MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis
<p>Abstract</p> <p>Background</p> <p>Methylthioadenosine, the main by-product of spermidine synthesis, is degraded in <it>Bacillus subtilis</it> as adenine and methylthioribose. The latter is an excellent sulfur source and the precursor of quorum-sensing sig...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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BMC
2001-08-01
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| Series: | BMC Microbiology |
| Online Access: | http://www.biomedcentral.com/1471-2180/1/15 |
| _version_ | 1811265552435380224 |
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| author | Tse Jane KS Krogh Susanne Mulard Laurence Sekowska Agnieszka Danchin Antoine |
| author_facet | Tse Jane KS Krogh Susanne Mulard Laurence Sekowska Agnieszka Danchin Antoine |
| author_sort | Tse Jane KS |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>Methylthioadenosine, the main by-product of spermidine synthesis, is degraded in <it>Bacillus subtilis</it> as adenine and methylthioribose. The latter is an excellent sulfur source and the precursor of quorum-sensing signalling molecules. Nothing was known about methylthioribose recycling in this organism.</p> <p>Results</p> <p>Using trifluoromethylthioribose as a toxic analog to select for resistant mutants, we demonstrate that methylthioribose is first phosphorylated by MtnK, methylthioribose kinase, the product of gene <it>mtnK</it> (formerly <it>ykrT</it>), expressed as an operon with <it>mtnS</it> (formerly <it>ykrS</it>) in an abundant transcript with a S-box leader sequence. Although participating in methylthioribose recycling, the function of <it>mtnS</it> remained elusive. We also show that MtnK synthesis is boosted under starvation condition, in the following decreasing order: carbon-, sulfur- and nitrogen-starvation. We finally show that this enzyme is part of the family Pfam 01633 (choline kinases) which belongs to a large cluster of orthologs comprizing antibiotic aminoglycoside kinases and protein serine/threonine kinases.</p> <p>Conclusions</p> <p>The first step of methylthioribose recycling is phosphoryltaion by MTR kinase, coded by the <it>mtnK</it> (formerly <it>ykrT</it>) gene. Analysis of the neighbourhood of <it>mtnK</it> demonstrates that genes located in its immediate vicinity (now named <it>mtnUVWXYZ</it>, formerly <it>ykrUVWXYZ</it>) are also required for methylthioribose recycling.</p> |
| first_indexed | 2024-04-12T20:25:45Z |
| format | Article |
| id | doaj.art-2794e947c8a545ed8464e423368a4d74 |
| institution | Directory Open Access Journal |
| issn | 1471-2180 |
| language | English |
| last_indexed | 2024-04-12T20:25:45Z |
| publishDate | 2001-08-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Microbiology |
| spelling | doaj.art-2794e947c8a545ed8464e423368a4d742022-12-22T03:17:52ZengBMCBMC Microbiology1471-21802001-08-01111510.1186/1471-2180-1-15MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilisTse Jane KSKrogh SusanneMulard LaurenceSekowska AgnieszkaDanchin Antoine<p>Abstract</p> <p>Background</p> <p>Methylthioadenosine, the main by-product of spermidine synthesis, is degraded in <it>Bacillus subtilis</it> as adenine and methylthioribose. The latter is an excellent sulfur source and the precursor of quorum-sensing signalling molecules. Nothing was known about methylthioribose recycling in this organism.</p> <p>Results</p> <p>Using trifluoromethylthioribose as a toxic analog to select for resistant mutants, we demonstrate that methylthioribose is first phosphorylated by MtnK, methylthioribose kinase, the product of gene <it>mtnK</it> (formerly <it>ykrT</it>), expressed as an operon with <it>mtnS</it> (formerly <it>ykrS</it>) in an abundant transcript with a S-box leader sequence. Although participating in methylthioribose recycling, the function of <it>mtnS</it> remained elusive. We also show that MtnK synthesis is boosted under starvation condition, in the following decreasing order: carbon-, sulfur- and nitrogen-starvation. We finally show that this enzyme is part of the family Pfam 01633 (choline kinases) which belongs to a large cluster of orthologs comprizing antibiotic aminoglycoside kinases and protein serine/threonine kinases.</p> <p>Conclusions</p> <p>The first step of methylthioribose recycling is phosphoryltaion by MTR kinase, coded by the <it>mtnK</it> (formerly <it>ykrT</it>) gene. Analysis of the neighbourhood of <it>mtnK</it> demonstrates that genes located in its immediate vicinity (now named <it>mtnUVWXYZ</it>, formerly <it>ykrUVWXYZ</it>) are also required for methylthioribose recycling.</p>http://www.biomedcentral.com/1471-2180/1/15 |
| spellingShingle | Tse Jane KS Krogh Susanne Mulard Laurence Sekowska Agnieszka Danchin Antoine MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis BMC Microbiology |
| title | MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis |
| title_full | MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis |
| title_fullStr | MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis |
| title_full_unstemmed | MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis |
| title_short | MtnK, methylthioribose kinase, is a starvation-induced protein in Bacillus subtilis |
| title_sort | mtnk methylthioribose kinase is a starvation induced protein in bacillus subtilis |
| url | http://www.biomedcentral.com/1471-2180/1/15 |
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