Orbifold boundary states from Cardy's condition

Boundary states for D-branes at orbifold fixed points are constructed in close analogy with Cardy's derivation of consistent boundary states in RCFT. Comments are made on the interpretation of the various coefficients in the explicit expressions, and the relation between fractional branes and wrapped branes is investigated for $\mathbb{C}^2/\Gamma$ orbifolds. The boundary states are generalised to theories with discrete torsion and a new check is performed on the relation between discrete torsion phases and projective representations.Comment: LaTeX2e, 50 pages, 5 figures. V3: final version to appear on JHEP (part of a section moved to an appendix, titles of some references added, one sentence in the introduction expanded

The Psb27 protein facilitates manganese cluster assembly in photosystem II

Photosystem II (PSII) is a large membrane protein complex that uses light energy to convert water to molecular oxygen. This enzyme undergoes an intricate assembly process to ensure accurate and efficient positioning of its many components. It has been proposed that the Psb27 protein, a lumenal extrinsic subunit, serves as a PSII assembly factor. Using a psb27 genetic deletion strain (Δpsb27) of the cyanobacterium Synechocystis sp. PCC 6803, we have defined the role of the Psb27 protein in PSII biogenesis. While the Psb27 protein was not essential for photosynthetic activity, various PSII assembly assays revealed that the Δpsb27 mutant was defective in integration of the Mn4Ca1Clx cluster, the catalytic core of the oxygen-evolving machinery within the PSII complex. The other lumenal extrinsic proteins (PsbO, PsbU, PsbV, and PsbQ) are key components of the fully assembled PSII complex and are important for the water oxidation reaction, but we propose that the Psb27 protein has a distinct function separate from these subunits. We show that the Psb27 protein facilitates Mn4Ca1Cl x cluster assembly in PSII at least in part by preventing the premature association of the other extrinsic proteins. Thus, we propose an exchange of lumenal subunits and cofactors during PSII assembly, in that the Psb27 protein is replaced by the other extrinsic proteins upon assembly of the Mn4Ca1Clx cluster. Furthermore, we show that the Psb27 protein provides a selective advantage for cyanobacterial cells under conditions such as nutrient deprivation where Mn4Ca 1Clx cluster assembly efficiency is critical for survival. © 2008 by The American Society for Biochemistry and Molecular Biology, Inc