Post translational modifications of Trifolitoxin: a blue fluorescent peptide antibiotic
Trifolitoxin (TFX, C 41 H 63 N 15 O 15 S) is a selective, ribosomally-synthesized, post-translationally modified, peptide antibiotic, produced by Rhizobium leguminosarum bv. trifolii T24. TFX specifically inhibits α-proteobacteria, including the plant symbiont Rhizobium spp., the plant pathogen Agro...
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| Veröffentlicht in: | Journal of antibiotics 2022-03, Vol.75 (3), p.125-135 |
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| creator | Lethbridge, Benjamin J. Asenstorfer, Robert E. Bailey, Laura S. Breil, Brenda T. Johnson, Jodie V. Jones, Graham P. Rumjanek, Victor Sims, James J. Tate, Max E. Triplett, Eric W. |
| description | Trifolitoxin (TFX, C
41
H
63
N
15
O
15
S) is a selective, ribosomally-synthesized, post-translationally modified, peptide antibiotic, produced by
Rhizobium leguminosarum
bv.
trifolii
T24. TFX specifically inhibits α-proteobacteria, including the plant symbiont
Rhizobium
spp., the plant pathogen
Agrobacterium
spp. and the animal pathogen
Brucella abortus
. TFX-producing strains prevent legume root nodulation by TFX-sensitive rhizobia. TFX has been isolated as a pair of geometric isomers, TFX1 and TFX2, which are derived from the biologically inactive primary amino acid sequence: Asp-Ile-Gly-Gly-Ser-Arg-Gln-Gly-Cys-Val-Ala. Gly-Cys is present as a thiazoline ring and the Arg-Gln-Gly sequence is extensively modified to a UV absorbing, blue fluorescent chromophore. The chromophore consists of a conjugated, 5-membered heterocyclic ring and side chain of modified glutamine. |
| doi_str_mv | 10.1038/s41429-021-00497-0 |
| format | Article |
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41
H
63
N
15
O
15
S) is a selective, ribosomally-synthesized, post-translationally modified, peptide antibiotic, produced by
Rhizobium leguminosarum
bv.
trifolii
T24. TFX specifically inhibits α-proteobacteria, including the plant symbiont
Rhizobium
spp., the plant pathogen
Agrobacterium
spp. and the animal pathogen
Brucella abortus
. TFX-producing strains prevent legume root nodulation by TFX-sensitive rhizobia. TFX has been isolated as a pair of geometric isomers, TFX1 and TFX2, which are derived from the biologically inactive primary amino acid sequence: Asp-Ile-Gly-Gly-Ser-Arg-Gln-Gly-Cys-Val-Ala. Gly-Cys is present as a thiazoline ring and the Arg-Gln-Gly sequence is extensively modified to a UV absorbing, blue fluorescent chromophore. The chromophore consists of a conjugated, 5-membered heterocyclic ring and side chain of modified glutamine.</description><identifier>ISSN: 0021-8820</identifier><identifier>EISSN: 1881-1469</identifier><identifier>DOI: 10.1038/s41429-021-00497-0</identifier><identifier>PMID: 35022574</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>101/58 ; 101/6 ; 631/92/611 ; 631/92/613 ; 82/29 ; Amino Acid Sequence ; Amino acids ; Amino Acids - genetics ; Anti-Bacterial Agents - metabolism ; Antibiotics ; Bacteriology ; Biomedical and Life Sciences ; Bioorganic Chemistry ; Chromophores ; Fluorescence ; Glutamine ; Isomers ; Legumes ; Life Sciences ; Medicinal Chemistry ; Microbiology ; Nodulation ; Organic Chemistry ; Pathogens ; Peptides ; Peptides - metabolism ; Post-translation ; Protein Processing, Post-Translational - genetics ; Rhizobium - genetics ; Thiazoline</subject><ispartof>Journal of antibiotics, 2022-03, Vol.75 (3), p.125-135</ispartof><rights>The Author(s) 2022</rights><rights>2022. The Author(s).</rights><rights>The Author(s) 2022. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-ed47bd8802e5d68046936727042361eece4652969b70a35e0e50aafcd4f492ac3</citedby><cites>FETCH-LOGICAL-c474t-ed47bd8802e5d68046936727042361eece4652969b70a35e0e50aafcd4f492ac3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,776,780,881,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35022574$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Lethbridge, Benjamin J.</creatorcontrib><creatorcontrib>Asenstorfer, Robert E.</creatorcontrib><creatorcontrib>Bailey, Laura S.</creatorcontrib><creatorcontrib>Breil, Brenda T.</creatorcontrib><creatorcontrib>Johnson, Jodie V.</creatorcontrib><creatorcontrib>Jones, Graham P.</creatorcontrib><creatorcontrib>Rumjanek, Victor</creatorcontrib><creatorcontrib>Sims, James J.</creatorcontrib><creatorcontrib>Tate, Max E.</creatorcontrib><creatorcontrib>Triplett, Eric W.</creatorcontrib><title>Post translational modifications of Trifolitoxin: a blue fluorescent peptide antibiotic</title><title>Journal of antibiotics</title><addtitle>J Antibiot</addtitle><addtitle>J Antibiot (Tokyo)</addtitle><description>Trifolitoxin (TFX, C
41
H
63
N
15
O
15
S) is a selective, ribosomally-synthesized, post-translationally modified, peptide antibiotic, produced by
Rhizobium leguminosarum
bv.
trifolii
T24. TFX specifically inhibits α-proteobacteria, including the plant symbiont
Rhizobium
spp., the plant pathogen
Agrobacterium
spp. and the animal pathogen
Brucella abortus
. TFX-producing strains prevent legume root nodulation by TFX-sensitive rhizobia. TFX has been isolated as a pair of geometric isomers, TFX1 and TFX2, which are derived from the biologically inactive primary amino acid sequence: Asp-Ile-Gly-Gly-Ser-Arg-Gln-Gly-Cys-Val-Ala. Gly-Cys is present as a thiazoline ring and the Arg-Gln-Gly sequence is extensively modified to a UV absorbing, blue fluorescent chromophore. The chromophore consists of a conjugated, 5-membered heterocyclic ring and side chain of modified glutamine.</description><subject>101/58</subject><subject>101/6</subject><subject>631/92/611</subject><subject>631/92/613</subject><subject>82/29</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Amino Acids - genetics</subject><subject>Anti-Bacterial Agents - metabolism</subject><subject>Antibiotics</subject><subject>Bacteriology</subject><subject>Biomedical and Life Sciences</subject><subject>Bioorganic Chemistry</subject><subject>Chromophores</subject><subject>Fluorescence</subject><subject>Glutamine</subject><subject>Isomers</subject><subject>Legumes</subject><subject>Life Sciences</subject><subject>Medicinal Chemistry</subject><subject>Microbiology</subject><subject>Nodulation</subject><subject>Organic Chemistry</subject><subject>Pathogens</subject><subject>Peptides</subject><subject>Peptides - metabolism</subject><subject>Post-translation</subject><subject>Protein Processing, Post-Translational - 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genetics</topic><topic>Anti-Bacterial Agents - metabolism</topic><topic>Antibiotics</topic><topic>Bacteriology</topic><topic>Biomedical and Life Sciences</topic><topic>Bioorganic Chemistry</topic><topic>Chromophores</topic><topic>Fluorescence</topic><topic>Glutamine</topic><topic>Isomers</topic><topic>Legumes</topic><topic>Life Sciences</topic><topic>Medicinal Chemistry</topic><topic>Microbiology</topic><topic>Nodulation</topic><topic>Organic Chemistry</topic><topic>Pathogens</topic><topic>Peptides</topic><topic>Peptides - metabolism</topic><topic>Post-translation</topic><topic>Protein Processing, Post-Translational - genetics</topic><topic>Rhizobium - genetics</topic><topic>Thiazoline</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Lethbridge, Benjamin J.</creatorcontrib><creatorcontrib>Asenstorfer, Robert E.</creatorcontrib><creatorcontrib>Bailey, Laura S.</creatorcontrib><creatorcontrib>Breil, Brenda T.</creatorcontrib><creatorcontrib>Johnson, Jodie V.</creatorcontrib><creatorcontrib>Jones, Graham P.</creatorcontrib><creatorcontrib>Rumjanek, Victor</creatorcontrib><creatorcontrib>Sims, James J.</creatorcontrib><creatorcontrib>Tate, Max E.</creatorcontrib><creatorcontrib>Triplett, Eric W.</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Immunology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of antibiotics</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Lethbridge, Benjamin J.</au><au>Asenstorfer, Robert E.</au><au>Bailey, Laura S.</au><au>Breil, Brenda T.</au><au>Johnson, Jodie V.</au><au>Jones, Graham P.</au><au>Rumjanek, Victor</au><au>Sims, James J.</au><au>Tate, Max E.</au><au>Triplett, Eric W.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Post translational modifications of Trifolitoxin: a blue fluorescent peptide antibiotic</atitle><jtitle>Journal of antibiotics</jtitle><stitle>J Antibiot</stitle><addtitle>J Antibiot (Tokyo)</addtitle><date>2022-03-01</date><risdate>2022</risdate><volume>75</volume><issue>3</issue><spage>125</spage><epage>135</epage><pages>125-135</pages><issn>0021-8820</issn><eissn>1881-1469</eissn><abstract>Trifolitoxin (TFX, C
41
H
63
N
15
O
15
S) is a selective, ribosomally-synthesized, post-translationally modified, peptide antibiotic, produced by
Rhizobium leguminosarum
bv.
trifolii
T24. TFX specifically inhibits α-proteobacteria, including the plant symbiont
Rhizobium
spp., the plant pathogen
Agrobacterium
spp. and the animal pathogen
Brucella abortus
. TFX-producing strains prevent legume root nodulation by TFX-sensitive rhizobia. TFX has been isolated as a pair of geometric isomers, TFX1 and TFX2, which are derived from the biologically inactive primary amino acid sequence: Asp-Ile-Gly-Gly-Ser-Arg-Gln-Gly-Cys-Val-Ala. Gly-Cys is present as a thiazoline ring and the Arg-Gln-Gly sequence is extensively modified to a UV absorbing, blue fluorescent chromophore. The chromophore consists of a conjugated, 5-membered heterocyclic ring and side chain of modified glutamine.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>35022574</pmid><doi>10.1038/s41429-021-00497-0</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0021-8820 |
| ispartof | Journal of antibiotics, 2022-03, Vol.75 (3), p.125-135 |
| issn | 0021-8820 1881-1469 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_8816728 |
| source | MEDLINE; Alma/SFX Local Collection |
| subjects | 101/58 101/6 631/92/611 631/92/613 82/29 Amino Acid Sequence Amino acids Amino Acids - genetics Anti-Bacterial Agents - metabolism Antibiotics Bacteriology Biomedical and Life Sciences Bioorganic Chemistry Chromophores Fluorescence Glutamine Isomers Legumes Life Sciences Medicinal Chemistry Microbiology Nodulation Organic Chemistry Pathogens Peptides Peptides - metabolism Post-translation Protein Processing, Post-Translational - genetics Rhizobium - genetics Thiazoline |
| title | Post translational modifications of Trifolitoxin: a blue fluorescent peptide antibiotic |
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