Evolutionary relationships of microbial aromatic prenyltransferases.

The linkage of isoprenoid and aromatic moieties, catalyzed by aromatic prenyltransferases (PTases), leads to an impressive diversity of primary and secondary metabolites, including important pharmaceuticals and toxins. A few years ago, a hydroxynaphthalene PTase, NphB, featuring a novel ten-stranded...

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Autores principales:	Tobias Bonitz, Vikram Alva, Orwah Saleh, Andrei N Lupas, Lutz Heide
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/76d2a61949754015883243e0f8fd21f0
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spelling	oai:doaj.org-article:76d2a61949754015883243e0f8fd21f02021-11-18T07:33:24ZEvolutionary relationships of microbial aromatic prenyltransferases.1932-620310.1371/journal.pone.0027336https://doaj.org/article/76d2a61949754015883243e0f8fd21f02011-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/22140437/?tool=EBIhttps://doaj.org/toc/1932-6203The linkage of isoprenoid and aromatic moieties, catalyzed by aromatic prenyltransferases (PTases), leads to an impressive diversity of primary and secondary metabolites, including important pharmaceuticals and toxins. A few years ago, a hydroxynaphthalene PTase, NphB, featuring a novel ten-stranded β-barrel fold was identified in Streptomyces sp. strain CL190. This fold, termed the PT-barrel, is formed of five tandem ααββ structural repeats and remained exclusive to the NphB family until its recent discovery in the DMATS family of indole PTases. Members of these two families exist only in fungi and bacteria, and all of them appear to catalyze the prenylation of aromatic substrates involved in secondary metabolism. Sequence comparisons using PSI-BLAST do not yield matches between these two families, suggesting that they may have converged upon the same fold independently. However, we now provide evidence for a common ancestry for the NphB and DMATS families of PTases. We also identify sequence repeats that coincide with the structural repeats in proteins belonging to these two families. Therefore we propose that the PT-barrel arose by amplification of an ancestral ααββ module. In view of their homology and their similarities in structure and function, we propose to group the NphB and DMATS families together into a single superfamily, the PT-barrel superfamily.Tobias BonitzVikram AlvaOrwah SalehAndrei N LupasLutz HeidePublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 11, p e27336 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Tobias Bonitz Vikram Alva Orwah Saleh Andrei N Lupas Lutz Heide Evolutionary relationships of microbial aromatic prenyltransferases.
description	The linkage of isoprenoid and aromatic moieties, catalyzed by aromatic prenyltransferases (PTases), leads to an impressive diversity of primary and secondary metabolites, including important pharmaceuticals and toxins. A few years ago, a hydroxynaphthalene PTase, NphB, featuring a novel ten-stranded β-barrel fold was identified in Streptomyces sp. strain CL190. This fold, termed the PT-barrel, is formed of five tandem ααββ structural repeats and remained exclusive to the NphB family until its recent discovery in the DMATS family of indole PTases. Members of these two families exist only in fungi and bacteria, and all of them appear to catalyze the prenylation of aromatic substrates involved in secondary metabolism. Sequence comparisons using PSI-BLAST do not yield matches between these two families, suggesting that they may have converged upon the same fold independently. However, we now provide evidence for a common ancestry for the NphB and DMATS families of PTases. We also identify sequence repeats that coincide with the structural repeats in proteins belonging to these two families. Therefore we propose that the PT-barrel arose by amplification of an ancestral ααββ module. In view of their homology and their similarities in structure and function, we propose to group the NphB and DMATS families together into a single superfamily, the PT-barrel superfamily.
format	article
author	Tobias Bonitz Vikram Alva Orwah Saleh Andrei N Lupas Lutz Heide
author_facet	Tobias Bonitz Vikram Alva Orwah Saleh Andrei N Lupas Lutz Heide
author_sort	Tobias Bonitz
title	Evolutionary relationships of microbial aromatic prenyltransferases.
title_short	Evolutionary relationships of microbial aromatic prenyltransferases.
title_full	Evolutionary relationships of microbial aromatic prenyltransferases.
title_fullStr	Evolutionary relationships of microbial aromatic prenyltransferases.
title_full_unstemmed	Evolutionary relationships of microbial aromatic prenyltransferases.
title_sort	evolutionary relationships of microbial aromatic prenyltransferases.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/76d2a61949754015883243e0f8fd21f0
work_keys_str_mv	AT tobiasbonitz evolutionaryrelationshipsofmicrobialaromaticprenyltransferases AT vikramalva evolutionaryrelationshipsofmicrobialaromaticprenyltransferases AT orwahsaleh evolutionaryrelationshipsofmicrobialaromaticprenyltransferases AT andreinlupas evolutionaryrelationshipsofmicrobialaromaticprenyltransferases AT lutzheide evolutionaryrelationshipsofmicrobialaromaticprenyltransferases
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Evolutionary relationships of microbial aromatic prenyltransferases.

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