295 research outputs found
Complex transcriptional regulation of the Saccharomyces cerevisiae CYB2 gene encoding cytochrome b2: CYP1(HAP1) activator binds to the CYB2 upstream activation site UAS1-B2.
No full textRegolazione del gene JEN1, codificante la lattato permeasi, nel lievito Saccharomyces cerevisiae
No full textCo-ordinated regulation of lactate metabolism genes in yeast: role of lactate permease gene JEN1
No full textEffect of HAP1 and HAP2-3-4-5 complex on the expression of DLD gene encoding the mitochondrial protein D-lactate ferricytochrome c oxidoreductase in Saccharomyces cerevisiae
No full text
Regulation of the CYB2 gene expression: transcriprtion co-ordination by the Hap1p, Hap2/3/4 and Adr1p transcription factors
No full textMolecular Microbiolog
Leçons cliniques sur les affections chirurgicales de la vessie et de la prostate, professées à l'hôpital Necker par J.-C.-Félix Guyon,... recueillies et publiées par le Dr F.-P. Guiard,...
No full textContient une table des matièresAvec mode text
Numerical vs. physical quantities in the Fitts paradigm of <b>Eq. 8</b>.
No full text<p>Numerical vs. physical quantities in the Fitts paradigm of <b>Eq. 8</b>.</p
Protein folding causes an arrest of preprotein translocation into mitochondria in vivo
No full textWith vital yeast cells, a hybrid protein consisting of the amino- terminal third of the precursor to cytochrome b2 and of the entire dihydrofolate reductase was arrested on the import pathway into mitochondria. Accumulation of the protein in the mitochondrial membranes was achieved by inducing a stable tertiary structure of the dihydrofolate reductase domain. Thereby, three salient features of mitochondrial protein uptake in vivo were demonstrated: its posttranslational character; the requirement for unfolding of precursors; and import through translocation contact sites. The permanent occupation of translocation sites by the fusion protein inhibited the import of other precursors; it did, however, not lead to leakage of mitochondrial ions, implying the existence of a channel that is sealed around the membrane spanning polypeptide segment
How the four <i>ID</i>s of <b>Eqs. 3</b>–6 vary in the experimentally practicable range of relative tolerance.
No full text<p>How the four <i>ID</i>s of <b>Eqs. 3</b>–6 vary in the experimentally practicable range of relative tolerance.</p
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