HAP4, the glucose‐repressed regulated subunit of the HAP transcriptional complex involved in the fermentation–respiration shift, has a functional homologue in the respiratory yeast <i>Kluyveromyces lactis</i>

Bourgarel, D; Nguyen, Chi-Hung; Bolotin‐Fukuhara, Monique

doi:10.1046/j.1365-2958.1999.01263.x

Cited by 53 publications

(60 citation statements)

References 56 publications

(83 reference statements)

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“…To address this possibility, protein-protein interaction studies were performed in VOL. 4,2005 Hap2p/Hap3p/Hap4p/Hap5p-DNA COMPLEX 1833 on May 9, 2018 by guest http://ec.asm.org/ the presence of a 37-bp double-stranded DNA oligonucleotide containing the sequence of the CCAAT site from CYC1 UAS2UP or an identical control DNA in which the CCAAT site was mutated to GGAAG to abolish binding by Hap2p/ Hap3p/Hap5p (Fig. 2B).…”

Section: Resultsmentioning

confidence: 99%

“…The first activation domain was mapped between amino acid residues 124 and 329, and a sec-VOL. 4,2005 Hap2p/Hap3p/Hap4p/Hap5p-DNA COMPLEX 1837…”

Section: Discussionmentioning

confidence: 99%

“…For several years, Hap4p homologs were not found in other yeast or fungi; however, recent studies have revealed that homologs exist in Kluyveromyces lactis (4) and Hansenula polymorpha (51). These Hap4p homologs were shown to functionally complement an S. cerevisiae hap4⌬ mutant in spite of the fact that the homology between these proteins was limited to a 16-amino-acid domain (4,51).…”

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confidence: 99%

“…These Hap4p homologs were shown to functionally complement an S. cerevisiae hap4⌬ mutant in spite of the fact that the homology between these proteins was limited to a 16-amino-acid domain (4,51). Nevertheless, once this conserved region was identified, it became apparent that Hap4p-like proteins exist in many different yeasts and fungi (51).…”

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confidence: 99%

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Assembly of the Hap2p/Hap3p/Hap4p/Hap5p-DNA Complex in Saccharomyces cerevisiae

McNabb

Pinto

2005

Eukaryot Cell

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The CCAAT-binding factor (CBF) is an evolutionarily conserved multimeric transcriptional activator in eukaryotes. In Saccharomyces cerevisiae, the CCAAT-binding factor is composed of four subunits, termed Hap2p, Hap3p, Hap4p, and Hap5p. The Hap2p/Hap3p/Hap5p heterotrimer is the DNA-binding component of the complex that binds to the consensus 5-CCAAT-3 sequence in the promoter of target genes. The Hap4p subunit contains the transcriptional activation domain necessary for stimulating transcription after interacting with Hap2p/Hap3p/Hap5p. In this report, we demonstrate that Hap2p, Hap3p, and Hap5p assemble via a one-step pathway requiring all three subunits simultaneously, as opposed to the mammalian CCAAT-binding factor which has been shown to assemble via a two-step pathway with CBF-A (Hap3p homolog) and CBF-C (Hap5p homolog) forming a stable dimer before CBF-B (Hap2p homolog) can interact. We have also found that the interaction of Hap4p with Hap2p/Hap3p/Hap5p requires DNA binding as a prerequisite. To further understand the protein-protein and protein-DNA interactions of this transcription factor, we identified the minimal domain of Hap4p necessary for interaction with the Hap2p/Hap3p/Hap5p-DNA complex, and we demonstrate that this domain is sufficient to complement the respiratory deficiency of a hap4⌬ mutant and activate transcription when fused with the VP16 activation domain. These studies provide a further understanding of the assembly of the yeast CCAAT-binding factor at target promoters and raise a number of questions concerning the protein-protein and protein-DNA interactions of this multisubunit transcription factor.Saccharomyces cerevisiae is a respirofermentative yeast that represses respiratory metabolism when growing in medium containing glucose as the sole carbon source, even in an oxygenated environment (14, 53). Following glucose depletion, cells undergo a major reprogramming of gene expression, known as the diauxic shift, to activate the genes that encode proteins needed for respiration and gluconeogenesis (12,16,30,45). Thus, the organism can utilize the ethanol that was generated during the fermentative metabolism. The CCAAT-binding factor (CBF; the Hap2p/ Hap3p/Hap4p/Hap5p complex) is one of the transcriptional activators responsible for the activation of many of the genes involved in respiratory metabolism (12,16,45,57), as well as other genes needed for other metabolic functions, such as ammonia assimilation (10, 11, 41).The CCAAT-binding factor is a multisubunit transcriptional activator that binds to the 5Ј-CCAAT-3Ј consensus elements within promoters (6, 36). This activator is unique among DNAbinding proteins in that it requires three heterologous subunits, termed Hap2p, Hap3p, and Hap5p, for DNA-binding activity (35,38). The Hap2p/Hap3p/Hap5p trimer has been shown to be sufficient for CCAAT-specific binding at target promoters (38); however, this complex lacks the ability to activate transcription. A fourth subunit of the complex, termed Hap4p, is necessary for transcriptional activat...

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Section: Resultsmentioning

confidence: 99%

“…The first activation domain was mapped between amino acid residues 124 and 329, and a sec-VOL. 4,2005 Hap2p/Hap3p/Hap4p/Hap5p-DNA COMPLEX 1837…”

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Assembly of the Hap2p/Hap3p/Hap4p/Hap5p-DNA Complex in Saccharomyces cerevisiae

McNabb

Pinto

2005

Eukaryot Cell

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“…This is also supported by the fact that no Hap4p homologs have been found except in some yeast strains. 55,56) Recently, the genome sequences of A. nidulans (http://www.broad. mit.edu/annotation/fungi/aspergillus/) and A. oryzae (Consortium for Genome Analysis of Aspergillus oryzae, unpublished data) have been determined, but no orthologs of the hap4 gene have been found by BLAST analysis of these data.…”

Section: Domain Analysis Of the Subunits Of The Hap Complexmentioning

confidence: 99%

An Overview of the CCAAT-Box Binding Factor in Filamentous Fungi: Assembly, Nuclear Translocation, and Transcriptional Enhancement

Kato

2005

Bioscience, Biotechnology, and Biochemistry

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Protein disulphide isomerase genes ofKluyveromyces lactis

Bao

Huo

et al. 2000

Yeast

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Two genes of Kluyveromyces lactis, KlPDI1 and KlMPD1, were studied. They code for a protein disulphide isomerase and its structural and functional homologue, respectively. The KlPDI1 product was 52.6% identical to Pdi1p and the KlMPD1 product 47% identical to Mpd1p of S. cerevisiae. Both genes contained the thioredoxin‐active site‐related signature. Their C‐termini showed a new variant of the endoplasmic reticulum‐retention signal, QDEL. A single copy of KlPDI1 was able to complement the growth defect of a pdi1 mutation. KlMPD1 on a multicopy vector partially suppressed the klpdi1 and pdi1 mutations. The Klpdi1 null mutation was lethal. The klmpd1 disruptant was viable, but showed an increased sensitivity to high temperature. Several stress response motifs were present in the upstream sequence of KlMPD1, but not of KlPDI1, whilst the opposite is known for the S. cerevisiae homologues. The viability of the klmpd1 mutant under starvation for nitrogen or carbon source was not different from that of the wild‐type. The syntenic relationship is discussed for the KlPDI1 gene regions with respect to the duplicated segments PDI1/EUG1 in S. cerevisiae. EMBL Accession Nos: AJ243958 (KlPDI1 region) and AJ243960 (KlMPD1 region). Copyright © 2000 John Wiley & Sons, Ltd.

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HAP4, the glucose‐repressed regulated subunit of the HAP transcriptional complex involved in the fermentation–respiration shift, has a functional homologue in the respiratory yeast Kluyveromyces lactis

Cited by 53 publications

References 56 publications

Assembly of the Hap2p/Hap3p/Hap4p/Hap5p-DNA Complex in Saccharomyces cerevisiae

Assembly of the Hap2p/Hap3p/Hap4p/Hap5p-DNA Complex in Saccharomyces cerevisiae

An Overview of the CCAAT-Box Binding Factor in Filamentous Fungi: Assembly, Nuclear Translocation, and Transcriptional Enhancement

Protein disulphide isomerase genes ofKluyveromyces lactis

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