Abstract
The localization and membrane topology of the Yersinia pestis. YscJ lipoprotein an essential component of the type III secretion apparatus, was investigated: YscJ was demonstrated to be an inner membrane (IM) lipoprotein that is anchored to the periplasmic face of the IM via an N-terminal lipid moiety and via a C-terminal transmembrane (TM) domain. Localization of the N-terminal lipid moiety to the IM occurred regardless of the amino-acid residues found in the +2 or +3 positions. IM localization was dependent upon an intact N-terminal domain (amino acids + 1 to + 61), suggesting that this region plays a role in YscJ localization. In contrast, the YscJ C-terminal domain and TM domain were not required for IM localization N-terminal sequence analysis demonstrated that a significant proportion of membrane-localized YscJ laoks N-acylation, the final modification required for Lol-dependent transport of a lipoprotein to the OM. Interestingly, attachment of the N-terminus to the IM was required for YscJ function; however, the YscJ secretion signal and lipo-box could be functionally replaced by the first TM domain of the YscV protein, suggesting that the mechanism of attachment to the IM was not critical.
| Original language | English |
|---|---|
| Pages (from-to) | 593-607 |
| Number of pages | 15 |
| Journal | Microbiology |
| Volume | 154 |
| Issue number | 2 |
| DOIs | |
| State | Published - Feb 1 2008 |
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ASJC Scopus subject areas
- Microbiology
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Membrane localization and topology of the Yersinia pestis YscJ lipoprotein. / Silva-Herzog, Eugenia; Ferracci, Franco; Jackson, Michael W.; Joseph, Sabrina S.; Plano, Gregory V.
In: Microbiology, Vol. 154, No. 2, 01.02.2008, p. 593-607.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Membrane localization and topology of the Yersinia pestis YscJ lipoprotein
AU - Silva-Herzog, Eugenia
AU - Ferracci, Franco
AU - Jackson, Michael W.
AU - Joseph, Sabrina S.
AU - Plano, Gregory V
PY - 2008/2/1
Y1 - 2008/2/1
N2 - The localization and membrane topology of the Yersinia pestis. YscJ lipoprotein an essential component of the type III secretion apparatus, was investigated: YscJ was demonstrated to be an inner membrane (IM) lipoprotein that is anchored to the periplasmic face of the IM via an N-terminal lipid moiety and via a C-terminal transmembrane (TM) domain. Localization of the N-terminal lipid moiety to the IM occurred regardless of the amino-acid residues found in the +2 or +3 positions. IM localization was dependent upon an intact N-terminal domain (amino acids + 1 to + 61), suggesting that this region plays a role in YscJ localization. In contrast, the YscJ C-terminal domain and TM domain were not required for IM localization N-terminal sequence analysis demonstrated that a significant proportion of membrane-localized YscJ laoks N-acylation, the final modification required for Lol-dependent transport of a lipoprotein to the OM. Interestingly, attachment of the N-terminus to the IM was required for YscJ function; however, the YscJ secretion signal and lipo-box could be functionally replaced by the first TM domain of the YscV protein, suggesting that the mechanism of attachment to the IM was not critical.
AB - The localization and membrane topology of the Yersinia pestis. YscJ lipoprotein an essential component of the type III secretion apparatus, was investigated: YscJ was demonstrated to be an inner membrane (IM) lipoprotein that is anchored to the periplasmic face of the IM via an N-terminal lipid moiety and via a C-terminal transmembrane (TM) domain. Localization of the N-terminal lipid moiety to the IM occurred regardless of the amino-acid residues found in the +2 or +3 positions. IM localization was dependent upon an intact N-terminal domain (amino acids + 1 to + 61), suggesting that this region plays a role in YscJ localization. In contrast, the YscJ C-terminal domain and TM domain were not required for IM localization N-terminal sequence analysis demonstrated that a significant proportion of membrane-localized YscJ laoks N-acylation, the final modification required for Lol-dependent transport of a lipoprotein to the OM. Interestingly, attachment of the N-terminus to the IM was required for YscJ function; however, the YscJ secretion signal and lipo-box could be functionally replaced by the first TM domain of the YscV protein, suggesting that the mechanism of attachment to the IM was not critical.
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UR - http://www.scopus.com/inward/citedby.url?scp=39749175060&partnerID=8YFLogxK
U2 - 10.1099/mic.0.2007/013045-0
DO - 10.1099/mic.0.2007/013045-0
M3 - Article
C2 - 18227263
AN - SCOPUS:39749175060
VL - 154
SP - 593
EP - 607
JO - Microbiology (United Kingdom)
JF - Microbiology (United Kingdom)
SN - 1350-0872
IS - 2
ER -