ALBERT — All Library Books, journals and Electronic Records Telegrafenberg

Hits per page

hits 1 - 2 | 2 hits

Sorting

Electronic Resource

Stress-induced transcriptional activation mediated by YAP1 and YAP2 genes that encode the Jun family of transcriptional activators in Saccharomyces cerevisiae (1994)

Hirata, Dai ; Yano, Kiichiro ; Miyakawa, Tokichi

Springer

Molecular genetics and genomics 242 (1994), S. 250-256

add to mindlist on the mindlist

Details

ISSN: 1617-4623

Keywords: Saccharomyces cerevisiae ; Transcriptional activator ; AP-1 ; Stress response

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Abstract The Saccharomyces cerevisiae YAP2 gene encoding an AP-1-like transcriptional activator protein was cloned by selection for genes that confer pleiotropic drug resistance when present in high copy number. The novel YAP2 gene encodes a protein of 45827 daltons and is homologous in part to a known transcriptional activator protein encoded by YAP1/PDR4/SNQ3/PAR1. Homology was found only in both terminal regions. The N-terminal portion contains a region rich in basic amino acids, followed by a “leucine zipper” motif. Overexpression of YAP2 led to the induction of expression of an AP-1 recognition element (ARE)-dependent promoter. The yap1 disruptant has been shown to be sensitive to H2O2. In this study, we demonstrated that the yap1 disruptant is also unable to grow in medium containing 150 μM cadmium, whereas the yap2 disruptant exhibited no significant phenotypes. However, YAP2 in high copy number did suppress cadmium sensitivity, but not H2O2 sensitivity of the yap1 disruptant. YAP1 was able to mediate both cadmium- and H2O2-induced transcriptional activation of an ARE-dependent promoter. A high-copy-number plasmid bearing YAP2 mediated cadmium-induced transcriptional activation of this promoter. The inductions were prevented by the antioxidant N-acetyl-l-cysteine.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1007/BF00280413

Permalink

	Location	Call Number	Expected	Availability

Others were also interested in ...

Paper (German National Licenses)

Fulltext

Electronic Resource

Membrane permeability of bifunctional, amino site-specific, cross-linking reagents (1978)

Miyakawa, Tokichi ; Takemoto, Larry J. ; Fox, C. Fred

New York, N.Y. : Wiley-Blackwell

Journal of Supramolecular Structure 8 (1978), S. 303-310

add to mindlist on the mindlist

Details

ISSN: 0091-7419

Keywords: membrane permeability ; cross-lining reagents ; erythrocyte membrane ; tartryldi(glycylazide) ; dimethyl-3,3′-dithiobispropionimidate ; Life Sciences ; Molecular Cell Biology

Source: Wiley InterScience Backfile Collection 1832-2000

Topics: Biology , Chemistry and Pharmacology , Medicine

Notes: The membrane permeability of a series of reversible cross-linking reagents which are diazide tartarate derivatives has been compared with that of dimethyl-3,3′-dithiobispropionimidate (DTBP). The diazide tartarate derivatives tested include tartryl-diazide (TDA), tartryl-di(glycylazide) (TDGA), tartryl-di(β-alanylazide) (TDAA), tartryl-di-(γ-aminobutyrylazide) (TDBA), tartryl-di (∊-aminocaproylazide) (TDCA). TDA, which has the shortest chain length of the diazide tartarate derivatives tested, proved to be readily permeable through the erythrocyte membrane. When added at equal concentration to unsealed ghosts, TDGA was at least as reactive as DTBP in its ability to cross link the internally displayed proteins 1, 2, 4.1, 4.2, and 6. Treatment of resealed ghosts by DTBP produced oligomeric complexes of these proteins plus apparent homooligomeric complexes of hemoglobin. TDGA at the same concentrations did not cross-link any of these components, indicating its membrane-impermeable nature. As the chain length of the homologous series increased from TDGA to TDCA, the cross-linkers became increasingly permeable through the erythrocyte membrane.

Additional Material: 3 Ill.