Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane.
Identifieur interne : 002017 ( PubMed/Checkpoint ); précédent : 002016; suivant : 002018Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane.
Auteurs : Alex Dajkovic [France] ; Elizabeth Hinde ; Calum Mackichan [France] ; Rut Carballido-Lopez [France]Source :
- PloS one [ 1932-6203 ] ; 2016.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Bacterial Proteins.
- chemical , secretion : Adenosine Triphosphatases, Bacterial Proteins, SEC Translocation Channels.
- metabolism : Bacillus subtilis, Cell Membrane, Cytosol.
- Protein Binding, Protein Transport.
Abstract
In prokaryotes, about one third of cellular proteins are translocated across the plasma membrane or inserted into it by concerted action of the cytoplasmic ATPase SecA and the universally conserved SecYEG heterotrimeric polypeptide-translocating pore. Secretion complexes have been reported to localize in specific subcellular sites in Bacillus subtilis. In this work, we used a combination of total internal reflection microscopy, scanning fluorescence correlation spectroscopy, and pair correlation function to study the localization and dynamics of SecA and SecY in growing Bacillus subtilis cells. Both SecA and SecY localized in transient and dynamic foci in the cytoplasmic membrane, which displayed no higher-level organization in helices. Foci of SecA and SecY were in constant flux with freely diffusing SecA and SecY molecules. Scanning FCS confirmed the existence of populations of cellular SecA and SecY molecules with a wide range of diffusion coefficients. Diffusion of SecY as an uncomplexed molecular species was short-lived and only local while SecY complexed with its protein partners traversed distances of over half a micrometer in the cell.
DOI: 10.1371/journal.pone.0157899
PubMed: 27336478
Affiliations:
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pubmed:27336478Le document en format XML
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INRA, AgroParisTech, Université Paris-Saclay, 78350 Jouy-en-Josas, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Micalis Institute, INRA, AgroParisTech, Université Paris-Saclay, 78350 Jouy-en-Josas</wicri:regionArea><placeName><region type="region" nuts="2">Île-de-France</region><settlement type="city">Jouy-en-Josas</settlement></placeName></affiliation></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adenosine Triphosphatases (secretion)</term><term>Bacillus subtilis (metabolism)</term><term>Bacterial Proteins (metabolism)</term><term>Bacterial Proteins (secretion)</term><term>Cell Membrane (metabolism)</term><term>Cytosol (metabolism)</term><term>Protein Binding</term><term>Protein Transport</term><term>SEC Translocation Channels (secretion)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adenosine triphosphatases (sécrétion)</term><term>Bacillus subtilis (métabolisme)</term><term>Canaux de translocation SEC (sécrétion)</term><term>Cytosol (métabolisme)</term><term>Liaison aux protéines</term><term>Membrane cellulaire (métabolisme)</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines bactériennes (sécrétion)</term><term>Transport de protéines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="secretion" xml:lang="en"><term>Adenosine Triphosphatases</term><term>Bacterial Proteins</term><term>SEC Translocation Channels</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Bacillus subtilis</term><term>Cell Membrane</term><term>Cytosol</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Bacillus subtilis</term><term>Cytosol</term><term>Membrane cellulaire</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" qualifier="sécrétion" xml:lang="fr"><term>Adenosine triphosphatases</term><term>Canaux de translocation SEC</term><term>Protéines bactériennes</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Protein Binding</term><term>Protein Transport</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Liaison aux protéines</term><term>Transport de protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">In prokaryotes, about one third of cellular proteins are translocated across the plasma membrane or inserted into it by concerted action of the cytoplasmic ATPase SecA and the universally conserved SecYEG heterotrimeric polypeptide-translocating pore. Secretion complexes have been reported to localize in specific subcellular sites in Bacillus subtilis. In this work, we used a combination of total internal reflection microscopy, scanning fluorescence correlation spectroscopy, and pair correlation function to study the localization and dynamics of SecA and SecY in growing Bacillus subtilis cells. Both SecA and SecY localized in transient and dynamic foci in the cytoplasmic membrane, which displayed no higher-level organization in helices. Foci of SecA and SecY were in constant flux with freely diffusing SecA and SecY molecules. Scanning FCS confirmed the existence of populations of cellular SecA and SecY molecules with a wide range of diffusion coefficients. Diffusion of SecY as an uncomplexed molecular species was short-lived and only local while SecY complexed with its protein partners traversed distances of over half a micrometer in the cell.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27336478</PMID><DateCreated><Year>2016</Year><Month>06</Month><Day>24</Day></DateCreated><DateCompleted><Year>2017</Year><Month>07</Month><Day>24</Day></DateCompleted><DateRevised><Year>2017</Year><Month>09</Month><Day>22</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>11</Volume><Issue>6</Issue><PubDate><Year>2016</Year></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>Dynamic Organization of SecA and SecY Secretion Complexes in the B. subtilis Membrane.</ArticleTitle><Pagination><MedlinePgn>e0157899</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0157899</ELocationID><Abstract><AbstractText>In prokaryotes, about one third of cellular proteins are translocated across the plasma membrane or inserted into it by concerted action of the cytoplasmic ATPase SecA and the universally conserved SecYEG heterotrimeric polypeptide-translocating pore. Secretion complexes have been reported to localize in specific subcellular sites in Bacillus subtilis. In this work, we used a combination of total internal reflection microscopy, scanning fluorescence correlation spectroscopy, and pair correlation function to study the localization and dynamics of SecA and SecY in growing Bacillus subtilis cells. Both SecA and SecY localized in transient and dynamic foci in the cytoplasmic membrane, which displayed no higher-level organization in helices. Foci of SecA and SecY were in constant flux with freely diffusing SecA and SecY molecules. Scanning FCS confirmed the existence of populations of cellular SecA and SecY molecules with a wide range of diffusion coefficients. Diffusion of SecY as an uncomplexed molecular species was short-lived and only local while SecY complexed with its protein partners traversed distances of over half a micrometer in the cell.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Dajkovic</LastName><ForeName>Alex</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Micalis Institute, INRA, AgroParisTech, Université Paris-Saclay, 78350 Jouy-en-Josas, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hinde</LastName><ForeName>Elizabeth</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>School of Medical Sciences, University of New South Wales, Sydney, Australia 2052.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>MacKichan</LastName><ForeName>Calum</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Micalis Institute, INRA, AgroParisTech, Université Paris-Saclay, 78350 Jouy-en-Josas, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Carballido-Lopez</LastName><ForeName>Rut</ForeName><Initials>R</Initials><AffiliationInfo><Affiliation>Micalis Institute, INRA, AgroParisTech, Université Paris-Saclay, 78350 Jouy-en-Josas, France.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>311231</GrantID><Agency>European Research Council</Agency><Country>International</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2016</Year><Month>06</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000069816">SEC Translocation Channels</NameOfSubstance></Chemical><Chemical><RegistryNumber>119129-39-4</RegistryNumber><NameOfSubstance UI="C066220">SecA protein, Bacteria</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.6.1.-</RegistryNumber><NameOfSubstance UI="D000251">Adenosine Triphosphatases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><CommentsCorrectionsList><CommentsCorrections RefType="Cites"><RefSource>Mol Microbiol. 2003 Oct;50(1):45-60</RefSource><PMID Version="1">14507362</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Mol Biol Cell. 2009 Oct;20(19):4256-66</RefSource><PMID Version="1">19656854</PMID></CommentsCorrections><CommentsCorrections RefType="Cites"><RefSource>Res Microbiol. 2013 Jul-Aug;164(6):497-504</RefSource><PMID Version="1">23538404</PMID></CommentsCorrections><CommentsCorrections 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