSR, indicating in conjunction with previous results that it is a major membrane protein in the neighborhood of translocating nascent chains of secretory proteins. The results support the existence of a translocon, a translocation complex involving the SSR, which constitutes the specific site of protein translocation across the ER membrane