Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in <it>Staphylococcus aureus</it>
<p>Abstract</p> <p>Background</p> <p><it>Staphylococcus aureus </it>synthesizes two siderophores, staphyloferrin A and staphyloferrin B, that promote iron-restricted growth. Previous work on the biosynthesis of staphyloferrin B has focused on the role of the...
Main Authors: | , , |
---|---|
Format: | Article |
Language: | English |
Published: |
BMC
2011-09-01
|
Series: | BMC Microbiology |
Online Access: | http://www.biomedcentral.com/1471-2180/11/199 |
id |
doaj-db9718c4e9d34b538624927b0d383e5a |
---|---|
record_format |
Article |
spelling |
doaj-db9718c4e9d34b538624927b0d383e5a2020-11-25T00:58:55ZengBMCBMC Microbiology1471-21802011-09-0111119910.1186/1471-2180-11-199Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in <it>Staphylococcus aureus</it>Heinrichs David ECheung JohnsonBeasley Federico C<p>Abstract</p> <p>Background</p> <p><it>Staphylococcus aureus </it>synthesizes two siderophores, staphyloferrin A and staphyloferrin B, that promote iron-restricted growth. Previous work on the biosynthesis of staphyloferrin B has focused on the role of the synthetase enzymes, encoded from within the <it>sbnA-I </it>operon, which build the siderophore from the precursor molecules citrate, alpha-ketoglutarate and L-2,3-diaminopropionic acid. However, no information yet exists on several other enzymes, expressed from the biosynthetic cluster, that are thought to be involved in the synthesis of the precursors (or synthetase substrates) themselves.</p> <p>Results</p> <p>Using mutants carrying insertions in <it>sbnA </it>and <it>sbnB</it>, we show that these two genes are essential for the synthesis of staphyloferrin B, and that supplementation of the growth medium with L-2,3-diaminopropionic acid can bypass the block in staphyloferrin B synthesis displayed by the mutants. Several mechanisms are proposed for how the enzymes SbnA, with similarity to cysteine synthase enzymes, and SbnB, with similarity to amino acid dehydrogenases and ornithine cyclodeaminases, function together in the synthesis of this unusual nonproteinogenic amino acid L-2,3-diaminopropionic acid.</p> <p>Conclusions</p> <p>Mutation of either <it>sbnA </it>or <it>sbnB </it>result in abrogation of synthesis of staphyloferrin B, a siderophore that contributes to iron-restricted growth of <it>S. aureus</it>. The loss of staphyloferrin B synthesis is due to an inability to synthesize the unusual amino acid L-2,3-diaminopropionic acid which is an important, iron-liganding component of the siderophore structure. It is proposed that SbnA and SbnB function together as an L-Dap synthase in the <it>S. aureus </it>cell.</p> http://www.biomedcentral.com/1471-2180/11/199 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Heinrichs David E Cheung Johnson Beasley Federico C |
spellingShingle |
Heinrichs David E Cheung Johnson Beasley Federico C Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in <it>Staphylococcus aureus</it> BMC Microbiology |
author_facet |
Heinrichs David E Cheung Johnson Beasley Federico C |
author_sort |
Heinrichs David E |
title |
Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in <it>Staphylococcus aureus</it> |
title_short |
Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in <it>Staphylococcus aureus</it> |
title_full |
Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in <it>Staphylococcus aureus</it> |
title_fullStr |
Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in <it>Staphylococcus aureus</it> |
title_full_unstemmed |
Mutation of L-2,3-diaminopropionic acid synthase genes blocks staphyloferrin B synthesis in <it>Staphylococcus aureus</it> |
title_sort |
mutation of l-2,3-diaminopropionic acid synthase genes blocks staphyloferrin b synthesis in <it>staphylococcus aureus</it> |
publisher |
BMC |
series |
BMC Microbiology |
issn |
1471-2180 |
publishDate |
2011-09-01 |
description |
<p>Abstract</p> <p>Background</p> <p><it>Staphylococcus aureus </it>synthesizes two siderophores, staphyloferrin A and staphyloferrin B, that promote iron-restricted growth. Previous work on the biosynthesis of staphyloferrin B has focused on the role of the synthetase enzymes, encoded from within the <it>sbnA-I </it>operon, which build the siderophore from the precursor molecules citrate, alpha-ketoglutarate and L-2,3-diaminopropionic acid. However, no information yet exists on several other enzymes, expressed from the biosynthetic cluster, that are thought to be involved in the synthesis of the precursors (or synthetase substrates) themselves.</p> <p>Results</p> <p>Using mutants carrying insertions in <it>sbnA </it>and <it>sbnB</it>, we show that these two genes are essential for the synthesis of staphyloferrin B, and that supplementation of the growth medium with L-2,3-diaminopropionic acid can bypass the block in staphyloferrin B synthesis displayed by the mutants. Several mechanisms are proposed for how the enzymes SbnA, with similarity to cysteine synthase enzymes, and SbnB, with similarity to amino acid dehydrogenases and ornithine cyclodeaminases, function together in the synthesis of this unusual nonproteinogenic amino acid L-2,3-diaminopropionic acid.</p> <p>Conclusions</p> <p>Mutation of either <it>sbnA </it>or <it>sbnB </it>result in abrogation of synthesis of staphyloferrin B, a siderophore that contributes to iron-restricted growth of <it>S. aureus</it>. The loss of staphyloferrin B synthesis is due to an inability to synthesize the unusual amino acid L-2,3-diaminopropionic acid which is an important, iron-liganding component of the siderophore structure. It is proposed that SbnA and SbnB function together as an L-Dap synthase in the <it>S. aureus </it>cell.</p> |
url |
http://www.biomedcentral.com/1471-2180/11/199 |
work_keys_str_mv |
AT heinrichsdavide mutationofl23diaminopropionicacidsynthasegenesblocksstaphyloferrinbsynthesisinitstaphylococcusaureusit AT cheungjohnson mutationofl23diaminopropionicacidsynthasegenesblocksstaphyloferrinbsynthesisinitstaphylococcusaureusit AT beasleyfedericoc mutationofl23diaminopropionicacidsynthasegenesblocksstaphyloferrinbsynthesisinitstaphylococcusaureusit |
_version_ |
1725219892777451520 |