II. Yeast sequencing reports. The complete sequence of a 33 kb fragment on the right arm of chromosome II fromSaccharomyces cerevisiae reveals 16 open reading frames, including ten new open reading frames, five previously identified genes and a homologue of theSCO1 gene

Smits, Paul H.M.; Haan, M. de; Maat, C.; Grivell, Leslie A.

doi:10.1002/yea.320100010

Cited by 37 publications

(27 citation statements)

References 24 publications

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“…DTT was added to the apoprotein in a 10 mM concentration to reduce the Cys residues of the CPXXCP motif before metal reconstitution. The Cu(I), Cu(II), Ni(II) metallated forms were obtained by addition of stoichiometric amounts of the metal ions {as [Cu(I)(CH 3 CN) 4 ]PF 6 , CuSO 4 , and NiCl 2 } to diluted protein solutions in 50 mM phosphate buffer at pH 7.2, followed by protein concentration under nitrogen atmosphere. The metal content was finally determined by inductively coupled plasma MS.…”

Section: Methodsmentioning

confidence: 99%

“…In the bacterial operons, Sco proteins often are associated with copper enzymes, suggesting that they are involved in the maturation or functioning of such enzymes (1). Eukaryotic genomes contain two paralogs, Sco1 and Sco2 (3,4), both involved in copper-dependent assembly of cytochrome c oxidase (CcO) (5). CcO contains two functional copper ions located in the binuclear Cu A site and one located in the binuclear Cu B -heme a 3 site (6).…”

mentioning

confidence: 99%

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A hint for the function of human Sco1 from different structures

Banci

Bertini

Calderone

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

101

162

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The solution structures of apo, Cu(I), and Ni(II) human Sco1 have been determined. The protein passes from an open and conformationally mobile state to a closed and rigid conformation upon metal binding as shown by electrospray ionization MS and NMR data. The metal ligands of Cu(l) are two Cys residues of the CPXXCP motif and a His residue. The latter is suitably located to coordinate the metal anchored by the two Cys residues. The coordination sphere of Ni(II) in solution is completed by another ligand, possibly Asp. Crystals of the Ni(II) derivative were also obtained with the Ni(II) ion bound to the same His residue and to the two oxidized Cys residues of the CPXXCP motif. We propose that the various structures solved here represent the various states of the protein in its functional cycle and that the metal can be bound to the oxidized protein at a certain stage. Although it now seems reasonable that Sco1, which is characterized by a thioredoxin fold, has evolved to bind a metal atom via the di-Cys motif to act as a copper chaperone, the oxidized form of the nickel-bound protein suggests that it may also maintain the thioredoxin function

show abstract

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

A hint for the function of human Sco1 from different structures

Banci

Bertini

Calderone

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

101

162

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“…Plasmid structures of YEp30 and its derivatives are shown in Fig. 1 (27). Wild-type yeast and cdg1 mutant cell cultures were maintained in YEPD (1% bacto-yeast extract, 2% bactopeptone, and 2% dextrose).…”

Section: Methodsmentioning

confidence: 99%

Reduction of CDP-diacylglycerol Synthase Activity Results in the Excretion of Inositol by Saccharomyces cerevisiae

Shen

Dowhan

1996

Journal of Biological Chemistry

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3 Tyr substitution) within the CDS1 gene (encodes CDP-DAG synthase) of this mutant. Expression of CDP-DAG synthase activity from a plasmid-borne copy of the CDS1 gene in the cdg1 mutant was not down-regulated, and this expression also corrected the inositol excretion phenotype. Introduction of the above mutated gene (CDS1*) controlled by its endogenous promoter on a single copy plasmid into a cds1-null background reconstituted a transformant with the cdg1 phenotype, including reduced CDP-DAG synthase activity, elevated phosphatidylserine synthase activity, and inositol excretion into the growth medium. Expression of CDS1* in a single copy in the cdg1 mutant raised CDP-DAG synthase activity from 15 to 30% of derepressed wild-type yeast levels but still did not correct the inositol excretion phenotype. CDP-DAG synthase activity was not regulated in response to precursors of phospholipid biosynthesis in the cdg1 mutant either with or without a trans copy of the CDS1* gene. An open reading frame was identified 5 to the CDS1 locus, YBR0314, which also resulted in inositol excretion when present in trans in multiple copies.

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“…Secondary structure prediction of the region in Sco1 and Sco2 prior to the transmembrane domain was not considered relevant for this figure. The sequences are the following: Sco2 (S. cerevisiae) (46), Sco1 (S. cerevisiae) (39), PrrC (R. sphaeroides), Msp5 (Anaplasma marginale) (51), Imm (Cowdria ruminantium) (31), and Orf193 (Pseudomonas stutzeri) (11). Dots were spaced every 10 residues.…”

Section: Vol 177 1995 Oxygen Regulation Of Gene Expression In R Spmentioning

confidence: 99%

Oxygen-insensitive synthesis of the photosynthetic membranes of Rhodobacter sphaeroides: a mutant histidine kinase

Eraso¹,

Kaplan²

1995

J Bacteriol

121

204

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Two new loci, prrB and prrC, involved in the positive regulation of photosynthesis gene expression in response to anaerobiosis, have been identified in Rhodobacter sphaeroides. prrB encodes a sensor histidine kinase that is responsive to the removal of oxygen and functions through the response regulator PrrA. Inactivation of prrB results in a substantial reduction of photosynthetic spectral complexes as well as in the inability of cells to grow photosynthetically at low to medium light intensities. Together, prrB and prrA provide the major signal involved in synthesis of the specialized intracytoplasmic membrane (ICM), harboring components essential to the light reactions of photosynthesis. Previously, J. K. Lee and S. Kaplan (J. Bacteriol. 174:1158-1171, 1992) identified a mutant which resulted in high-level expression of the puc operon, encoding the apoproteins giving rise to the B800-850 spectral complex, in the presence of oxygen as well as in the synthesis of the ICM under conditions of high oxygenation. This mutation is shown to reside in prrB, resulting in a leucine-to-proline change at position 78 in mutant PrrB (PRRB78). Measurements of mRNA levels in cells containing the prrB78 mutation support the idea that prrB is a global regulator of photosynthesis gene expression. Two additional mutants, PRRB1 and PRRB2, which make two truncated forms of the PrrB protein, possess substantially reduced amounts of spectral complexes. Although the precise role of prrC remains to be determined, evidence suggests that it too is involved in the regulatory cascade involving prrB and prrA. The genetic organization of the photosynthesis response regulatory (PRR) region is discussed.Rhodobacter sphaeroides is a purple, nonsulfur photoheterotrophic bacterium whose mode of growth depends on the concentration of oxygen in the surrounding environment (49). At high oxygen concentrations, R. sphaeroides grows chemoheterotrophically, and morphologically it resembles a typical gram-negative bacterium (3). Under low oxygen or anaerobiosis, the photosynthetic membrane system, designated the intracytoplasmic membrane (ICM), is induced; the ICM fills the interior of the cell, and its abundance is inversely related to the incident light intensity (25). The ICM contains all of the structural and functional components of the photosynthetic apparatus. Included are three distinct bacteriochlorophyll (Bchl) a pigment-protein complexes: the photochemical reaction center (RC) (36) and the two light-harvesting complexes, designated the B800-850 and B-875 spectral complexes (7, 9). When grown anaerobically in the dark, in the presence of alternative electron acceptors, the gratuitous synthesis of the ICM occurs (53).Lee and Kaplan (28) provided the first demonstration that a relatively simple switching mechanism must be involved in the repression of photosynthesis gene expression by oxygen in the genus Rhodobacter when they isolated the spontaneous mutant T 1a , which accumulates photosynthetic membranes in the presence of high oxygen. Subsequen...

show abstract

II. Yeast sequencing reports. The complete sequence of a 33 kb fragment on the right arm of chromosome II fromSaccharomyces cerevisiae reveals 16 open reading frames, including ten new open reading frames, five previously identified genes and a homologue of theSCO1 gene

Cited by 37 publications

References 24 publications

A hint for the function of human Sco1 from different structures

A hint for the function of human Sco1 from different structures

Reduction of CDP-diacylglycerol Synthase Activity Results in the Excretion of Inositol by Saccharomyces cerevisiae

Oxygen-insensitive synthesis of the photosynthetic membranes of Rhodobacter sphaeroides: a mutant histidine kinase

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