Nuclear accessory factors enhance the binding of progesterone receptor to specific target DNA

Prendergast, Paul; Sa, Oñate; Christensen, Kurt D.; Dp, Edwards

doi:10.1016/0960-0760(94)90245-3

Cited by 35 publications

(23 citation statements)

References 47 publications

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“…Although such behavior by CDP/CUT in cells could be explained by invoking the phosphorylation of the homeodomain during the G 1 phase of the cell cycle, the same explanation cannot hold in the case of the purified full-length protein that was dephosphorylated in vitro prior to DNA binding (27). We considered the possibility that CR1ϩ2, in a manner analogous to high mobility group proteins, may impart a conformational change to DNA that would cause the quick release of CR3HD from its adjacent binding site (55)(56)(57). But when tested as individual proteins, CR1ϩ2 and CR3HD were able to bind simultaneously to the N 19 probe, which contains binding sites for both proteins (data not shown).…”

Section: Full-length Cdp/cut Displays Dna-binding Kinetics and Specifmentioning

confidence: 99%

CCAAT Displacement Activity Involves CUT Repeats 1 and 2, Not the CUT Homeodomain

Moon

Bérubé

Nepveu

2000

Journal of Biological Chemistry

126

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The CCAAT displacement protein, the homolog of the Drosophila melanogaster CUT protein, contains four DNA-binding domains: three CUT repeats (CR1, CR2, and CR3) and the CUT homeodomain (HD). Using a panel of fusion proteins, we found that a CUT repeat cannot bind to DNA as a monomer, but that certain combinations of domains exhibit high DNA-binding affinity: CR1؉2, CR3HD, CR1HD, and CR2HD. One combination (CR1؉2) exhibited strikingly different DNA-binding kinetics and specificities. CR1؉2 displayed rapid on and off rates and bound preferably to two C(A/G)AT sites, organized as direct or inverted repeats. Accordingly, only CR1؉2 was able to bind to the CCAAT sequence, and its affinity was increased by the presence of a C(A/G)AT site at close proximity. A purified CCAAT displacement protein/CUT protein exhibited DNA-binding properties similar to those of CR1؉2; and in nuclear extracts, the CCAAT displacement activity also required the simultaneous presence of a C(A/G)AT site. Moreover, CR1؉2, but not CR3HD, was able to displace nuclear factor Y. Thus, the CCAAT displacement activity requires the presence of an additional sequence (CAAT or CGAT) and involves CR1 and CR2, but not the CUT homeodomain.

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Section: Full-length Cdp/cut Displays Dna-binding Kinetics and Specifmentioning

confidence: 99%

CCAAT Displacement Activity Involves CUT Repeats 1 and 2, Not the CUT Homeodomain

Moon

Bérubé

Nepveu

2000

Journal of Biological Chemistry

126

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“…In addition, one or more members of a heteromeric complex may interact with mixed DNA elements or half sites in a responsive gene (37). In regard to other interactions with activated receptors, the nonhistone high-mobility-group chromatin protein (HMG-1) has been shown to substitute for an unidentified factor present in partially purified progesterone receptor fractions that is responsible for promoting PR-DNA binding (38). Also, an unidentified single strand DNA-binding protein has been implicated as being necessary for high affinity binding of ER to the vitellogenin A2 estrogen response element (ERE) (39).…”

Section: Introductionmentioning

confidence: 99%

Estrogen receptor accessory proteins: effects on receptor-DNA interactions.

Landel

Kushner

Greene

1995

Environ Health Perspect

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Despite a wealth of information about the structure and composition of steroid receptors and their functional domains, little is known about the role of accessory proteins as mediators of receptor activity. To better define the role of such proteins in estrogen receptor (ER) function, we have used immunoaffinity, steroid affinity, and site-specific DNA-affinity chromatography to identify and characterize proteins that associate with human ER (hER) in extracts from MCF-7 cells and hER-expressing CHO (CHO-ER) cells. In addition to the expected 66-kDa hER, a 70-kDa protein was obtained and subsequently identified as a member of the heat shock protein family (hsp70). A 55-kDa protein, detected by all three approaches, was identified as a member of the protein disulfide isomerase family (PDI). Two proteins that were preferentially retained by an ER-specific DNA affinity column (p48 and p45) remain unidentified. Maximal interaction of purified hER with the vitellogenin A2 estrogen response element (ERE) occurred in the presence of all four associated proteins isolated by DNA-affinity chromatography. The increased stability of this complex was due primarily to an increase in the association rate of hER with ERE. Thus, accessory proteins may be required for optimal interaction of ER with EREs. -Environ Health Perspect 1 03(Suppl 7): 23-28 (1995)

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“…2,3 Although the nuclear role of HMGB1 is incompletely understood, the protein has been implicated in bending DNA to facilitate gene transcription, DNA replication and repair. [4][5][6][7] The importance of HMGB1 in regulating these nuclear processes is emphasized by the phenotype of HMGB1-deficient mice, which die shortly after birth because of severe energy deficits and hypoglycemia, In addition to its roles in regulating nucleosome function and transcription, HMGB1 more recently emerged as an extracellularly released mediator of inflammation and repair responses in lipopolysaccharide (LPS)-induced endotoxemia and sepsis. 9 Passive immunization with HMGB1-neutralizing antibodies prevented organ damage in animal endotoxemia and sepsis models.…”

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confidence: 99%