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Bacterial Transmembrane Proteins that Lack N-Terminal Signal Sequences

Tail-anchored membrane proteins (TAMPs), a class of proteins characterized by their lack of N-terminal signal sequence and Sec-independent membrane targeting, play critical roles in apoptosis, vesicle trafficking and other vital processes in eukaryotic organisms. Until recently, this class of membra...

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Detalles Bibliográficos
Autores principales: Craney, Arryn, Tahlan, Kapil, Andrews, David, Nodwell, Justin
Formato: Texto
Lenguaje:English
Publicado: Public Library of Science 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3087755/
https://www.ncbi.nlm.nih.gov/pubmed/21573234
http://dx.doi.org/10.1371/journal.pone.0019421
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author Craney, Arryn
Tahlan, Kapil
Andrews, David
Nodwell, Justin
author_facet Craney, Arryn
Tahlan, Kapil
Andrews, David
Nodwell, Justin
author_sort Craney, Arryn
collection PubMed
description Tail-anchored membrane proteins (TAMPs), a class of proteins characterized by their lack of N-terminal signal sequence and Sec-independent membrane targeting, play critical roles in apoptosis, vesicle trafficking and other vital processes in eukaryotic organisms. Until recently, this class of membrane proteins has been unknown in bacteria. Here we present the results of bioinformatic analysis revealing proteins that are superficially similar to eukaryotic TAMPs in the bacterium Streptomyces coelicolor. We demonstrate that at least four of these proteins are bona fide membrane-spanning proteins capable of targeting to the membrane in the absence of their N-terminus and the C-terminal membrane-spanning domain is sufficient for membrane targeting. Several of these proteins, including a serine/threonine kinase and the SecE component of the Sec translocon, are widely conserved in bacteria.
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spelling pubmed-30877552011-05-13 Bacterial Transmembrane Proteins that Lack N-Terminal Signal Sequences Craney, Arryn Tahlan, Kapil Andrews, David Nodwell, Justin PLoS One Research Article Tail-anchored membrane proteins (TAMPs), a class of proteins characterized by their lack of N-terminal signal sequence and Sec-independent membrane targeting, play critical roles in apoptosis, vesicle trafficking and other vital processes in eukaryotic organisms. Until recently, this class of membrane proteins has been unknown in bacteria. Here we present the results of bioinformatic analysis revealing proteins that are superficially similar to eukaryotic TAMPs in the bacterium Streptomyces coelicolor. We demonstrate that at least four of these proteins are bona fide membrane-spanning proteins capable of targeting to the membrane in the absence of their N-terminus and the C-terminal membrane-spanning domain is sufficient for membrane targeting. Several of these proteins, including a serine/threonine kinase and the SecE component of the Sec translocon, are widely conserved in bacteria. Public Library of Science 2011-05-04 /pmc/articles/PMC3087755/ /pubmed/21573234 http://dx.doi.org/10.1371/journal.pone.0019421 Text en Craney et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Craney, Arryn
Tahlan, Kapil
Andrews, David
Nodwell, Justin
Bacterial Transmembrane Proteins that Lack N-Terminal Signal Sequences
title Bacterial Transmembrane Proteins that Lack N-Terminal Signal Sequences
title_full Bacterial Transmembrane Proteins that Lack N-Terminal Signal Sequences
title_fullStr Bacterial Transmembrane Proteins that Lack N-Terminal Signal Sequences
title_full_unstemmed Bacterial Transmembrane Proteins that Lack N-Terminal Signal Sequences
title_short Bacterial Transmembrane Proteins that Lack N-Terminal Signal Sequences
title_sort bacterial transmembrane proteins that lack n-terminal signal sequences
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3087755/
https://www.ncbi.nlm.nih.gov/pubmed/21573234
http://dx.doi.org/10.1371/journal.pone.0019421
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