Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both <it>Bacillus subtilis </it>and <it>Escherichia coli</it>
<p>Abstract</p> <p>Background</p> <p>Phospholipid biosynthesis commences with the acylation of glycerol-3-phosphate (G3P) to form 1-acyl-G3P. This step is catalyzed by the PlsB protein in <it>Escherichia coli</it>. The gene encoding this protein has not been...
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BMC
2007-07-01
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Series: | BMC Microbiology |
Online Access: | http://www.biomedcentral.com/1471-2180/7/69 |
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author | Ogasawara Naotake Oshima Taku Yoshimura Mika |
author_facet | Ogasawara Naotake Oshima Taku Yoshimura Mika |
author_sort | Ogasawara Naotake |
collection | DOAJ |
description | <p>Abstract</p> <p>Background</p> <p>Phospholipid biosynthesis commences with the acylation of glycerol-3-phosphate (G3P) to form 1-acyl-G3P. This step is catalyzed by the PlsB protein in <it>Escherichia coli</it>. The gene encoding this protein has not been identified, however, in the majority of bacterial genome sequences, including that of <it>Bacillus subtilis</it>. Recently, a new two-step pathway catalyzed by PlsX and PlsY proteins for the initiation of phospholipid formation in <it>Streptococcus pneumoniae </it>has been reported.</p> <p>Results</p> <p>In <it>B. subtilis</it>, 271 genes have been reported to be indispensable, when inactivated singly, for growth in LB medium. Among these, 11 genes encode proteins with unknown functions. As part of a genetic study to identify the functions of these genes, we show here that the <it>B. subtilis </it>ortholog of <it>S. pneumoniae </it>PlsY, YneS, is required for G3P acyltransferase activity, together with PlsX. The <it>B. subtilis </it>genome lacks <it>plsB</it>, and we show in vivo that the PlsX/Y pathway is indeed essential for the growth of bacteria lacking <it>plsB</it>. Interestingly, in addition to <it>plsB</it>, <it>E. coli </it>possesses <it>plsX </it>and the <it>plsY </it>ortholog, <it>ygiH</it>. We therefore explored the functional relationship between PlsB, PlsX and YgiH in <it>E. coli</it>, and found that <it>plsB </it>is essential for <it>E. coli </it>growth, indicating that PlsB plays an important role in 1-acyl-G3P synthesis in <it>E. coli</it>. We also found, however, that the simultaneous inactivation of <it>plsX </it>and <it>ygiH </it>was impossible, revealing important roles for PlsX and YgiH in <it>E. coli </it>growth.</p> <p>Conclusion</p> <p>Both <it>plsX </it>and <it>yneS </it>are essential for 1-acyl-G3P synthesis in <it>B. subtilis</it>, in agreement with recent reports on their biochemical functions. In <it>E. coli</it>, PlsB plays a principal role in 1-acyl-G3P synthesis and is also essential for bacterial growth. PlsX and YgiH also, however, play important roles in <it>E. coli </it>growth, possibly by regulating the intracellular concentration of acyl-ACP. These proteins are therefore important targets for development of new antibacterial agents.</p> |
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spelling | doaj.art-5439b0ee8e6444919a215000e341241d2022-12-22T02:48:36ZengBMCBMC Microbiology1471-21802007-07-01716910.1186/1471-2180-7-69Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both <it>Bacillus subtilis </it>and <it>Escherichia coli</it>Ogasawara NaotakeOshima TakuYoshimura Mika<p>Abstract</p> <p>Background</p> <p>Phospholipid biosynthesis commences with the acylation of glycerol-3-phosphate (G3P) to form 1-acyl-G3P. This step is catalyzed by the PlsB protein in <it>Escherichia coli</it>. The gene encoding this protein has not been identified, however, in the majority of bacterial genome sequences, including that of <it>Bacillus subtilis</it>. Recently, a new two-step pathway catalyzed by PlsX and PlsY proteins for the initiation of phospholipid formation in <it>Streptococcus pneumoniae </it>has been reported.</p> <p>Results</p> <p>In <it>B. subtilis</it>, 271 genes have been reported to be indispensable, when inactivated singly, for growth in LB medium. Among these, 11 genes encode proteins with unknown functions. As part of a genetic study to identify the functions of these genes, we show here that the <it>B. subtilis </it>ortholog of <it>S. pneumoniae </it>PlsY, YneS, is required for G3P acyltransferase activity, together with PlsX. The <it>B. subtilis </it>genome lacks <it>plsB</it>, and we show in vivo that the PlsX/Y pathway is indeed essential for the growth of bacteria lacking <it>plsB</it>. Interestingly, in addition to <it>plsB</it>, <it>E. coli </it>possesses <it>plsX </it>and the <it>plsY </it>ortholog, <it>ygiH</it>. We therefore explored the functional relationship between PlsB, PlsX and YgiH in <it>E. coli</it>, and found that <it>plsB </it>is essential for <it>E. coli </it>growth, indicating that PlsB plays an important role in 1-acyl-G3P synthesis in <it>E. coli</it>. We also found, however, that the simultaneous inactivation of <it>plsX </it>and <it>ygiH </it>was impossible, revealing important roles for PlsX and YgiH in <it>E. coli </it>growth.</p> <p>Conclusion</p> <p>Both <it>plsX </it>and <it>yneS </it>are essential for 1-acyl-G3P synthesis in <it>B. subtilis</it>, in agreement with recent reports on their biochemical functions. In <it>E. coli</it>, PlsB plays a principal role in 1-acyl-G3P synthesis and is also essential for bacterial growth. PlsX and YgiH also, however, play important roles in <it>E. coli </it>growth, possibly by regulating the intracellular concentration of acyl-ACP. These proteins are therefore important targets for development of new antibacterial agents.</p>http://www.biomedcentral.com/1471-2180/7/69 |
spellingShingle | Ogasawara Naotake Oshima Taku Yoshimura Mika Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both <it>Bacillus subtilis </it>and <it>Escherichia coli</it> BMC Microbiology |
title | Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both <it>Bacillus subtilis </it>and <it>Escherichia coli</it> |
title_full | Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both <it>Bacillus subtilis </it>and <it>Escherichia coli</it> |
title_fullStr | Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both <it>Bacillus subtilis </it>and <it>Escherichia coli</it> |
title_full_unstemmed | Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both <it>Bacillus subtilis </it>and <it>Escherichia coli</it> |
title_short | Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both <it>Bacillus subtilis </it>and <it>Escherichia coli</it> |
title_sort | involvement of the ynes ygih and plsx proteins in phospholipid biosynthesis in both it bacillus subtilis it and it escherichia coli it |
url | http://www.biomedcentral.com/1471-2180/7/69 |
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