Isolation and characterization of a novel anionic peroxidase cDNA found in poplar (Populus nigra) suspension cultured cells

2001 ◽  
Vol 47 (3) ◽  
pp. 165-170 ◽  
Author(s):  
Yoshiaki Kato ◽  
Yoh Sakuma ◽  
Tomonori Azuma ◽  
Akira Ando ◽  
Kiyoshi Miura ◽  
...  
1985 ◽  
Vol 26 (6) ◽  
pp. 1119-1133 ◽  
Author(s):  
Showkat Ali ◽  
Mikio Nishimura ◽  
Toshiaki Mitsui ◽  
Takashi Akazawa ◽  
Kiyohide Kojima

Heterocycles ◽  
2002 ◽  
Vol 56 (1-2) ◽  
pp. 509
Author(s):  
Toshifumi Hirata ◽  
Shin-ya Yamane ◽  
Kei Shimoda ◽  
Takeshi Fujino ◽  
Shinji Ohta

2014 ◽  
Vol 171 (6) ◽  
pp. 429-437 ◽  
Author(s):  
Daniela Seifertová ◽  
Petr Skůpa ◽  
Jan Rychtář ◽  
Martina Laňková ◽  
Markéta Pařezová ◽  
...  

1985 ◽  
Vol 101 (3) ◽  
pp. 1071-1077 ◽  
Author(s):  
D Schubert ◽  
M LaCorbiere

Adherons are high molecular weight glycoprotein complexes which are released into the growth medium of cultured cells. They mediate the adhesive interactions of many cell types, including those of embryonic chick neural retina. The cell surface receptor for chick neural retina adherons has been purified, and shown to be a heparan sulfate proteoglycan (Schubert, D., and M. LaCorbiere, 1985, J. Cell Biol., 100:56-63). This paper describes the isolation and characterization of a protein in neural retina adherons which interacts specifically with the cell surface receptor. The 20,000-mol-wt protein, called retinal purpurin (RP), stimulates neural retina cell-substratum adhesion and prolongs the survival of neural retina cells in culture. The RP protein interacts with heparin and heparan sulfate, but not with other glycosaminoglycans. Monovalent antibodies against RP inhibit RP-cell adhesion as well as adheron-cell interactions. The RP protein is found in neural retina, but not in other tissues such as brain and muscle. These data suggest that RP plays a role in both the survival and adhesive interactions of neural retina cells.


1988 ◽  
Vol 88 (1) ◽  
pp. 119-124 ◽  
Author(s):  
Poontariga Harinasut ◽  
Tetsuko Takabe ◽  
Takashi Akazawa ◽  
Mitsuo Tagaya ◽  
Toshio Fukui

2004 ◽  
Vol 45 (7) ◽  
pp. 845-854 ◽  
Author(s):  
Nobutaka Mitsuda ◽  
Toru Hisabori ◽  
Kunio Takeyasu ◽  
Masa H. Sato

Abstract A 38-bp pollen-specific cis-acting region of the AVP1 gene is involved in the expression of the Arabidopsis thaliana V-PPase during pollen development. Here, we report the isolation and structural characterization of AtVOZ1 and AtVOZ2, novel transcription factors that bind to the 38-bp cis-acting region of A. thaliana V-PPase gene, AVP1. AtVOZ1 and AtVOZ2 show 53% amino acid sequence similarity. Homologs of AtVOZ1 and AtVOZ2 are found in various vascular plants as well as a moss, Physcomitrella patens. Promoter-β-glucuronidase reporter analysis shows that AtVOZ1 is specifically expressed in the phloem tissue and AtVOZ2 is strongly expressed in the root. In vivo transient effector-reporter analysis in A. thaliana suspension-cultured cells demonstrates that AtVOZ1 and AtVOZ2 function as transcriptional activators in the Arabidopsis cell. Two conserved regions termed Domain-A and Domain-B were identified from an alignment of AtVOZ proteins and their homologs of O. sativa and P. patens. AtVOZ2 binds as a dimer to the specific palindromic sequence, GCGTNx7ACGC, with Domain-B, which is comprised of a functional novel zinc coordinating motif and a conserved basic region. Domain-B is shown to function as both the DNA-binding and the dimerization domains of AtVOZ2. From highly the conservative nature among all identified VOZ proteins, we conclude that Domain-B is responsible for the DNA binding and dimerization of all VOZ-family proteins and designate it as the VOZ-domain.


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