Composition and metabolism of lipids within repressed and active chromatin of interphase lymphocytes

Rose, Herbert G.; Frenster, John H.

doi:10.1016/0005-2760(65)90073-1

Cited by 109 publications

(26 citation statements)

References 35 publications

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“…Sequence similarity between this known phospholipid transporter and RFBP supports the idea that RFBP may regulate nuclear phospholipid composition such that levels of intranuclear phospholipids are higher for active chromatin than for repressed chromatin (60). However, the unique structure of RFBP coupled to its ability to bind the RING domain and contact euchromatin supports the idea that it has a very different function.…”

Section: An Atypical Nuclear P-type Atpase Is a Rfbp 3645mentioning

confidence: 74%

Cloning and Characterization of an Atypical Type IV P-type ATPase That Binds to the RING Motif of RUSH Transcription Factors

Mansharamani

Hewetson

Chilton³

2001

Journal of Biological Chemistry

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RUSH proteins are SWI/SNF-related transcription factors with RING finger signatures near their COOH termini. Long suspected of mediating protein-protein interactions, the RING motif was used to clone a binding partner. The RING finger binding protein (RFBP) is a Type IV P-type ATPase, a putative phospholipid pump, with conserved sequences for two loop segments, an ATP-binding site, a phosphorylation domain, and transmembrane passes potentially involved in substrate binding and translocation. However, RFBP differs from all other Type IV P-type ATPases in three ways. It has only three of four highly conserved NH 2 -terminal transmembrane passes, it is located in the inner nuclear membrane, and it binds the RING domain. Topographically the orientation of the adjacent hydrophilic domains and the determinants of transport specificity are altered. As a result, the small, hydrophilic loop extends into the perinuclear space that is contiguous with the lumen of the endoplasmic reticulum. The large, conformationally flexible loop extends into the nucleoplasm to contact euchromatin. Competitive reverse transcriptasepolymerase chain reaction and high performance liquid chromatography analysis revealed that endometrial RFBP mRNA expression is hormonally regulated. The physical association of a hormone-dependent RING finger-binding protein with transcriptionally active chromatin supports the speculation that RFBP plays a role in the subnuclear trafficking of transcription factors with RING motifs.RUSH is an acronym for proteins with RING finger motifs that bind to the uteroglobin promoter (1); RUSH nucleophosphoproteins contain regions of homology with members of the SWI/SNF superfamily of DNA-dependent helicases/ATPases. The expression of RUSH-1␣ (1005-amino acids, 113 kDa) and RUSH-1␤ (836 amino acids, 95 kDa) is regulated by a steroiddependent alternative splicing mechanism (2) in which ␣ is the progesterone-dependent splice variant, and ␤ is the estrogendependent splice variant. Thus, the acronym acknowledges that in a changing hormonal milieu transcription is bypassed by alternative splicing, and the response of individual target genes is accelerated or "RUSHed."Sequence alignment of homologs from rabbit, human, rodent, and plant (3) showed that all RUSH proteins contain the RING finger motif (C 3 HC 4 or RING-HC), which binds two zinc ions in a unique cross-braced system (4). RING fingers can be associated with other motifs to form larger, conserved domains such as the RING finger-B box-␣-helical coiled-coil (RBCC) domain (4). Some changes have occurred in the RING such that RING-H2 (C 3 H 2 C 3 ) designates a subclass in which a histidine residue was substituted for the fourth cysteine residue. The U-box (UFD2 homology domain) is a degenerate version of the RING motif that lacks the signature metal-chelating residues (5, 6). Unlike the authentic RING finger that is stabilized by binding zinc ions, it has been inferred from the PROMODII model that the U-box is maintained by a system of salt bridges and hydrogen bonds (6...

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Section: An Atypical Nuclear P-type Atpase Is a Rfbp 3645mentioning

confidence: 74%

Cloning and Characterization of an Atypical Type IV P-type ATPase That Binds to the RING Motif of RUSH Transcription Factors

Mansharamani

Hewetson

Chilton³

2001

Journal of Biological Chemistry

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“…However, in addition to these abundant molecules, the nuclear interior was also shown to contain minor components such as lipids (Rose and Frenster, 1965). Several biochemical studies (Boronenkov et al, 1998;Cocco et al, 1987;Divecha et al, 1991;Vann et al, 1997) have shown that purified nuclei contain enzymes involved in the production and degradation of phosphoinositides (PI).…”

Section: Introductionmentioning

confidence: 99%

Involvement of PIP2 in RNA Polymerase I transcription

Yıldırım

Castaño

Sobol

et al. 2013

Journal of Cell Science

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SummaryRNA polymerase I (Pol I) transcription is essential for the cell cycle, growth and protein synthesis in eukaryotes. In the present study, we found that phosphatidylinositol 4,5-bisphosphate (PIP2) is a part of the protein complex on the active ribosomal promoter during transcription. PIP2 makes a complex with Pol I and the Pol I transcription factor UBF in the nucleolus. PIP2 depletion reduces Pol I transcription, which can be rescued by the addition of exogenous PIP2. In addition, PIP2 also binds directly to the pre-rRNA processing factor fibrillarin (Fib), and co-localizes with nascent transcripts in the nucleolus. PIP2 binding to UBF and Fib modulates their binding to DNA and RNA, respectively. In conclusion, PIP2 interacts with a subset of Pol I transcription machinery, and promotes Pol I transcription.

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“…In 1965, Rose and Frenster first pointed to the possible role that phosholipids may play in the nuclei as they detected that both the quantity and the intensity of phospholipid metabolism was much higher in active than repressed chromatin (62). In 1983, Smith and 4 Wells observed increased incorporation of 32 P into a mixture of phospholipids containing PtdIns(4)P and PtdIns(4,5)P 2 in nuclear envelopes isolated from rat liver nuclei (65).…”

Section: Introduction and Historical Overviewmentioning

confidence: 99%

Nuclear phospholipid signaling: phosphatidylinositol-specific phospholipase C and phosphoinositide 3-kinase

Višnjić

Banfíƈ

2007

Pflugers Arch - Eur J Physiol

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Over the last 20 years, numerous studies have demonstrated the existence of nuclear phosphoinositide signaling distinct from the one at the plasma membrane. The activation of phosphatidylinositol-specific phospholipase C (PI-PLC) and phosphoinositide 3-kinase (PI3K), the generation of diacylglycerol (DAG) and the accumulation of the 3-phosphorylated phosphoinositides have been documented in the nuclei of different cell types.In this review, we summarize some recent studies of the subnuclear localization, mechanisms of activation and the possible physiological roles of the nuclear PI-PLC and PI-3 kinases in the regulation of cell cycle, survival and differentiation.

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Composition and metabolism of lipids within repressed and active chromatin of interphase lymphocytes

Cited by 109 publications

References 35 publications

Cloning and Characterization of an Atypical Type IV P-type ATPase That Binds to the RING Motif of RUSH Transcription Factors

Cloning and Characterization of an Atypical Type IV P-type ATPase That Binds to the RING Motif of RUSH Transcription Factors

Involvement of PIP2 in RNA Polymerase I transcription

Nuclear phospholipid signaling: phosphatidylinositol-specific phospholipase C and phosphoinositide 3-kinase

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