ABCC1 p.Ser288Cys
| Predicted by SNAP2: | A: N (87%), C: N (78%), D: N (82%), E: N (87%), F: N (61%), G: N (87%), H: N (82%), I: N (72%), K: N (93%), L: N (72%), M: N (72%), N: N (93%), P: N (78%), Q: N (87%), R: N (87%), T: N (93%), V: N (82%), W: D (53%), Y: D (53%), |
| Predicted by PROVEAN: | A: N, C: D, D: N, E: N, F: D, G: N, H: N, I: D, K: N, L: D, M: N, N: N, P: N, Q: N, R: N, T: N, V: N, W: D, Y: D, |
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[hide] Cadmium-glutathione solution structures provide ne... FEBS J. 2010 Dec;277(24):5086-96. doi: 10.1111/j.1742-4658.2010.07913.x. Epub 2010 Nov 16. Delalande O, Desvaux H, Godat E, Valleix A, Junot C, Labarre J, Boulard Y
Cadmium-glutathione solution structures provide new insights into heavy metal detoxification.
FEBS J. 2010 Dec;277(24):5086-96. doi: 10.1111/j.1742-4658.2010.07913.x. Epub 2010 Nov 16., [PMID:21078121]
Abstract [show]
Cadmium is a heavy metal and a pollutant that can be found in large quantities in the environment from industrial waste. Its toxicity for living organisms could arise from its ability to alter thiol-containing cellular components. Glutathione is an abundant tripeptide (gamma-Glu-Cys-Gly) that is described as the first line of defence against cadmium in many cell types. NMR experiments for structure and dynamics determination, molecular simulations, competition reactions for metal chelation by different metabolites (gamma-Glu-Cys-Gly, alpha-Glu-Cys-Gly and gamma-Glu-Cys) combined with biochemical and genetics experiments have been performed to propose a full description of bio-inorganic reactions occurring in the early steps of cadmium detoxification processes. Our results give unambiguous information about the spontaneous formation, under physiological conditions, of the Cd(GS)(2) complex, about the nature of ligands involved in cadmium chelation by glutathione, and provide insights on the structures of Cd(GS)(2) complexes in solution at different pH. We also show that gamma-Glu-Cys, the precursor of glutathione, forms a stable complex with cadmium, but biological studies of the first steps of cadmium detoxification reveal that this complex does not seem to be relevant for this purpose.
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No. Sentence Comment
176 Experimental procedures Strains and culture conditions The Saccharomyces cerevisiae strain used for the production of 15 N-GSH was S288C (Mata SUC2 mal mel gal2 CUP1).
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ABCC1 p.Ser288Cys 21078121:176:131
status: NEW185 This extract contained soluble yeast metabolites, including 15 N-GSH (S288C strain) and 15 Nc-Glu-Cys (Dgsh2 strain).
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ABCC1 p.Ser288Cys 21078121:185:70
status: NEW206 Strain No treatment 100 lM cadmium S288C 4.4 ± 0.3% 5.9 ± 0.8% BY4742 4.4 ± 0.8% 8.7 ± 0.3% resonances through TOCSY and off-resonance ROESY experiments.
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ABCC1 p.Ser288Cys 21078121:206:35
status: NEW[hide] Saccharomyces cerevisiae contains an RNase MRP tha... Mol Cell Biol. 1992 Jun;12(6):2561-9. Stohl LL, Clayton DA
Saccharomyces cerevisiae contains an RNase MRP that cleaves at a conserved mitochondrial RNA sequence implicated in replication priming.
Mol Cell Biol. 1992 Jun;12(6):2561-9., [PMID:1588958]
Abstract [show]
Yeast mitochondrial DNA contains multiple promoters that sponsor different levels of transcription. Several promoters are individually located immediately adjacent to presumed origins of replication and have been suggested to play a role in priming of DNA replication. Although yeast mitochondrial DNA replication origins have not been extensively characterized at the primary sequence level, a common feature of these putative origins is the occurrence of a short guanosine-rich region in the priming strand downstream of the transcriptional start site. This situation is reminiscent of vertebrate mitochondrial DNA origins and raises the possibility of common features of origin function. In the case of human and mouse cells, there exists an RNA processing activity with the capacity to cleave at a guanosine-rich mitochondrial RNA sequence at an origin; we therefore sought the existence of a yeast endoribonuclease that had such a specificity. Whole cell and mitochondrial extracts of Saccharomyces cerevisiae contain an RNase that cleaves yeast mitochondrial RNA in a site-specific manner similar to that of the human and mouse RNA processing activity RNase MRP. The exact location of cleavage within yeast mitochondrial RNA corresponds to a mapped site of transition from RNA to DNA synthesis. The yeast activity also cleaved mammalian mitochondrial RNA in a fashion similar to that of the mammalian RNase MRPs. The yeast endonuclease is a ribonucleoprotein, as judged by its sensitivity to nucleases and proteinase, and it was present in yeast strains lacking mitochondrial DNA, which demonstrated that all components required for in vitro cleavage are encoded by nuclear genes. We conclude that this RNase is the yeast RNase MRP.
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No. Sentence Comment
65 S. cerevisiae strains used in this study were wild-type strains MH41-7B (a ade his [rho+]), S288C (obtained from the American Type Culture Collection stock center), and BJ2168 (a pep4-3 trpl) (obtained from T. Lisowsky); [rhoo] tester strainD243-4A 18 (a adel lys2, [rho°]) (obtained from T. Lisowsky); and a strain containing a disrupted mtRNA polymerase gene (rpo4l:: Tn:URA3), whose construction has been described in detail elsewhere (15).
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ABCC1 p.Ser288Cys 1588958:65:92
status: NEW241 Lanes: M, HpaII-digested pBR322 DNA; 1, minus-enzyme control; 2 and 3, 1 and 5 p.l of extract from strain MH41-7B; 4 and 5, 1 and 5 pil of extract from strain S288C; 6 and 7, 1 and 5 pul of extract from the strain containing a disrupted mtRNA polymerase gene (15); 8 and 9, 1 and 5 pll of extract from [rhoo] tester strain D243-4A 18. indicating that the observed inactivation is not due to the presence oT an inhibitor generated during micrococcal nuclease digestion.
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ABCC1 p.Ser288Cys 1588958:241:159
status: NEW62 S. cerevisiae strains used in this study were wild-type strains MH41-7B (a ade his [rho+]), S288C (obtained from the American Type Culture Collection stock center), and BJ2168 (a pep4-3 trpl) (obtained from T. Lisowsky); [rhoo] tester strain D243-4A 18 (a adel lys2, [rho&#b0;]) (obtained from T. Lisowsky); and a strain containing a disrupted mtRNA polymerase gene (rpo4l:: Tn:URA3), whose construction has been described in detail elsewhere (15).
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ABCC1 p.Ser288Cys 1588958:62:92
status: NEW240 Lanes: M, HpaII-digested pBR322 DNA; 1, minus-enzyme control; 2 and 3, 1 and 5 p.l of extract from strain MH41-7B; 4 and 5, 1 and 5 pil of extract from strain S288C; 6 and 7, 1 and 5 pul of extract from the strain containing a disrupted mtRNA polymerase gene (15); 8 and 9, 1 and 5 pll of extract from [rhoo] tester strain D243-4A 18. indicating that the observed inactivation is not due to the presence oT an inhibitor generated during micrococcal nuclease digestion.
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ABCC1 p.Ser288Cys 1588958:240:159
status: NEW[hide] A region within a lumenal loop of Saccharomyces ce... Eukaryot Cell. 2003 Jun;2(3):588-98. Mason DL, Mallampalli MP, Huyer G, Michaelis S
A region within a lumenal loop of Saccharomyces cerevisiae Ycf1p directs proteolytic processing and substrate specificity.
Eukaryot Cell. 2003 Jun;2(3):588-98., [PMID:12796304]
Abstract [show]
Ycf1p, a member of the yeast multidrug resistance-associated protein (MRP) subfamily of ATP-binding cassette proteins, is a vacuolar membrane transporter that confers resistance to a variety of toxic substances such as cadmium and arsenite. Ycf1p undergoes a PEP4-dependent processing event to yield N- and C-terminal cleavage products that remain associated with one another. In the present study, we sought to determine whether proteolytic cleavage is required for Ycf1p activity. We have identified a unique region within lumenal loop 6 of Ycf1p, designated the loop 6 insertion (L6(ins)), which appears to be necessary and sufficient for proteolytic cleavage, since L6(ins) can promote processing when moved to new locations in Ycf1p or into a related transporter, Bpt1p. Surprisingly, mutational results indicate that proteolytic processing is not essential for Ycf1p transport activity. Instead, the L6(ins) appears to regulate substrate specificity of Ycf1p, since certain mutations in this region lower cellular cadmium resistance with a concomitant gain in arsenite resistance. Although some of these L6(ins) mutations block processing, there is no correlation between processing and substrate specificity. The activity profiles of the Ycf1p L6(ins) mutants are dramatically affected by the strain background in which they are expressed, raising the possibility that another cellular component may functionally impact Ycf1p activity. A candidate component may be a new full-length MRP-type transporter (NFT1), reported in the Saccharomyces Genome Database as two adjacent open reading frames, YKR103w and YKR104w, but which we show here is present in most Saccharomyces strains as a single open reading frame.
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No. Sentence Comment
203 We also examined the cadmium and arsenite resistance of the Ycf1p mutant proteins expressed from the chromosome in a different strain background, BY4741, which is the parental strain for the yeast knockout collection and a derivative of the strain S288C (17) (Fig. 6).
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ABCC1 p.Ser288Cys 12796304:203:248
status: NEW214 We hypothesized that the nonsense codon might represent a mutation in S288C (the strain used to sequence the genome and the strain from which BY4741 is derived), whereas in SM1058 (also known as EG123 and whose lineage is distinct from S288C [40]), YKR103/104w may actually code a single "full-length" MRP-type transporter homologous throughout its length to Ycf1p and Bpt1p (6).
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ABCC1 p.Ser288Cys 12796304:214:70
status: NEWX
ABCC1 p.Ser288Cys 12796304:214:236
status: NEW216 To examine the possibility that YKR103/104w varies between strains, we used PCR amplification of genomic DNA, followed by DNA sequence analysis to confirm that, in the S288C- FIG. 5.
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ABCC1 p.Ser288Cys 12796304:216:168
status: NEW224 Interestingly, other S. cerevisiae strains, whose lineages derive independently of S288C (SK1 and éa;1278b), and other species of yeast from the wild (S. paradoxus and S. mikatae), also encode the full-length NFT1 gene (Fig. 7B).
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ABCC1 p.Ser288Cys 12796304:224:83
status: NEW268 In the course of our Ycf1p studies, we used two differing strain backgrounds: (i) SM1058, also designated EG123, which is our standard laboratory strain and has a poorly defined lineage (40), and (ii) BY4741, an S288C derivative that is the parental strain for the yeast deletion collection (17).
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ABCC1 p.Ser288Cys 12796304:268:212
status: NEW277 The sequence deposited in SGD for S288C and our sequence results for BY4741 both contain a stop codon (*) at amino acid 1219, whereas other S. cerevisiae strains, as well as additional "wild" yeast strains, contain a tyrosine (Y) and thus code for a full-length ABC transporter.
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ABCC1 p.Ser288Cys 12796304:277:34
status: NEW289 We discovered that in the strain SM1058, YKR103/104w is one continuous ORF rather than two ORFs separated by a nonsense codon, as in the strains BY4741 and S288C (Fig. 7).
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ABCC1 p.Ser288Cys 12796304:289:156
status: NEW291 Interestingly, possession of a full-length NFT1 gene appears to be the "wild-type" situation for yeast, since other S. cerevisiae laboratory strains (éa;1278b and SK1) that differ in lineage from S288C also possess the full-length NFT1 gene, as do other Saccharomyces species (S. paradoxus and S. mikitae).
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ABCC1 p.Ser288Cys 12796304:291:200
status: NEW292 Differences between S288C and other S. cerevisiae strains, as well as other Saccharomyces species, have been reported for a variety of genes, such as the aquaporin genes (9).
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ABCC1 p.Ser288Cys 12796304:292:20
status: NEW293 It is possible that the manner in which S288C was cultivated in the laboratory led to an unintentional selection against the presence of full-length NFT1.
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ABCC1 p.Ser288Cys 12796304:293:40
status: NEW