@ARTICLE{TreeBASE2Ref24484,
author = {Tsvetan Radoslavov Bachvaroff and Ernest P Williams and Rosemary Jagus and Allen R Place},
title = {A noncryptic noncanonical multi-module PKS/NRPS found in dinoflagellates},
year = {2015},
keywords = {polyketide, non-ribosomal peptide synthase, dinoflagellate, Burkholderia},
doi = {},
url = {http://},
pmid = {},
journal = {Proceedings of the 16th International Conference on Harmful Algae. International Society for the Study of Harmful Algae 2015},
volume = {},
number = {},
pages = {},
abstract = {Dinoflagellates produce a variety of compounds, likely using polyketide synthases (PKS) or non-ribosomal peptide synthases (NRPS) based on structure and labeling studies. An 8 domain hybrid PKS/NRPS greater than 8 thousand bases was identified in 19 deeply sequenced dinoflagellate transcriptomes. The gene was found in data from Oxyrrhis marina and 18 core dinoflagellates, but not the syndinean genus Amoebophrya. Spliced leaders, introns, and multiple subtle sequence variants were found, ruling out bacterial contaminants and confirming the dinoflagellate source of the sequences. However, the domain content and order are shared with a bacterial cryptic noncanonical PKS/NRPS (BurA) from Burkholderia spp., indicating a likely bacterial origin through horizontal gene transfer. The dinoflagellate and bacterial genes also have similar amino acid and malonyl CoA binding pockets. Based on labeling studies from Burkholderia spp. the dinoflagellates may use methionine to produce a propionate for incorporation into natural products.}
}
Citation for Study 17476
Citation title:
"A noncryptic noncanonical multi-module PKS/NRPS found in dinoflagellates".
Study name:
"A noncryptic noncanonical multi-module PKS/NRPS found in dinoflagellates".
This study is part of submission 17476
(Status: Published).
Citation
Bachvaroff T.R., Williams E.P., Jagus R., & Place A.R. 2015. A noncryptic noncanonical multi-module PKS/NRPS found in dinoflagellates. Proceedings of the 16th International Conference on Harmful Algae. International Society for the Study of Harmful Algae 2015, .
Authors
-
Bachvaroff T.R.
(submitter)
301 367 0559
-
Williams E.P.
-
Jagus R.
-
Place A.R.
Abstract
Dinoflagellates produce a variety of compounds, likely using polyketide synthases (PKS) or non-ribosomal peptide synthases (NRPS) based on structure and labeling studies. An 8 domain hybrid PKS/NRPS greater than 8 thousand bases was identified in 19 deeply sequenced dinoflagellate transcriptomes. The gene was found in data from Oxyrrhis marina and 18 core dinoflagellates, but not the syndinean genus Amoebophrya. Spliced leaders, introns, and multiple subtle sequence variants were found, ruling out bacterial contaminants and confirming the dinoflagellate source of the sequences. However, the domain content and order are shared with a bacterial cryptic noncanonical PKS/NRPS (BurA) from Burkholderia spp., indicating a likely bacterial origin through horizontal gene transfer. The dinoflagellate and bacterial genes also have similar amino acid and malonyl CoA binding pockets. Based on labeling studies from Burkholderia spp. the dinoflagellates may use methionine to produce a propionate for incorporation into natural products.
Keywords
polyketide, non-ribosomal peptide synthase, dinoflagellate, Burkholderia
External links
About this resource
- Canonical resource URI:
http://purl.org/phylo/treebase/phylows/study/TB2:S17476
- Other versions:
Nexus
NeXML
- Show BibTeX reference
@ARTICLE{TreeBASE2Ref24484,
author = {Tsvetan Radoslavov Bachvaroff and Ernest P Williams and Rosemary Jagus and Allen R Place},
title = {A noncryptic noncanonical multi-module PKS/NRPS found in dinoflagellates},
year = {2015},
keywords = {polyketide, non-ribosomal peptide synthase, dinoflagellate, Burkholderia},
doi = {},
url = {http://},
pmid = {},
journal = {Proceedings of the 16th International Conference on Harmful Algae. International Society for the Study of Harmful Algae 2015},
volume = {},
number = {},
pages = {},
abstract = {Dinoflagellates produce a variety of compounds, likely using polyketide synthases (PKS) or non-ribosomal peptide synthases (NRPS) based on structure and labeling studies. An 8 domain hybrid PKS/NRPS greater than 8 thousand bases was identified in 19 deeply sequenced dinoflagellate transcriptomes. The gene was found in data from Oxyrrhis marina and 18 core dinoflagellates, but not the syndinean genus Amoebophrya. Spliced leaders, introns, and multiple subtle sequence variants were found, ruling out bacterial contaminants and confirming the dinoflagellate source of the sequences. However, the domain content and order are shared with a bacterial cryptic noncanonical PKS/NRPS (BurA) from Burkholderia spp., indicating a likely bacterial origin through horizontal gene transfer. The dinoflagellate and bacterial genes also have similar amino acid and malonyl CoA binding pockets. Based on labeling studies from Burkholderia spp. the dinoflagellates may use methionine to produce a propionate for incorporation into natural products.}
}
- Show RIS reference
TY - JOUR
ID - 24484
AU - Bachvaroff,Tsvetan Radoslavov
AU - Williams,Ernest P
AU - Jagus,Rosemary
AU - Place,Allen R
T1 - A noncryptic noncanonical multi-module PKS/NRPS found in dinoflagellates
PY - 2015
KW - polyketide
KW - non-ribosomal peptide synthase
KW - dinoflagellate
KW - Burkholderia
UR - http://dx.doi.org/
N2 - Dinoflagellates produce a variety of compounds, likely using polyketide synthases (PKS) or non-ribosomal peptide synthases (NRPS) based on structure and labeling studies. An 8 domain hybrid PKS/NRPS greater than 8 thousand bases was identified in 19 deeply sequenced dinoflagellate transcriptomes. The gene was found in data from Oxyrrhis marina and 18 core dinoflagellates, but not the syndinean genus Amoebophrya. Spliced leaders, introns, and multiple subtle sequence variants were found, ruling out bacterial contaminants and confirming the dinoflagellate source of the sequences. However, the domain content and order are shared with a bacterial cryptic noncanonical PKS/NRPS (BurA) from Burkholderia spp., indicating a likely bacterial origin through horizontal gene transfer. The dinoflagellate and bacterial genes also have similar amino acid and malonyl CoA binding pockets. Based on labeling studies from Burkholderia spp. the dinoflagellates may use methionine to produce a propionate for incorporation into natural products.
L3 -
JF - Proceedings of the 16th International Conference on Harmful Algae. International Society for the Study of Harmful Algae 2015
VL -
IS -
ER -
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