Regulation of the Yeast HO Gene

Breeden, Linda; Nasmyth, Kim

doi:10.1101/sqb.1985.050.01.078

Cited by 496 publications

(268 citation statements)

References 1 publication

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“…Initial selection was on synthetic complete (SC) medium lacking Leu, Trp, and adenine. Colonies were tested subsequently for growth on SC medium supplemented with 3 mM 3-amino-1,2,4-triazole and lacking Leu, Trp, and His, and those that grew were assayed using an X-gal filter lift method (Breeden and Nasmyth, 1985). Colonies that passed all three tests were analyzed further.…”

Section: Yeast Two-hybrid Screensmentioning

confidence: 99%

A Cysteine-Rich Extracellular Protein, LAT52, Interacts with the Extracellular Domain of the Pollen Receptor Kinase LePRK2[W]

et al. 2002

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Pollen germination and pollen tube growth are thought to require extracellular cues, but how these cues are perceived and transduced remains largely unknown. Pollen receptor kinases are plausible candidates for this role; they might bind extracellular ligands and thereby mediate cytoplasmic events required for pollen germination and pollen tube growth. To search for pollen-expressed ligands for pollen receptor kinases, we used the extracellular domains of three pollen-specific receptor kinases of tomato (LePRK1, LePRK2, and LePRK3) as baits in a yeast two-hybrid screen. We identified numerous secreted or plasma membrane-bound candidate ligands. One of these, the Cys-rich protein LAT52, was known to be essential during pollen hydration and pollen tube growth. We used in vivo coimmunoprecipitation to demonstrate that LAT52 was capable of forming a complex with LePRK2 in pollen and to show that the extracellular domain of LePRK2 was sufficient for the interaction. Soluble LAT52 can exist in differently sized forms, but only the larger form can interact with LePRK2. We propose that LAT52 might be a ligand for LePRK2.

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Section: Yeast Two-hybrid Screensmentioning

confidence: 99%

A Cysteine-Rich Extracellular Protein, LAT52, Interacts with the Extracellular Domain of the Pollen Receptor Kinase LePRK2[W]

et al. 2002

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“…Double transformants were plated on yeast drop-out medium lacking tryptophan and leucine (Sherman et al, 1986). They were grown for 3 days at 308C and then colonies were patched on the same medium and replica-plated on Whatman 40 ®lters, to test the bgalactosidase activity (Breeden and Nasmyth, 1985), and on yeast drop-out media lacking tryptophan and leucine and supplemented with 5 mM 3-amino-1,2,4-triazole (Sherman et al, 1986) (the Gal4-Grb3-3 fusion protein had a weak transcriptional activity if yeast grew only in selective medium). Positive clones were rescued and tested for speci®city by retransformation into Hf7c either with pGBT-Grb3-3 or with irrelevant targets.…”

Section: Two-hybrid Screenmentioning

confidence: 99%

hpttg, a human homologue of rat pttg, is overexpressed in hematopoietic neoplasms. Evidence for a transcriptional activation function of hPTTG

et al. 1998

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We have isolated a human cDNA clone encoding a novel protein of 22 kDa that is a human counterpart of the rat oncoprotein PTTG. We show that the corresponding gene (hpttg) is overexpressed in Jurkat cells (a human T lymphoma cell line) and in samples from patients with di erent kinds of hematopoietic malignancies. Analysis of the sequence showed that hPTTG has an aminoterminal basic domain and a carboxyl-terminal acidic domain, and that it is a proline-rich protein with several putative SH3-binding sites. Subcellular fractionation studies show that, although hPTTG is mainly a cytosolic protein, it is partially localized in the nucleus. In addition we demonstrate that the acidic carboxyl-terminal region of hPTTG acts as a transactivation domain when fused to a heterologous DNA binding domain, both in yeast and in mammalian cells.

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“…HF7c-DEWS was transformed with the pACT-cDNA library (Durfee et al, 1993) and spread on his 7 , leu 7 , trp 7 selective media containing 30 mM 3-aminotriazole. After 5 days at 308C histidine prototroph clones were restreaked and single colonies were tested for b-galactosidase activity (Breeden and Nasmyth, 1985). Positive (blue) clones were grown in leu 7 selective broth to allow for loss of pGBT-ESWD82 ± 246, approximately 200 cells were spread on leu 7 selective plates and after 3 days replicata-plated on SC-trp plates.…”

Section: Yeast Two-hybrid Interaction Trap Cloningmentioning

confidence: 99%

Oncogenic EWS-Fli1 interacts with hsRPB7, a subunit of human RNA polymerase II

et al. 1998

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As a result of the t(11;22)(q24;q12) chromosomal translocation characterizing the Ewing family of tumors (ET), the amino terminal portion of EWS, an RNA binding protein of unknown function, is fused to the DNA-binding domain of the ets transcription factor Fli1. The hybrid EWS-Fli1 protein acts as a strong transcriptional activator and, in contrast to wildtype Fli1, is a potent transforming agent. Similar rearrangements involving EWS or the highly homologous TLS with various transcription factors have been found in several types of human tumors. Employing yeast twohybrid cloning we isolated the seventh largest subunit of human RNA polymerase II (hsRPB7) as a protein that speci®cally interacts with the amino terminus of EWS. This association was con®rmed by in vitro immunocoprecipitation. In nuclear extracts, hsRPB7 was found to copurify with EWS-Fli1 but not with Fli1. Overexpression of recombinant hsRPB7 speci®cally increased gene activation by EWS-chimeric transcription factors. Replacement of the EWS portion by hsRPB7 in the oncogenic fusion protein restored the transactivating potential of the chimera. Our results suggest that the interaction of the amino terminus of EWS with hsRPB7 contributes to the transactivation function of EWS-Fli1 and, since hsRPB7 has characteristics of a regulatory subunit of RNA polymerase II, may in¯uence promoter selectivity.

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Regulation of the Yeast HO Gene

Cited by 496 publications

References 1 publication

A Cysteine-Rich Extracellular Protein, LAT52, Interacts with the Extracellular Domain of the Pollen Receptor Kinase LePRK2[W]

A Cysteine-Rich Extracellular Protein, LAT52, Interacts with the Extracellular Domain of the Pollen Receptor Kinase LePRK2[W]

hpttg, a human homologue of rat pttg, is overexpressed in hematopoietic neoplasms. Evidence for a transcriptional activation function of hPTTG

Oncogenic EWS-Fli1 interacts with hsRPB7, a subunit of human RNA polymerase II

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