Unexpected Diversity of Signal Peptides in Prokaryotes

ABSTRACT Signal peptides are a cornerstone mechanism for cellular protein localization, yet until now experimental determination of signal peptides has come from only a narrow taxonomic sampling. As a result, the dominant view is that Sec-cleaved signal peptides in prokaryotes are defined by a canon...

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Autores principales:	Samuel H. Payne, Stefano Bonissone, Si Wu, Roslyn N. Brown, Dmitry N. Ivankov, Dmitrij Frishman, Ljiljana Paša-Tolić, Richard D. Smith, Pavel A. Pevzner
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2012
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/d97b16dedef64b4e89c86a8a1c5f39b4
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spelling	oai:doaj.org-article:d97b16dedef64b4e89c86a8a1c5f39b42021-11-15T15:39:11ZUnexpected Diversity of Signal Peptides in Prokaryotes10.1128/mBio.00339-122150-7511https://doaj.org/article/d97b16dedef64b4e89c86a8a1c5f39b42012-12-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00339-12https://doaj.org/toc/2150-7511ABSTRACT Signal peptides are a cornerstone mechanism for cellular protein localization, yet until now experimental determination of signal peptides has come from only a narrow taxonomic sampling. As a result, the dominant view is that Sec-cleaved signal peptides in prokaryotes are defined by a canonical AxA motif. Although other residues are permitted in the motif, alanine is by far the most common. Here we broadly examine proteomics data to reveal the signal peptide sequences for 32 bacterial and archaeal organisms from nine phyla and demonstrate that this alanine preference is not universal. Discoveries include fundamentally distinct signal peptide motifs from Alphaproteobacteria, Spirochaetes, Thermotogae and Euryarchaeota. In these novel motifs, alanine is no longer the dominant residue but has been replaced in a different way for each taxon. Surprisingly, divergent motifs correlate with a proteome-wide reduction in alanine. Computational analyses of ~1,500 genomes reveal numerous major evolutionary clades which have replaced the canonical signal peptide sequence with novel motifs. IMPORTANCE This article replaces a widely held general model with a more detailed model describing phylogenetically correlated variation in motifs for Sec secretion.Samuel H. PayneStefano BonissoneSi WuRoslyn N. BrownDmitry N. IvankovDmitrij FrishmanLjiljana Paša-TolićRichard D. SmithPavel A. PevznerAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 3, Iss 6 (2012)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 Samuel H. Payne Stefano Bonissone Si Wu Roslyn N. Brown Dmitry N. Ivankov Dmitrij Frishman Ljiljana Paša-Tolić Richard D. Smith Pavel A. Pevzner Unexpected Diversity of Signal Peptides in Prokaryotes
description	ABSTRACT Signal peptides are a cornerstone mechanism for cellular protein localization, yet until now experimental determination of signal peptides has come from only a narrow taxonomic sampling. As a result, the dominant view is that Sec-cleaved signal peptides in prokaryotes are defined by a canonical AxA motif. Although other residues are permitted in the motif, alanine is by far the most common. Here we broadly examine proteomics data to reveal the signal peptide sequences for 32 bacterial and archaeal organisms from nine phyla and demonstrate that this alanine preference is not universal. Discoveries include fundamentally distinct signal peptide motifs from Alphaproteobacteria, Spirochaetes, Thermotogae and Euryarchaeota. In these novel motifs, alanine is no longer the dominant residue but has been replaced in a different way for each taxon. Surprisingly, divergent motifs correlate with a proteome-wide reduction in alanine. Computational analyses of ~1,500 genomes reveal numerous major evolutionary clades which have replaced the canonical signal peptide sequence with novel motifs. IMPORTANCE This article replaces a widely held general model with a more detailed model describing phylogenetically correlated variation in motifs for Sec secretion.
format	article
author	Samuel H. Payne Stefano Bonissone Si Wu Roslyn N. Brown Dmitry N. Ivankov Dmitrij Frishman Ljiljana Paša-Tolić Richard D. Smith Pavel A. Pevzner
author_facet	Samuel H. Payne Stefano Bonissone Si Wu Roslyn N. Brown Dmitry N. Ivankov Dmitrij Frishman Ljiljana Paša-Tolić Richard D. Smith Pavel A. Pevzner
author_sort	Samuel H. Payne
title	Unexpected Diversity of Signal Peptides in Prokaryotes
title_short	Unexpected Diversity of Signal Peptides in Prokaryotes
title_full	Unexpected Diversity of Signal Peptides in Prokaryotes
title_fullStr	Unexpected Diversity of Signal Peptides in Prokaryotes
title_full_unstemmed	Unexpected Diversity of Signal Peptides in Prokaryotes
title_sort	unexpected diversity of signal peptides in prokaryotes
publisher	American Society for Microbiology
publishDate	2012
url	https://doaj.org/article/d97b16dedef64b4e89c86a8a1c5f39b4
work_keys_str_mv	AT samuelhpayne unexpecteddiversityofsignalpeptidesinprokaryotes AT stefanobonissone unexpecteddiversityofsignalpeptidesinprokaryotes AT siwu unexpecteddiversityofsignalpeptidesinprokaryotes AT roslynnbrown unexpecteddiversityofsignalpeptidesinprokaryotes AT dmitrynivankov unexpecteddiversityofsignalpeptidesinprokaryotes AT dmitrijfrishman unexpecteddiversityofsignalpeptidesinprokaryotes AT ljiljanapasatolic unexpecteddiversityofsignalpeptidesinprokaryotes AT richarddsmith unexpecteddiversityofsignalpeptidesinprokaryotes AT pavelapevzner unexpecteddiversityofsignalpeptidesinprokaryotes
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Unexpected Diversity of Signal Peptides in Prokaryotes

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