Isolation of a class C transcription factor which forms a stable complex with tRNA genes.

Ruet, Anny; Camier, Sylvie; Smagowicz, Wiesław J.; Sentenac, André; Fromageot, P.

doi:10.1002/j.1460-2075.1984.tb01809.x

Cited by 123 publications

(74 citation statements)

References 33 publications

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“…Assays were performed as described previously (24) using purified protein extracts obtained from heparin-Sepharose chromatography (25). Proteins were extracted from yeast strain BWG1-7A, purified, and incubated with 40-base pair DNA fragments harboring the glycine regulatory region of GCV2.…”

Section: Gel Mobility Shift Assaymentioning

confidence: 99%

Regulation of the Balance of One-carbon Metabolism inSaccharomyces cerevisiae

Piper¹,

Hong²,

Ball³

et al. 2000

Journal of Biological Chemistry

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One-carbon metabolism in yeast is an essential process that relies on at least one of three one-carbon donor molecules: serine, glycine, or formate. By a combination of genetics and biochemistry we have shown how cells regulate the balance of one-carbon flow between the donors by regulating cytoplasmic serine hydroxymethyltransferase activity in a side reaction occurring in the presence of excess glycine. This control governs the level of 5,10-methylene tetrahydrofolate (5,10-CH 2 -H 4 folate) in the cytoplasm, which has a direct role in signaling transcriptional control of the expression of key genes, particularly those encoding the unique components of the glycine decarboxylase complex (GCV1, GCV2, and GCV3). Based on these and other observations, we propose a model for how cells balance the need to supplement their one-carbon pools when charged folates are limiting or when glycine is in excess. We also propose that under normal conditions, cytoplasmic 5,10-CH 2 -H 4 folate is mainly directed to generating methyl groups via methionine, whereas one-carbon units generated from glycine in mitochondria are more directed to purine biosynthesis. When glycine is in excess, 5,10-CH 2 -H 4 folate is decreased, and the regulation loop shifts the balance of generation of one-carbon units into the mitochondrion.

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Section: Gel Mobility Shift Assaymentioning

confidence: 99%

Regulation of the Balance of One-carbon Metabolism inSaccharomyces cerevisiae

Piper¹,

Hong²,

Ball³

et al. 2000

Journal of Biological Chemistry

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“…The TFIIIB factor was partially purified on a heparin-ultrogel (Pharmacia) column from cells expressing the wild type or a modified copy of PCF4 as described (31,32). Heparin-ultrogel fractions containing TFIIIB activity were pooled and used for affinity purification (see Figure 2).…”

Section: Tfiib' Fractionationmentioning

confidence: 99%

Interactions between yeast TFIIIB components

Huet¹,

Conesa²,

Manaud³

et al. 1994

Nucl Acids Res

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“…The selective recognition of the tRNA genes by this ©IRL Press machinery rests on the presence of two conserved intragenic sequence elements, the A and B blocks, which correspond to the invariant bases of the D and TICG loops of tRNAs (Ciliberto et al, 1983;Geiduschek and Tocchini-Valentini, 1988). As a primary step of gene activation, the promoting sequences are recognized by transcription factor TFIHC, or T in the yeast system, in the absence of any other transcriptional component (Lassar et al, 1983;Ruet et al, 1984). Factor TFIIIB contributes to the stability of TFIIIC -DNA complexes and is required for transcription complex formation.…”

Section: Introductionmentioning

confidence: 99%

“…It does not bind to DNA by itself (Klekamp and Weil, 1986;Waldschmidt et al, 1988). Yeast factor r and its interaction with tDNA have been extensively studied (Klementz et al, 1982;Ruet et al, 1984). Nuclease protection and methylation experiments (Camier et al, 1985;Stillman et al, 1985a), as well as point mutation analyses (Baker and Hall, 1984;Baker et al, 1986), have demonstrated the specific binding of r to the A and B blocks, the involvement of critical bases and the prominent role of the B block sequence in complex formation.…”

Section: Introductionmentioning

confidence: 99%

The two DNA-binding domains of yeast transcription factor tau as observed by scanning transmission electron microscopy.

et al. 1989

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Yeast transcription factor X interacts with the intragenic promoter of tRNA genes, binding to both the A and B block elements. Affinity-purified r factor and r-tDNA complexes were examined by scanning transmission electron microscopy to analyze the structural features of free and DNA bound factor. The free factor appeared as two tightly associated globular domains of roughly similar size (10 nm in diameter) and mass ( -300 kd).A combination of these two domains results in a mass for the factor of 510-670 kd. When r was allowed to interact with recombinant tRNA3Leu genes with variable A block-B block spacing, different structures were observed. With short genes, the two globular domains were not resolved and T appeared as a large particle covering the A and B block region. On the other hand, with genes having a larger A-B distance (53 or 74 bp), mostly dumb-bell-shaped complexes were formed with individualized factor domains bound separately to the A and B blocks. A smaller proportion of the complexes appeared to consist of a large particle bound at only one site, essentially on the B block. Mapping of the binding domains in the DNA showed a good correlation with the respective positions of the A and B promoter elements. Factor binding did not induce a noticeable DNA bending, although with extended genes apparent DNA shortening and cases of DNA looping were observed. Upon cleavage of the tRNA3 uu gene between the A and B blocks after or prior to complex formation, the two factor domains remained attached to the same DNA fragment (mostly the B-DNA fragment). In addition, images of proteinlinked, reconstituted full-length genes were also observed. These different conformational states of the r-tDNA complexes probably reflect the dynamic aspect of the interaction of the factor with its DNA target.

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Isolation of a class C transcription factor which forms a stable complex with tRNA genes.

Cited by 123 publications

References 33 publications

Regulation of the Balance of One-carbon Metabolism inSaccharomyces cerevisiae

Regulation of the Balance of One-carbon Metabolism inSaccharomyces cerevisiae

Interactions between yeast TFIIIB components

The two DNA-binding domains of yeast transcription factor tau as observed by scanning transmission electron microscopy.

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