Very-long-chain fatty acid-containing phospholipids accumulate in fatty acid synthase temperature-sensitive mutant strains of the fission yeast Schizosaccharomyces pombe fas2/lsd1

Author(s):  
Kazuaki Yokoyama ◽  
Shigeaki Saitoh ◽  
Mayuko Ishida ◽  
Yoshio Yamakawa ◽  
Kazumi Nakamura ◽  
...  
2004 ◽  
Vol 59 (7-8) ◽  
pp. 549-553 ◽  
Author(s):  
Thomas Götz ◽  
Peter Böger

AbstractThe first elongation step to form very-long-chain fatty acids (VLCFAs) is catalyzed by the VLCFA-synthase. CoA-activated fatty acids react with malonyl-CoA to condense a C2-unit. As shown with recombinant enzyme this reaction is specifically inhibited by chloroacetamide herbicides. The inhibition is alleviated when the inhibitor (e.g. metazachlor) is incubated together with adequate concentrations of the substrate (e.g. oleoyl-CoA). Malonyl-CoA has no influence. However, once a chloroacetamide has been tightly bound to the synthase after an appropriate time it cannot be displaced anymore by the substrate. In contrast, oleoyl- CoA, is easily removed from the synthase by metazachlor. The irreversible binding of the chloroacetamides and their competition with the substrate explains the very low half-inhibition values of 10-8 м and below. Chiral chloroacetamides like metolachlor or dimethenamid give identical results. However, only the (S)-enantiomers are active.


2019 ◽  
Vol 132 (10) ◽  
pp. jcs229021 ◽  
Author(s):  
Yasuha Kinugasa ◽  
Yasuhiro Hirano ◽  
Megumi Sawai ◽  
Yusuke Ohno ◽  
Tomoko Shindo ◽  
...  

2017 ◽  
Vol 30 (2) ◽  
pp. 161-175 ◽  
Author(s):  
Dianna V. Bourassa ◽  
Elmar L. Kannenberg ◽  
D. Janine Sherrier ◽  
R. Jeffrey Buhr ◽  
Russell W. Carlson

Rhizobium bacteria live in soil and plant environments, are capable of inducing symbiotic nodules on legumes, invade these nodules, and develop into bacteroids that fix atmospheric nitrogen into ammonia. Rhizobial lipopolysaccharide (LPS) is anchored in the bacterial outer membrane through a specialized lipid A containing a very long-chain fatty acid (VLCFA). VLCFA function for rhizobial growth in soil and plant environments is not well understood. Two genes, acpXL and lpxXL, encoding acyl carrier protein and acyltransferase, are among the six genes required for biosynthesis and transfer of VLCFA to lipid A. Rhizobium leguminosarum mutant strains acpXL, acpXL−/lpxXL−, and lpxXL− were examined for LPS structure, viability, and symbiosis. Mutations in acpXL and lpxXL abolished VLCFA attachment to lipid A. The acpXL mutant transferred a shorter acyl chain instead of VLCFA. Strains without lpxXL neither added VLCFA nor a shorter acyl chain. In all strains isolated from nodule bacteria, lipid A had longer acyl chains compared with laboratory-cultured bacteria, whereas mutant strains displayed altered membrane properties, modified cationic peptide sensitivity, and diminished levels of cyclic β-glucans. In pea nodules, mutant bacteroids were atypically formed and nitrogen fixation and senescence were affected. The role of VLCFA for rhizobial environmental fitness is discussed.


2000 ◽  
Vol 41 (1) ◽  
pp. 41-47 ◽  
Author(s):  
Karin A. J.M. van der Lee ◽  
Michaël M. Vork ◽  
Johan E. De Vries ◽  
Peter H.M. Willemsen ◽  
Jan F.C. Glatz ◽  
...  

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