Cloning of human and bovine homologs of SNF2/SWI2: a global activator of transcription in yeast<i>S.cerevisiae</i>

Okabe, Ichiro; Bailey, Leonard C.; Attree, Olivier; Srinivasan, Sudha; Perkel, Jeffrey M.; Laurent, Brehon C.; Carlson, Marian; Nelson, David L.; Nussbaum, Robert L.

doi:10.1093/nar/20.17.4649

Cited by 97 publications

(68 citation statements)

References 21 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…36 We found that the expression of Smarca1 mRNA and protein peaked at passages 8-9, followed by a decline after p53LOH was attained in the majority of the population (Figures 7c-e). No change in the expression patterns of other major chromatin remodelers, 36 such as Smarca2, Smarca4 and Smarca5, was observed (Supplementary Figure 9). This indicates a unique correlation between Smarca1 expression and p53LOH.…”

Section: Resultsmentioning

confidence: 77%

The onset of p53 loss of heterozygosity is differentially induced in various stem cell types and may involve the loss of either allele

et al. 2014

View full text Add to dashboard Cite

1,5 p53 loss of heterozygosity (p53LOH) is frequently observed in Li-Fraumeni syndrome (LFS) patients who carry a mutant (Mut) p53 germ-line mutation. Here, we focused on elucidating the link between p53LOH and tumor development in stem cells (SCs). Although adult mesenchymal stem cells (MSCs) robustly underwent p53LOH, p53LOH in induced embryonic pluripotent stem cells (iPSCs) was significantly attenuated. Only SCs that underwent p53LOH induced malignant tumors in mice. These results may explain why LFS patients develop normally, yet acquire tumors in adulthood. Surprisingly, an analysis of single-cell sub-clones of iPSCs, MSCs and ex vivo bone marrow (BM) progenitors revealed that p53LOH is a bi-directional process, which may result in either the loss of wild-type (WT) or Mut p53 allele. Interestingly, most BM progenitors underwent Mutp53LOH. Our results suggest that the bi-directional p53LOH process may function as a cell-fate checkpoint. The loss of Mutp53 may be regarded as a DNA repair event leading to genome stability. Indeed, gene expression analysis of the p53LOH process revealed upregulation of a specific chromatin remodeler and a burst of DNA repair genes. However, in the case of loss of WTp53, cells are endowed with uncontrolled growth that promotes cancer.

show abstract

Section: Resultsmentioning

confidence: 77%

The onset of p53 loss of heterozygosity is differentially induced in various stem cell types and may involve the loss of either allele

et al. 2014

View full text Add to dashboard Cite

show abstract

“…Furthermore, chromatin structure on the SUC2 promoter is altered in snJ2 and sniS mutants (38). Finally, homologs of SWI2/SNF2 have been identified in yeast (16,17), Drosophila (39,40), mouse (41), and humans (42,43), and the protein encoded by the Drosophila brm gene appears to affect the transcription of several genes by assisting in the remodeling of chromatin structure (44). Thus, complexes analogous to the yeast SWP complex may help in general to mediate the transition from the repressed to the derepressed state of chromatin.…”

Section: Discussionmentioning

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.

361

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

“…Most of these are ered to a synthetic DNA-binding domain, hSNF2L is unable to important regulatory factors in several pathways of gene expresactivate the transcription of a reporter gene or to complement sion. Saccharomyces cerevisiae Snf2 has been shown to form a snf2 mutations in S. cerevisiae [15]. Conversely, hSNF2L and multiprotein complex, Snf/Swi, together with Swi1, Swi3, Snf5…”

mentioning

confidence: 99%

Identification of a human 17p‐located cDNA encoding a protein of the Snf2‐like helicase family

Aubry

Matteï

Galibert

1998

European Journal of Biochemistry

View full text Add to dashboard Cite

Following immunoscreening, we have cloned and sequenced a human cDNA encoding a novel member of the expanding helicase family. The deduced protein, designated hZFH (human zinc-finger helicase), contains the seven domains conserved among the helicase superfamily II and four potential zinc-fingers motifs. In particular, hZFH shows significant similarity to some proteins of the Snf2-like family, known to act as transcriptional regulators for multiples genes. Furthermore, hZFH has 68.5% identity to a human Mi-2 autoantigen to which autoantibodies are produced by a subgroup of patients affected by dermatomyositis. Northern-blot analyses have revealed several hZFH mRNAs with quantitative differences in various human tissues. One alternative splice site of hZFH mRNA was demonstrated and others were predicted. We also report the chromosomal localization of gene hZFH to locus 17p13-17p12 by in situ hybridization. Thus, this novel gene appears as a candidate for several malignant and genetic diseases associated with this region of the genome. The combination of these features suggests that hZFH plays an important role in gene regulation.Keywords : helicase ; human; cDNA; autoimmunity; chromosomal localization.Helicases constitute a large family of enzymes endowed with tional activation of a large set of inducible genes [7, 8]. These factors are believed to enhance transcription by assisting on ATPase activity and involved in double-stranded DNA and RNA unwinding. Numerous processes of nucleic acid metabolism, in-gene-specific activators in relieving repression, probably via an alteration of the chromatin structure [6, 9, 10]. cluding DNA replication, DNA repair, transcription, RNA splicing and translation require DNA and/or RNA helicases [1Ϫ3].Snf/Swi homologs have now been identified in Drosophila, mouse and human, suggesting a conserved role throughout euDespite the diversity of their physiological functions and the wide range of organisms in which they have been found, pro-karyotes in transcriptional activation. The human homolog, called hBRM, is 56% identical to brahma (also called brm), a nounced sequence conservation was maintained in helicase families. On the basis of different sequence signatures, the members regulator of homeotic genes in Drosophila [11], and 33% identical to yeast Snf2. hBRM was shown to be a strong activator of this protein family are subdivided into superfamilies I, II and III [4, 5]. Each protein of superfamilies I and II contains seven of transcription when tethered to DNA through fusion with a specific DNA-binding domain [12]. Moreover, hBRM (also highly conserved motifs (I, Ia, IIϪVI) termed helicase domains, clustered in a region of 200Ϫ700 amino acids. The similarity known as hSNF2A) and a strikingly related (75% identity) protein, BRG1 (also known as hSNF2β), can function as two tranin the structure and arrangement of these motifs suggests that superfamilies I and II have evolved from a common ances-scriptional coactivators cooperating with the estrogen, the glucocorticoid and the retin...

show abstract

Cloning of human and bovine homologs of SNF2/SWI2: a global activator of transcription in yeastS.cerevisiae

Cited by 97 publications

References 21 publications

The onset of p53 loss of heterozygosity is differentially induced in various stem cell types and may involve the loss of either allele

The onset of p53 loss of heterozygosity is differentially induced in various stem cell types and may involve the loss of either allele

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

Identification of a human 17p‐located cDNA encoding a protein of the Snf2‐like helicase family

Contact Info

Product

Resources

About