Characterization of X-Ray-Induced Immunostaining of Proliferating Cell Nuclear Antigen in Human Diploid Fibroblasts

1996 ◽  
Vol 145 (1) ◽  
pp. 75 ◽  
Author(s):  
Masahiko Miura ◽  
Takehito Sasaki ◽  
Yoshinari Takasaki
Planta ◽  
2008 ◽  
Vol 227 (6) ◽  
pp. 1233-1241 ◽  
Author(s):  
Yukinobu Uchiyama ◽  
Yuko Suzuki ◽  
Kengo Sakaguchi

2013 ◽  
Vol 94 (4) ◽  
pp. 723-731 ◽  
Author(s):  
Alessia De Chiara ◽  
Magali Pederzoli-Ribeil ◽  
Julie Mocek ◽  
Céline Candalh ◽  
Patrick Mayeux ◽  
...  

1991 ◽  
Vol 193 (2) ◽  
pp. 283-290 ◽  
Author(s):  
Zbigniew Pietrzkowski ◽  
Hansjuerg Alder ◽  
Chung-Der Chang ◽  
De-Hui Ku ◽  
Renato Baserga

1998 ◽  
Vol 332 (2) ◽  
pp. 557-563 ◽  
Author(s):  
Hirokazu SETO ◽  
Masami HATANAKA ◽  
Seisuke KIMURA ◽  
Masahiko OSHIGE ◽  
Yuri TSUYA ◽  
...  

A DNA polymerase from cauliflower (Brassica oleracea var. botrytis) inflorescence has been purified to near homogeneity through five successive column chromatographies, and temporally designated cauliflower polymerase 1. Cauliflower polymerase 1 is a monopolypeptide with a molecular mass of 100 kDa. The enzyme efficiently uses synthetic DNA homopolymers and moderately activated DNA and a synthetic RNA homopolymer as template-primers. The enzyme is strongly sensitive to dideoxythymidine triphosphate and N-ethylmaleimide, but it is insensitive to aphidicolin. It was stimulated with 250 mM KCl. Its mode of DNA synthesis is high-processive with or without proliferating-cell nuclear antigen. A 3´ → 5´ exonuclease activity is associated with cauliflower polymerase 1. The enzyme is clearly different from cauliflower mitochondrial polymerase and does not resemble the four different types of wheat DNA polymerase, designated wheat DNA polymerases A, B, CI and CII. In the present paper the role of the enzyme in plant DNA synthesis is discussed.


Author(s):  
Ewa Kowalska ◽  
Wojciech Strzałka ◽  
Takuji Oyama

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.


2000 ◽  
Vol 275 (22) ◽  
pp. 16810-16819 ◽  
Author(s):  
Mariappan Vairapandi ◽  
Naiyer Azam ◽  
Arthur G. Balliet ◽  
Barbara Hoffman ◽  
Dan A. Liebermann

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