A Nitrilase-Like Protein Interacts with GCC Box DNA-Binding Proteins Involved in Ethylene and Defense Responses1

Ethylene-responsive element-binding proteins (EREBPs) of tobacco (Nicotiana tabacum L.) bind to the GCC box of many pathogenesis-related (PR) gene promoters, including osmotin (PR-5). The two GCC boxes on the osmotin promoter are known to be required, but not sufficient, for maximal ethylene responsiveness. EREBPs participate in the signal transduction pathway leading from exogenous ethylene application and pathogen infection to PR gene induction. In this study EREBP3 was used as bait in a yeast two-hybrid interaction trap with a tobacco cDNA library as prey to isolate signal transduction pathway intermediates that interact with EREBPs. One of the strongest interactors was found to encode a nitrilase-like protein (NLP). Nitrilase is an enzyme involved in auxin biosynthesis. NLP interacted with other EREBP family members, namely tobacco EREBP2 and tomato (Lycopersicon esculentum L.) Pti4/5/6. The EREBP2-EREBP3 interaction with NLP required part of the DNA-binding domain. The specificity of interaction was further confirmed by protein-binding studies in solution. We propose that the EREBP-NLP interaction serves to regulate PR gene expression by sequestration of EREBPs in the cytoplasm.

CENP-C reshapes and stabilizes CENP-A nucleosomes at the centromere

Inheritance of each chromosome depends upon its centromere. A histone H3 variant, centromere protein A (CENP-A), is essential for epigenetically marking centromere location. We find that CENP-A is quantitatively retained at the centromere upon which it is initially assembled. CENP-C binds to CENP-A nucleosomes and is a prime candidate to stabilize centromeric chromatin. Using purified components, we find that CENP-C reshapes the octameric histone core of CENP-A nucleosomes, rigidifies both surface and internal nucleosome structure, and modulates terminal DNA to match the loose wrap that is found on native CENP-A nucleosomes at functional human centromeres. Thus, CENP-C affects nucleosome shape and dynamics in a manner analogous to allosteric regulation of enzymes. CENP-C depletion leads to rapid removal of CENP-A from centromeres, indicating their collaboration in maintaining centromere identity.

Evaluation of the standard sampling technique for suspended solids /

Mode of access: Internet.

Planning water supply : cost-rate differentials and plumbing permits /

Mode of access: Internet.

Dredging alternatives study Cubits Gap, Lower Mississippi River.

Cover title.

Houston-Galveston Navigation Channels, Texas Project.

"July 1995."

Houston-Galveston Navigation Channels, Texas Project.

"September 1995."

Space station : leadership for the future /

Cover title.

Solid-state metallurgy studies of pure columbium and Cb-1 Zr alloy /

"Contract AT(11-1)-229."

Day camping for developmentally disabled and exceptional children /

On cover: Guidelines for establishing day camp programs.

Histoire de l'admirable Don Quichotte de la Manche.

François Filleau de Saint Martin's translation, including his continuation (v. 5-6) Cf. Barcelona. Biblioteca Central. Catàleg de la col-ecció, 1916, v. 1, no. 323.

Histoire de l'admirable Don Quichotte de la Manche : en vi. volumes.

Vols. 5-6 described by Plaza Escudero, no. 2303 as having 9, 7 plates.

Histoire de l'admirable Don Quixotte de la Manche.

Vol. 2 has imprint date: 1595 [i.e. 1695].

Histoire de l'admirable Don Quichotte de la Manche,

Translated by François Filleau de Saint-Martin. Cf. Leopolde Rius y de Llosellas, Bibliografía crítica, 1895-1905, v. 1, no. 484.