SNF6 encodes a nuclear protein that is required for expression of many genes in Saccharomyces cerevisiae.

Estruch, Francisco; Carlson, Marian

doi:10.1128/mcb.10.6.2544

Cited by 68 publications

(58 citation statements)

References 43 publications

(33 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The pellet, containing the majority of SNF6HT protein, was suspended in 10 ml of buffer-B containing 0.5% Triton X-100 and 1 M lithum chloride, incubated at 40C for 10 erously provided by C. Peterson and E. Young, respectively. An additional antibody to SNF2, used for the initial monitoring of SNF2 fractionation, was generously provided by M. Carlson.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

A multisubunit complex containing the SWI1/ADR6,SWI2/SNF2, SWI3, SNF5, and SNF6 gene products isolated fromyeast.

Cairns

Kim

Sayre

et al. 1994

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

365

232

View full text Add to dashboard Cite

(7)(8)(9)(10), the GALl gene (which encodes galactokinase) (7), the ADH2 gene (which encodes alcohol dehydrogenase) (7,11,12), and Ty elements (13,14). These SWI and SNF proteins do not appear to contain any DNA-binding motifs, nor have these proteins exhibited any DNA-binding activity in vitro (7,9,15). SWI2/SNF2, however, contains a domain homologous to certain DNA-dependent ATPases, and a recombinant form of this domain exhibits DNAdependent ATPase activity (16)(17)(18). Genetic data suggest that these SWI and SNF proteins form a complex that is recruited to promoter regions through interactions with gene-specific DNA-binding proteins (7,9,19 Hepes-KOH, pH 7.6/20% glycerol/l mM dithiothreitol/l mM. EDTA/2 ,ug of chymostatin per ml/2 puM pepstatin A/0.6 pM leupeptin/2 mM benzamidine/1 mM phenylmethylsulfonyl fluoride/0.01% Nonidet P-40). The purification was monitored by imiunoblot analysis with antisera to SWI1/ADR6, SWI2/SNF2, and SWI3 proteins.Preparation of Recombinant SNF6 Protein. The SNF6 gene was transferred from the plasmid YCp5O-SNF6 to the Escherichia coli expression vector pETliA (Novagen) and tagged with six histidine residues at its carboxyl terminus by means of a polymerase chain reaction with the oligonucleotide primers BCSNF6N (5'-CCCCAGATCTTACATATGGGT-GTCATCAAGAAGAAA-3') and BCSNF6C (5'-CCCG-GATCCTCTAGACTAGTGATGGTGATGGTGATGTC-CAAAAAATACAGCATCAAGATCTCC-3'). The resulting product was digested with Nde I and BamHI and ligated to complementary sites in pETilA to form pET11A-SNF6HT. BL21 (DE3) cells (Novagen) containing the lysozyme-expressing plasmid pLysS (Novagen) were transformed with pET11A-SNF6HT. The transformant was grown at 300C in LB medium (2 liters) containing 100 pRg of ampicillin per ml and 25 ptg of chloramphenicol per ml to an optical density at 600 nm of 0.7. The culture was induced with 0.5 mM isopropyl P-D-thiogalactoside and grown an additional 2 hr.The cells were harvested by centrifugation at 5000 x g for 10 min, washed with 100 ml of 20 mM Hepes (pH 7.5), and suspended in 100 ml of buffer B (20 mM Hepes, pH 7.5/10% glycerol/5 mM 2-mercaptoethanol/l mM EDTA/2 pg of chymostatin per ml/2 pM pepstatin A/0.6 pM leupeptin/2 mM benzamidine/1 mM phenylmethylsulfonyl fluoride), containing 400 mM NaCl. The suspension was lysed by sonication at 40C and centrifuged at 10,000 x g for 10 min.The pellet, containing the majority of SNF6HT protein, was suspended in 10 ml of buffer-B containing 0.5% Triton X-100 and 1 M lithum chloride, incubated at 40C for 10 min, sonicated briefly, and centrifuged at 10,000 x g for 10 m' at 4°C. The pellet was washed three additional times in the same manner and suspended in 1 ml of buffer B containing 50 mM NaCl and 0.5% SDS. The resulting SNF6HT protein was judged to be roughly 95% pure by SDS/PAGE.Antisera. Approximately 4 mg of purified SNF6HT protein was subjected to electrophoresis in a 10% SDS/polyacrylamide gel. The gel was stained with Coomassie brilliant blue R-250, and a slice containing SNF6HT protein was removed. Rabbits were initially immuni...

show abstract

Section: Methodsmentioning

confidence: 99%

“…

…”

mentioning

confidence: 99%

A multisubunit complex containing the SWI1/ADR6,SWI2/SNF2, SWI3, SNF5, and SNF6 gene products isolated fromyeast.

Cairns

Kim

Sayre

et al. 1994

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

365

232

View full text Add to dashboard Cite

show abstract

“…The C terminus, containing an acidic region and a glutamine-rich region, is not absolutely required in vivo for SWI/SNF activity, and the extreme N terminus contains a highly basic region (39). The association of Snf6, unlike Swi2/Snf2, with DNA is not dependent on the packaging of DNA into a nucleosome core particle.…”

Section: Hydrolysis and Not Just Binding Of Atp Is Required For Changmentioning

confidence: 99%

The Interactions of Yeast SWI/SNF and RSC with the Nucleosome before and after Chromatin Remodeling

Sengupta¹,

VanKanegan²,

Persinger³

et al. 2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

Interactions of the yeast chromatin-remodeling complexes SWI/SNF and RSC with nucleosomes were probed using site-specific DNA photoaffinity labeling. 5 S rDNA was engineered with photoreactive nucleotides incorporated at different sites in DNA to scan for the subunits of SWI/SNF in close proximity to DNA when SWI/SNF is bound to the 5 S nucleosome or to the free 5 S rDNA. The Swi2/Snf2 and Snf6 subunits of SWI/SNF were efficiently cross-linked at several positions in the nucleosome, whereas only Snf6 was efficiently cross-linked when SWI/SNF was bound to free DNA. DNA photoaffinity labeling of RSC showed that the Rsc4 subunit is in close proximity to nucleosomal DNA and not when RSC is bound to free DNA. After remodeling, the Swi2/Snf2 and Rsc4 subunits are no longer detected near the nucleosomal DNA and are evidently displaced from the surface of the nucleosome, indicating significant changes in SWI/ SNF and RSC contacts with DNA after remodeling.

show abstract

“…The genes were subsequently cloned by complementation of the phenotype (Abrams et al, 1986;Estruch and Carlson, 1990b). GAMZ was described as a gene required for transcription of the STAI gene which encodes an extracellular glucoamylase of S .…”

Section: Snf2 ( G a M I ) Snfs Snf6mentioning

confidence: 99%

“…The SNF6 gene encodes another highly charged protein of 332 amino acids; the central third of the protein has 45% charged residues, the number of acidic and basic residues being very similar (Estruch and Carlson, 1990b).…”

Section: Snf2 ( G a M I ) Snfs Snf6mentioning

confidence: 99%

Carbon catabolite repression in yeast

Gancedo

1992

European Journal of Biochemistry

410

247

View full text Add to dashboard Cite

Control of gene expression is a basic regulatory mechanism of living organisms. In microorganisms, glucose or other rapidly metabolizable carbon sources repress the expression of genes that code for enzymes related to the metabolism of other carbon sources. This phenomenon, known as catabolite repression, allows microorganisms to cope effectively with changes in the carbon sources present in their environment. In the case of Escherichiu coli, a model to explain at the molecular level the mechanism of catabolite repression has been worked out (Ullmann, 1985;Saier, 1989), although some of its elements remain unidentified.Yeasts are also subject to carbon catabolite repression but the underlying mechanism(s) is less understood than it is in E. coli and we do not yet know how glucose exerts its repressive effect. In the present article I will review information gathered in the last few years on a variety of catabolite-repressible systems, try to integrate it and to elaborate a scheme for carbon catabolite repression consistent with the results obtained. Although this review will be centered around Sacchuromyces cerevisiue, reference to other yeast species will be made when information is available.The degree of repression caused by glucose depends strongly on the enzyme affected and the strain used. As shown in Table 1, it can vary from about 800-fold for invertase to less than 10-fold for aconitase, cytochrome c oxidase or isocitrate dehydrogenase. In most cases, the decrease in enzyme levels caused by glucose is paralleled by a decrease in the concentration of the corresponding mRNA. This could be due to an effect of glucose either on the rate of transcription, or on the stability of the corresponding mRNA or on both.Direct measurements of transcription rates have been performed in only a few cases. For the genes CYCI, encoding iso-1 cytochrome c, and MAL6S, encoding maltase, it was found that derepressed cells synthesized the corresponding mRNAs 6 times and 15 times faster, respectively, than repressed cells (Zitomer et al., 1979;Federoff et al., 1983a). It should be noted that, in the case of maltase, an induction by maltose is superimposed on the process of catabolite repression, but even in the presence of maltose, the addition of glucose to a yeast culture causes an approximately I5-fold decrease in the rate of transcription of the MAL6S gene in Correspondence to J. M. Gancedo,

show abstract

SNF6 encodes a nuclear protein that is required for expression of many genes in Saccharomyces cerevisiae.

Abstract: The SNF6 gene appears to affect transcription from a variety of promoters in Saccharomyces cerevisiae.

Cited by 68 publications

References 43 publications

A multisubunit complex containing the SWI1/ADR6,SWI2/SNF2, SWI3, SNF5, and SNF6 gene products isolated fromyeast.

A multisubunit complex containing the SWI1/ADR6,SWI2/SNF2, SWI3, SNF5, and SNF6 gene products isolated fromyeast.

The Interactions of Yeast SWI/SNF and RSC with the Nucleosome before and after Chromatin Remodeling

Carbon catabolite repression in yeast

Contact Info

Product

Resources

About