scholarly journals Cloning and functional characterization of an acyl-acyl carrier protein thioesterase (JcFATB1) from Jatropha curcas

2009 ◽  
Vol 29 (10) ◽  
pp. 1299-1305 ◽  
Author(s):  
P.-Z. Wu ◽  
J. Li ◽  
Q. Wei ◽  
L. Zeng ◽  
Y.-P. Chen ◽  
...  
2017 ◽  
Vol 214 ◽  
pp. 152-160 ◽  
Author(s):  
Wangdan Xiong ◽  
Qian Wei ◽  
Pingzhi Wu ◽  
Sheng Zhang ◽  
Jun Li ◽  
...  

2006 ◽  
Vol 28 (9) ◽  
pp. 657-662 ◽  
Author(s):  
Luo Tong ◽  
Peng Shu-Ming ◽  
Deng Wu-Yuan ◽  
Ma Dan-Wei ◽  
Xu Ying ◽  
...  

Microbiology ◽  
2010 ◽  
Vol 156 (2) ◽  
pp. 484-495 ◽  
Author(s):  
Mariano A. Martinez ◽  
Diego de Mendoza ◽  
Gustavo E. Schujman

Acyl carrier protein (ACP) is a universal and highly conserved carrier of acyl intermediates during fatty acid biosynthesis. The molecular mechanisms of regulation of the acpP structural gene, as well as the function of its gene product, are poorly characterized in Bacillus subtilis and other Gram-positive organisms. Here, we report that transcription of acpP takes place from two different promoters: PfapR and PacpP. Expression of acpP from PfapR is coordinated with a cluster of genes involved in lipid synthesis (the fapR operon); the operon consists of fapR-plsX-fabD-fabG-acpP. PacpP is located immediately upstream of the acpP coding sequence, and is necessary and sufficient for normal fatty acid synthesis. We also report that acpP is essential for growth and differentiation, and that ACP localizes in the mother-cell compartment of the sporangium during spore formation. These results provide the first detailed characterization of the expression of the ACP-encoding gene in a Gram-positive bacterium, and highlight the importance of this protein in B. subtilis physiology.


2012 ◽  
Vol 169 (8) ◽  
pp. 816-824 ◽  
Author(s):  
Qian Wei ◽  
Jun Li ◽  
Lin Zhang ◽  
Pingzhi Wu ◽  
Yaping Chen ◽  
...  

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