Signal sequence directs localized secretion of bacterial surface proteins.
(2006) In Nature 442(7105). p.943-946- Abstract
- All living cells require specific mechanisms that target proteins to the cell surface. In eukaryotes, the first part of this process involves recognition in the endoplasmic reticulum of amino-terminal signal sequences and translocation through Sec translocons, whereas subsequent targeting to different surface locations is promoted by internal sorting signals(1). In bacteria, N-terminal signal sequences promote translocation across the cytoplasmic membrane, which surrounds the entire cell, but some proteins are nevertheless secreted in one part of the cell by poorly understood mechanisms(2,3). Here we analyse localized secretion in the Gram-positive pathogen Streptococcus pyogenes, and show that the signal sequences of two surface proteins,... (More)
- All living cells require specific mechanisms that target proteins to the cell surface. In eukaryotes, the first part of this process involves recognition in the endoplasmic reticulum of amino-terminal signal sequences and translocation through Sec translocons, whereas subsequent targeting to different surface locations is promoted by internal sorting signals(1). In bacteria, N-terminal signal sequences promote translocation across the cytoplasmic membrane, which surrounds the entire cell, but some proteins are nevertheless secreted in one part of the cell by poorly understood mechanisms(2,3). Here we analyse localized secretion in the Gram-positive pathogen Streptococcus pyogenes, and show that the signal sequences of two surface proteins, M protein and protein F ( PrtF), direct secretion to different subcellular regions. The signal sequence of M protein promotes secretion at the division septum, whereas that of PrtF preferentially promotes secretion at the old pole. Our work therefore shows that a signal sequence may contain information that directs the secretion of a protein to one subcellular region, in addition to its classical role in promoting secretion. This finding identifies a new level of complexity in protein translocation and emphasizes the potential of bacterial systems for the analysis of fundamental cell-biological problems(4). (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/159922
- author
- Carlsson, Fredric LU ; Stålhammar-Carlemalm, Margaretha LU ; Flärdh, Klas LU ; Sandin, Charlotta LU ; Carlemalm, Eric LU and Lindahl, Gunnar LU
- organization
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Nature
- volume
- 442
- issue
- 7105
- pages
- 943 - 946
- publisher
- Nature Publishing Group
- external identifiers
-
- pmid:16929299
- wos:000239960500043
- scopus:33747870454
- pmid:16929299
- ISSN
- 0028-0836
- DOI
- 10.1038/nature05021
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Electron Microscopy Unit (013100002), Division of Medical Microbiology (013250400), Molecular Cell Biology (432112241)
- id
- 9927cb26-c697-4dc1-944c-5ac0e66d21eb (old id 159922)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16929299&dopt=Abstract
- date added to LUP
- 2016-04-01 12:30:35
- date last changed
- 2022-03-29 01:51:52
@article{9927cb26-c697-4dc1-944c-5ac0e66d21eb,
abstract = {{All living cells require specific mechanisms that target proteins to the cell surface. In eukaryotes, the first part of this process involves recognition in the endoplasmic reticulum of amino-terminal signal sequences and translocation through Sec translocons, whereas subsequent targeting to different surface locations is promoted by internal sorting signals(1). In bacteria, N-terminal signal sequences promote translocation across the cytoplasmic membrane, which surrounds the entire cell, but some proteins are nevertheless secreted in one part of the cell by poorly understood mechanisms(2,3). Here we analyse localized secretion in the Gram-positive pathogen Streptococcus pyogenes, and show that the signal sequences of two surface proteins, M protein and protein F ( PrtF), direct secretion to different subcellular regions. The signal sequence of M protein promotes secretion at the division septum, whereas that of PrtF preferentially promotes secretion at the old pole. Our work therefore shows that a signal sequence may contain information that directs the secretion of a protein to one subcellular region, in addition to its classical role in promoting secretion. This finding identifies a new level of complexity in protein translocation and emphasizes the potential of bacterial systems for the analysis of fundamental cell-biological problems(4).}},
author = {{Carlsson, Fredric and Stålhammar-Carlemalm, Margaretha and Flärdh, Klas and Sandin, Charlotta and Carlemalm, Eric and Lindahl, Gunnar}},
issn = {{0028-0836}},
language = {{eng}},
number = {{7105}},
pages = {{943--946}},
publisher = {{Nature Publishing Group}},
series = {{Nature}},
title = {{Signal sequence directs localized secretion of bacterial surface proteins.}},
url = {{http://dx.doi.org/10.1038/nature05021}},
doi = {{10.1038/nature05021}},
volume = {{442}},
year = {{2006}},
}