scholarly journals Stimulation of Eukaryotic Flap Endonuclease-1 Activities by Proliferating Cell Nuclear Antigen (PCNA) Is Independent of Itsin VitroInteraction via a Consensus PCNA Binding Region

2001 ◽  
Vol 276 (39) ◽  
pp. 36295-36302 ◽  
Author(s):  
Geoffrey Frank ◽  
Junzhuan Qiu ◽  
Li Zheng ◽  
Binghui Shen
Keyword(s):  
Proliferating Cell Nuclear Antigen ◽  
Nuclear Antigen ◽  
Binding Region ◽  
Flap Endonuclease 1 ◽  
Proliferating Cell ◽  
Stimulation Of

scholarly journals Stimulation of DNA synthesis by natural ceramide 1-phosphate

1997 ◽  
Vol 325 (2) ◽  
pp. 435-440 ◽  
Author(s):  
Antonio GOMEZ-MUÑOZ ◽  
Laura M. FRAGO ◽  
Luis ALVAREZ ◽  
Isabel VARELA-NIETO
Keyword(s):  
Dna Synthesis ◽  
Proliferating Cell Nuclear Antigen ◽  
Solvent Mixture ◽  
Mitogen Activated Protein Kinase ◽  
Nuclear Antigen ◽  
Tyrosine Residues ◽  
Mitogen Activated Protein ◽  
Ceramide 1 ◽  
Proliferating Cell ◽  
Stimulation Of

We found that natural (long-chain) ceramide 1-phosphate can be dispersed into aqueous solution when dissolved in an appropriate mixture of methanol/dodecane (49:1, v/v). This solvent mixture facilitates the interaction of this phosphosphingolipid with cells. Under these conditions, incubation of EGFR T17 fibroblasts with natural ceramide 1-phosphate caused a potent stimulation of DNA synthesis. This effect was accompanied by an increase in the levels of proliferating-cell nuclear antigen. Concentrations of natural ceramide 1-phosphate that stimulated the synthesis of DNA did not inhibit adenylate cyclase activity, nor did they stimulate phospholipase D. Natural ceramide 1-phosphate did not alter the cellular phosphorylation state of tyrosine residues or of mitogen-activated protein kinase. Furthermore, natural ceramide 1-phosphate failed to induce the expression of the proto-oncogenes c-myc and c-fos. Both the stimulation of DNA synthesis and the induction of proliferating-cell nuclear antigen by natural ceramide 1-phosphate were inhibited by natural ceramides. This work suggests that the use of methanol and dodecane to deliver natural ceramide 1-phosphate to cells may be useful for elucidation of the biological function(s) and mechanism(s) of action of ceramide 1-phosphate.

Ultrasound stimulation of tendon cell proliferation and upregulation of proliferating cell nuclear antigen

2005 ◽  
Vol 23 (4) ◽  
pp. 970-976 ◽  
Author(s):  
Wen-Chung Tsai ◽  
Chih-Chin Hsu ◽  
Fuk-Tan Tang ◽  
Shih-Wei Chou ◽  
Ying-Jen Chen ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Proliferating Cell Nuclear Antigen ◽  
Nuclear Antigen ◽  
Tendon Cell ◽  
Ultrasound Stimulation ◽  
Proliferating Cell ◽  
Stimulation Of

The Two DNA Clamps Rad9/Rad1/Hus1 Complex and Proliferating Cell Nuclear Antigen Differentially Regulate Flap Endonuclease 1 Activity

2005 ◽  
Vol 353 (5) ◽  
pp. 980-989 ◽  
Author(s):  
Erica Friedrich-Heineken ◽  
Magali Toueille ◽  
Barbara Tännler ◽  
Christine Bürki ◽  
Elena Ferrari ◽  
...  
Keyword(s):  
Proliferating Cell Nuclear Antigen ◽  
Nuclear Antigen ◽  
Flap Endonuclease 1 ◽  
Proliferating Cell

scholarly journals A crystallization and preliminary X-ray diffraction study of the Arabidopsis thaliana proliferating cell nuclear antigen (PCNA2) alone and in a complex with a PIP-box peptide from Flap endonuclease 1

2020 ◽  
Author(s):  
Ewa Kowalska ◽  
Wojciech Strzałka ◽  
Takuji Oyama
Keyword(s):  
Arabidopsis Thaliana ◽  
Proliferating Cell Nuclear Antigen ◽  
Nuclear Antigen ◽  
X Ray Diffraction ◽  
Interacting Protein ◽  
Space Group ◽  
X Ray ◽  
Flap Endonuclease 1 ◽  
Living Organisms ◽  
Proliferating Cell

DNA replication is an important event for all living organisms and the mechanism is essentially conserved from archaea, bacteria to eukaryotes. Proliferating cell nuclear antigen (PCNA) acts as the universal platform for many DNA transacting proteins. Flap endonuclease 1 (FEN1) is one such enzyme whose activity is largely affected by the interaction with PCNA. To elucidate the key interactions between plant PCNA and FEN1 and possible structural change of PCNA caused by binding of FEN1 at the atomic level, crystallization and preliminary studies of X-ray diffraction of crystals of Arabidopsis thaliana PCNA2 (AtPCNA2) alone and in a complex with a peptide derived from AtFEN1, which contains a typical PCNA-interacting protein (PIP)-box motif, were performed. Both peptide-free and peptide-bound AtPCNA2s were crystallized using the same reservoir solution but in different crystal systems, indicating that the peptide affected the intermolecular interactions in the crystals. Crystals of AtPCNA2 belonged to the hexagonal space group P63, while those of the peptide-bound AtPCNA2 belonged to the rhombohedral space group H3, both of which could contain the functional homo-trimers.

scholarly journals Mutant DNA polymerase δ from thermosensitive Schizosaccharomyces pombe strains display reduced stimulation by proliferating cell nuclear antigen

1998 ◽  
Vol 335 (3) ◽  
pp. 581-588 ◽  
Author(s):  
Mylène PERDERISET ◽  
Giovanni MAGA ◽  
Karine PIARD ◽  
Stefania FRANCESCONI ◽  
Isabelle TRATNER ◽  
...  
Keyword(s):  
Schizosaccharomyces Pombe ◽  
Dna Polymerase ◽  
Proliferating Cell Nuclear Antigen ◽  
Catalytic Subunit ◽  
Nuclear Antigen ◽  
Wild Type ◽  
Low Levels ◽  
Proliferating Cell ◽  
Stimulation Of

We have isolated and characterized DNA polymerase δ (pol δ) from two thermosensitive Schizosaccharomyces pombe strains, polδts1 and polδts3, mutated in two different evolutionarily conserved domains of the catalytic subunit. At the restrictive temperature of 37 °C polδts1 and polδts3 mutant strains arrest growth in the S phase of the cell cycle. We show that at low levels of primer ends, in vitro stimulation by proliferating cell nuclear antigen (PCNA) of mutant enzymes is lower than stimulation of wild-type pol δ. Affinity for primer (3´-OH) ends and processivity of mutant enzymes do not appear different from wild-type pol δ. In contrast, Vmax values are lower than the wild-type value. The major in vitro defect appears to be decreased stimulation of mutant enzymes by PCNA, resulting in reduced velocity of DNA synthesis. In addition, ts1 pol δ is not stimulated by low PCNA concentration at 37 °C, although low concentrations stimulate activity at 25 °C, suggesting that this thermolability at low levels of primer ends could be its critical defect in vivo. Thus, both ts1 and ts3 pol δ mutations are located in regions of the catalytic subunit that seem necessary, directly or indirectly, for its efficient interaction with PCNA.

Sign in / Sign up

Export Citation Format

Share Document