Corts en la centúria 1400 a 1500 [Manuscrito]

Alcance y contenido: Copia ms. de fragmentos de varios capitulos de las Cortes celebradas entre 1418 en Valencia y 1510 en Monzón siendo reyes Alfonso V el Magnánimo (1416-1458) y Fernando el Católico (1474-1517).

El deseo regulado por el entendimiento regulador en vn Principe bueno desde los principios de su Reynado

Según Palau, IV, 71120, fue publicado en 1701

[Reflecciones sobre la [exc]elencia, antiguedad, virtudes, y propiedades de la fuente de Encorts, y su prodigiosa agua] [Manuscrito]

Alcance y contenido: Ms. autógrafo, que relata las propiedades curativas de la font d'en Corts.

Documentos en el archivo de Vall Digna [Manuscrito]

Alcance y contenido: Ms. que contiene un breve relación de los documentos sitos en el Monasterio de Valldigna relativos a la fundación del Monasterio de San Bernardo en la huerta de Valencia, conocido como Sant Bernat de Rascanya, hoy San Miguel de los Reyes y a las tierras de realengo que poseían.

Plan [sic] y corte de los baños árabes de Valencia [Material gráfico] =Plan et coupe des bains arabes à Valence=Plan and section of the arabians baths at Valencia

Resumen: Descripción: dos interiores, un corte transversal, la planta y el corte transversal de una columna de los Baños Árabes de Valencia

Fuero Juzgo

Marca tip. en port

[Copia de documentos relativos a Franciscus Carolus de Borja et Centelles, Marchio de Lombai...] [Manuscrito]

Enc. piel con hierros dorados deteriorada

La fuente [Material gráfico] : Játiva

Alcance y contenido: Fuente Real de la Trinidad y fachada principal de la Igleisa del Antiguo Convento de la Trinidad

Sucessos fatales desta ciudad, y Reyno de Valencia o Puntual Diario de lo sucedido en los Años de 1705, 1706 y 1707 [Manuscrito] : Tomo I

En algunas notas del ms. y en lomo se le da el título de "Dietario"

[Colección de grabados con inscripciones y detalles árabes de Córdoba y Granada] [Material gráfico]

Contiene: INSCRIPCIONES ARABES de CORDOVA / Mme. Lingée sculp. INSCRIPCIONES Y CAPITELES Arabes en CORDOVA / E. Lingée sc., Dormier sc. 2.ª ESTAMPA de INSCRIPCIONES y DETALLES ARABIGOS en GRANADA / E.ce Lingée sculp. DETALLES y INSCRIPCIONES Arabes de GRANADA / D. Pedro Arnal del. ; E. Lingée scupsit

Single prenyl-binding site on protein prenyl transferases

Three distinct protein prenyl transferases, one protein farnesyl transferase (FTase) and two protein geranylgeranyl transferases (GGTase), catalyze prenylation of many cellular proteins. One group of protein substrates contains a C-terminal CAAX motif (C is Cys, A is aliphatic, and X is a variety of amino acids) in which the single cysteine residue is modified with either farnesyl or geranylgeranyl (GG) by FTase or GGTase type-I (GGTase-I), respectively. Rab proteins constitute a second group of substrates that contain a C-terminal double-cysteine motif (such as XXCC in Rab1a) in which both cysteines are geranylgeranylated by Rab GG transferase (RabGGTase). Previous characterization of CAAX prenyl transferases showed that the enzymes form stable complexes with their prenyl pyrophosphate substrates, acting as prenyl carriers. We developed a prenyl-binding assay and show that RabGGTase has a prenyl carrier function similar to the CAAX prenyl transferases. Stable RabGGTase:GG pyrophosphate (GGPP), FTase:GGPP, and GGTase-I:GGPP complexes show 1:1 (enzyme:GGPP) stoichiometry. Chromatographic analysis of prenylated products after single turnover reactions by using isolated RabGGTase:GGPP complex revealed that Rab is mono-geranylgeranylated. This study establishes that all three protein prenyl transferases contain a single prenyl-binding site and suggests that RabGGTase transfers two GG groups to Rabs in independent and consecutive reactions.

The Phosphatidylinositol 3-Phosphate Binding Protein Vac1p Interacts with a Rab GTPase and a Sec1p Homologue to Facilitate Vesicle-mediated Vacuolar Protein Sorting

Activated GTP-bound Rab proteins are thought to interact with effectors to elicit vesicle targeting and fusion events. Vesicle-associated v-SNARE and target membrane t-SNARE proteins are also involved in vesicular transport. Little is known about the functional relationship between Rabs and SNARE protein complexes. We have constructed an activated allele of VPS21, a yeast Rab protein involved in vacuolar protein sorting, and demonstrated an allele-specific interaction between Vps21p and Vac1p. Vac1p was found to bind the Sec1p homologue Vps45p. Although no association between Vps21p and Vps45p was seen, a genetic interaction between VPS21 and VPS45 was observed. Vac1p contains a zinc-binding FYVE finger that may bind phosphatidylinositol 3-phosphate [PtdIns(3)P]. In other FYVE domain proteins, this motif and PtdIns(3)P are necessary for membrane association. Vac1 proteins with mutant FYVE fingers still associated with membranes but showed vacuolar protein sorting defects and reduced interactions with Vps45p and activated Vps21p. Vac1p membrane association was not dependent on PtdIns(3)P, Pep12p, Vps21p, Vps45p, or the PtdIns 3-kinase, Vps34p. Vac1p FYVE finger mutant missorting phenotypes were suppressed by a defective allele of VPS34. These data indicate that PtdIns(3)P may perform a regulatory role, possibly involved in mediating Vac1p protein–protein interactions. We propose that activated-Vps21p interacts with its effector, Vac1p, which interacts with Vps45p to regulate the Golgi to endosome SNARE complex.

Promiscuity in Rab–SNARE Interactions

Fusion of post-Golgi secretory vesicles with the plasma membrane in yeast requires the function of a Rab protein, Sec4p, and a set of v- and t-SNAREs, the Snc, Sso, and Sec9 proteins. We have tested the hypothesis that a selective interaction between Sec4p and the exocytic SNAREs is responsible for ensuring that secretory vesicles fuse with the plasma membrane but not with intracellular organelles. Assembly of Sncp and Ssop into a SNARE complex is defective in a sec4-8 mutant strain. However, Snc2p binds in vivo to many other syntaxin-like t-SNAREs, and binding of Sncp to the endosomal/Golgi t-SNARE Tlg2p is also reduced in sec4-8 cells. In addition, binding of Sncp to Ssop is reduced by mutations in two other Rab genes and four non-Rab genes that block the secretory pathway before the formation of secretory vesicles. In an alternate approach to look for selective Rab–SNARE interactions, we report that the nucleotide-free form of Sec4p coimmunoprecipitates with Ssop. However, Rab–SNARE binding is nonselective, because the nucleotide-free forms of six Rab proteins bind with similar low efficiency to three SNARE proteins, Ssop, Pep12p, and Sncp. We conclude that Rabs and SNAREs do not cooperate to specify the target membrane.