H. Stewart Chamberlain und seine Beurtheilung des Judenthums

B. Sopher

H. Stewart Chamberlain und seine Beurtheilung des Judenthums : II.

B. Sopher

H. Stewart Chamberlain und seine Beurtheilung des Judenthums : III.

B. Sopher

H. Stewart Chamberlain und seine Beurtheilung des Judenthums

B. Sopher

H. Stewart Chamberlain und seine Beurtheilung des Judenthums : V.

B. Sopher

H. Stewart Chamberlain und seine Beurtheilung des Judenthums : (Schluss)

B. Sopher

Über H. St. Chamberlain

Pantarhei

Über H. St. Chamberlain : (Schluss)

Pantarhei

Joseph Chamberlain

X. Y. Z.

Rho1p-Bni1p-Spa2p Interactions: Implication in Localization of Bni1p at the Bud Site and Regulation of the Actin Cytoskeleton in Saccharomyces cerevisiae

Rho1p is a yeast homolog of mammalian RhoA small GTP-binding protein. Rho1p is localized at the growth sites and required for bud formation. We have recently shown that Bni1p is a potential target of Rho1p and that Bni1p regulates reorganization of the actin cytoskeleton through interactions with profilin, an actin monomer-binding protein. Using the yeast two-hybrid screening system, we cloned a gene encoding a protein that interacted with Bni1p. This protein, Spa2p, was known to be localized at the bud tip and to be implicated in the establishment of cell polarity. The C-terminal 254 amino acid region of Spa2p, Spa2p(1213–1466), directly bound to a 162-amino acid region of Bni1p, Bni1p(826–987). Genetic analyses revealed that both the bni1 and spa2 mutations showed synthetic lethal interactions with mutations in the genes encoding components of the Pkc1p-mitogen-activated protein kinase pathway, in which Pkc1p is another target of Rho1p. Immunofluorescence microscopic analysis showed that Bni1p was localized at the bud tip in wild-type cells. However, in the spa2 mutant, Bni1p was not localized at the bud tip and instead localized diffusely in the cytoplasm. A mutant Bni1p, which lacked the Rho1p-binding region, also failed to be localized at the bud tip. These results indicate that both Rho1p and Spa2p are involved in the localization of Bni1p at the growth sites where Rho1p regulates reorganization of the actin cytoskeleton through Bni1p.

The ricinosomes of senescing plant tissue bud from the endoplasmic reticulum

The ricinosome (synonym, precursor protease vesicle) is a novel organelle, found so far exclusively in plant cells. Electron microscopic studies suggest that it buds off from the endoplasmic reticulum in senescing tissues. Biochemical support for this unusual origin now comes from the composition of the purified organelle, which contains large amounts of a 45-kDa cysteine endoprotease precursor with a C-terminal KDEL motif and the endoplasmic reticulum lumen residents BiP (binding protein) and protein disulfide isomerase. Western blot analysis, peptide sequencing, and mass spectrometry demonstrate retention of KDEL in the protease proform. Acidification of isolated ricinosomes causes castor bean cysteine endopeptidase activation, with cleavage of the N-terminal propeptide and the C-terminal KDEL motif. We propose that ricinosomes accumulate during senescence by programmed cell death and are activated by release of protons from acidic vacuoles.

The mosquitoes of the southern United States east of Oklahoma and Texas, by Stanley J. Carpenter ... Woodrow W. Middlekauff ... and Roy W. Chamberlain ...

no.3

Budūr al-ḍāwīyah fī al-taʻrīf bi-al-sādāt ahl al-Zāwiyah al-Dilāʼīyah : manuscript, undated

بسم الله الرحمن الرحيم وصلى الله على سيدنا ومولانا محمد وآله حدايق الازهار النددية في التعريف باهل الزاوية ... :Incipit