Characterization of an acyl-CoA synthetase from Arabidopsis thaliana

2000 ◽  
Vol 28 (6) ◽  
pp. 957-958 ◽  
Author(s):  
J. A. Schnurr ◽  
J. Shockey ◽  
John Browse

One of the major goals of modern plant biotechnology is to manipulate lipid metabolism in oilseed crops to produce new and improved edible and industrial vegetable oils. Lipids constitute the structural components of cellular membranes and act as sources of energy for the germinating seed and are therefore essential to plant cell function. Both de novo synthesis and modification of existing lipids are dependent on the activity of acyl-CoA synthetases (ACSs). To date, ACSs have been recalcitrant to traditional methods of purification due to their association with membranes. In our laboratory, several isoforms of ACSs have been identified in Arabidopsis thaliana. Reverse genetics allowed us to identify a mutant containing a transfer DNA-interrupted ACS gene. Results will be presented that describe the isolation and characterization of this mutant. The elucidation of the specific roles of ACSs will lead to a greater understanding of plant lipid metabolism.

1990 ◽  
Vol 93 (3) ◽  
pp. 907-914 ◽  
Author(s):  
Deborah A. Samac ◽  
Cathy M. Hironaka ◽  
Peter E. Yallaly ◽  
Dilip M. Shah

1999 ◽  
Vol 262 (4-5) ◽  
pp. 633-642 ◽  
Author(s):  
M. Jean ◽  
J. Pelletier ◽  
M. Hilpert ◽  
F. Belzile ◽  
R. Kunze

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.


2000 ◽  
Vol 267 (23) ◽  
pp. 6775-6783 ◽  
Author(s):  
Dominique Eeckhout ◽  
Esbjörn Fiers ◽  
Rebecca Sienaert ◽  
Veerle Snoeck ◽  
Ann Depicker ◽  
...  

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