Cloning of yeast HAP5: a novel subunit of a heterotrimeric complex required for CCAAT binding.

McNabb, David S.; Xing, Yongzhong; Guarente, Leonard

doi:10.1101/gad.9.1.47

Cited by 263 publications

(249 citation statements)

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“…The CCAAT/enhancer element is a common cis-element in the promoters of many genes (Edwards et al, 1998;Kato, 2005;McNabb et al, 1995;Yazawa & Kamada, 2007). Several studies have demonstrated that the CCAAT/enhancer binding protein sites in the human immunodeficiency virus type 1 (HIV-1) LTR are crucial for HIV-1 replication in monocyte/macrophages and for the ability of IFN-b to inhibit ongoing active HIV replication in these cells (Henderson & Calame, 1997;Henderson et al, 1995Henderson et al, , 1996Ravimohan et al, 2010).…”

Section: Discussionmentioning

confidence: 99%

An avian leukosis virus subgroup J isolate with a Rous sarcoma virus-like 5′-LTR shows enhanced replication capability

Gao

Guan

Liu

et al. 2015

Journal of General Virology

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Section: Discussionmentioning

confidence: 99%

An avian leukosis virus subgroup J isolate with a Rous sarcoma virus-like 5′-LTR shows enhanced replication capability

Gao

Guan

Liu

et al. 2015

Journal of General Virology

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“…Since HAPC is part of PENR1 and since for the HAP-like mouse CCAAT-binding complex NF-Y it was shown that binding of this heteromeric factor distorted DNA in vitro (Ronchi et al, 1995), we wished to find out whether this is also true for binding of HAP-containing protein complexes in lower eukaryotes. Hence, a DNA fragment spanning the PENR1-binding site derived from the intergenic region of acvA and ipnA was cloned into plasmid pBEND4 to give pBENDIRAI (see Materials and Methods section).…”

Section: Methodsmentioning

confidence: 99%

“…The aat (penDE) gene lies fusions) (Then Bergh et al, 1996);FLIRT∆hapC-1, yA1, biA1; 825 bp downstream of the ipnA gene (Ramon et al, 1987;Montenegro argB2 ::pFLIRT; hapC ::riboB ϩ (this study) ; FLIRT∆hapC-2, et al, 1990 ;Tobin et al, 1990). biA1; argB2 ::pFLIRT; pyroA4 ; hapC::riboB ϩ (this study) ; OLAB1, biA1; bga0; argB2 ::pOLAB1 (aat-lacZ gene fusion integrated in single copy at the chromosomal argB gene locus) omers (e.g. Hahn and Guarente, 1988;Raymondjean et al, (Litzka et al, 1995);OLAB1MUT1, biA1;bga0;argB2::pO-1988;Chen and Kinsey, 1995;McNabb et al, 1995).…”

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confidence: 99%

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The penicillin regulator PENR1 of Aspergillus nidulans is a HAP‐like transcriptional complex

Litzka¹,

Papagiannopolous

Davis

et al. 1998

European Journal of Biochemistry

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In Aspergillus nidulans, a DNA-binding complex, PENR1, was shown to bind to two CCAAT-boxcontaining DNA elements located in the promoter regions of the bidirectionally oriented penicillin biosynthesis genes acvA and ipnA, and of the aat promoter. Here, partial purification of PENR1 and western blotting using anti-HAPC sera indicated that the previously identified HAPC protein, which was suggested to be part of the CCAAT-binding complex AnCF, is also part of PENR1. This was confirmed by band shift assays using protein extracts of a ∆hapC strain which exhibited no PENR1 DNA-binding activity. Supershift assays and immunoprecipitation analysis using anti-HAPC sera provided evidence that HAPC is part of the PENR1 complex. In ∆hapC strains, penicillin production was reduced, as was expression of both an ipnA-lacZ and aat-lacZ gene fusion. Hence, HAPC-containing PENR1 appears to act as an activator on ipnA and aat expression. However, deletion of hapC had little effect on acvA expression during a fermentation run in fermentation medium. Previous results which had shown that specific deletion of the PENR1-binding site between acvA and ipnA resulted in a strong increase of expression of an acvA-uidA gene fusion, together with the present data, suggest the possibility of the existence of a repressor protein that binds close to or overlaps the PENR1-binding site. It is also shown that binding of PENR1 induced bending of a DNA fragment spanning the PENR1-binding site between acvA and ipnA in vitro.

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“…The cloning of NF-Y genes from several species including yeast, maize, lamprey, and sea urchin, evidenced highly conserved domains (16 -22). The NF-YA homology domain can be divided into subunit association and DNA-contacting subdomains (20). The N-terminal contains a hydrophobic and Gln-rich activation surface (18).…”

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confidence: 99%

NF-Y Organizes the γ-Globin CCAAT Boxes Region

Liberati

Ronchi²,

Lievens

et al. 1998

Journal of Biological Chemistry

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The CCAAT-binding activator NF-Y is formed by three evolutionary conserved subunits, two of which contain putative histone-like domains. We investigated NF-Y binding to all CCAAT boxes of globin promoters in direct binding, competition, and supershift electrophoretic mobility shift assay; we found that the ␣, , and proximal ␥ CCAAT boxes of human and the prosimian Galago bind avidly, and distal ␥ CCAAT boxes have intermediate affinity, whereas the ⑀ and ␤ sequences bind NF-Y very poorly. We developed an efficient in vitro transcription system from erythroid K562 cells and established that both the distal and the proximal CCAAT boxes are important for optimal ␥-globin promoter activity. Surprisingly, NF-Y binding to a mutated distal CCAAT box (a C to T at position ؊114) is remarkably increased upon occupancy of the high affinity proximal element, located 27 base pairs away. Shortening the distance between the two CCAAT boxes progressively prevents simultaneous The CCAAT box is a widespread regulatory sequence found in promoters and enhancers of several genes (1), whose functional importance has been well established in different systems (2-12). NF-Y (also termed CBF) has an almost absolute requirement for these five nucleotides and a strong preference for additional flanking sequences (13,14). Based on supershift experiments with anti-NF-Y antibodies, on competition analysis with the original Ea Y box oligo, 1 or on the heteromeric nature of the DNA-binding complex, NF-Y has been identified as the CCAAT box activator in over 100 promoters (7-11, 14, 15). The CCAAT consensus derived statistically by Bucher (1) (RRCCAAT(C/G)(A/G)) fits well with the optimal NF-Y-binding site.NF-Y is a ubiquitous heteromeric protein composed of three subunits, NF-YA, NF-YB, and NF-YC, all necessary for DNA binding (16,17). The cloning of NF-Y genes from several species including yeast, maize, lamprey, and sea urchin, evidenced highly conserved domains (16 -22). The NF-YA homology domain can be divided into subunit association and DNA-contacting subdomains (20). The N-terminal contains a hydrophobic and Gln-rich activation surface (18). The NF-YC gene has been recently cloned and is specular with respect to NF-YA, since the homology domain is at the N terminus, whereas the Cterminal 180 amino acids are rich in glutamines and hydrophobic residues. NF-YB and NF-YC tightly interact with each other, and their association is a prerequisite for NF-YA binding and sequence-specific DNA interactions (16,22). Both the NF-YB-and NF-YC-conserved domains contain putative histone fold motifs. This motif, common to all core histones, is responsible for the formation of the histone octamer (24) and is composed of three ␣-helices, separated by short loops/strand regions, enabling histones to dimerize with companion subunits (24,25). Recent experiments on the yeast HAP3 (26), NF-YB/ CBF-A (27), and NF-YC/CBF-C (28) indicate that this 65 amino acid long motif is necessary for subunit interactions and DNA binding. NF-Y has additional interesting featur...

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Cloning of yeast HAP5: a novel subunit of a heterotrimeric complex required for CCAAT binding.

Cited by 263 publications

References 62 publications

An avian leukosis virus subgroup J isolate with a Rous sarcoma virus-like 5′-LTR shows enhanced replication capability

An avian leukosis virus subgroup J isolate with a Rous sarcoma virus-like 5′-LTR shows enhanced replication capability

The penicillin regulator PENR1 of Aspergillus nidulans is a HAP‐like transcriptional complex

NF-Y Organizes the γ-Globin CCAAT Boxes Region

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