Mutational and Bioinformatic Analysis of Haloarchaeal Lipobox-Containing Proteins
Identifieur interne : 000186 ( Ncbi/Checkpoint ); précédent : 000185; suivant : 000187Mutational and Bioinformatic Analysis of Haloarchaeal Lipobox-Containing Proteins
Auteurs : Stefanie Storf [États-Unis] ; Friedhelm Pfeiffer [Allemagne] ; Kieran Dilks [États-Unis] ; Zhong Qiang Chen ; Saheed Imam [États-Unis] ; Mechthild Pohlschröder [États-Unis]Source :
- Archaea [ 1472-3646 ] ; 2010.
Abstract
A conserved lipid-modified cysteine found in a protein motif commonly referred to as a lipobox mediates the membrane anchoring of a subset of proteins transported across the bacterial cytoplasmic membrane via the Sec pathway. Sequenced haloarchaeal genomes encode many putative lipoproteins and recent studies have confirmed the importance of the conserved lipobox cysteine for signal peptide processing of three lipobox-containing proteins in the model archaeon
Url:
DOI: 10.1155/2010/410975
PubMed: 20886060
PubMed Central: 2945643
Affiliations:
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Mutational and Bioinformatic Analysis of Haloarchaeal Lipobox-Containing Proteins</title>
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<series><title level="j">Archaea</title>
<idno type="ISSN">1472-3646</idno>
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<imprint><date when="2010">2010</date>
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<front><div type="abstract" xml:lang="en"><p>A conserved lipid-modified cysteine found in a protein motif commonly referred to as a lipobox mediates the membrane anchoring of a subset of proteins transported across the bacterial cytoplasmic membrane via the Sec pathway. Sequenced haloarchaeal genomes encode many putative lipoproteins and recent studies have confirmed the importance of the conserved lipobox cysteine for signal peptide processing of three lipobox-containing proteins in the model archaeon <italic>Haloferax volcanii</italic>
. We have extended these <italic>in vivo</italic>
analyses to additional <italic>Hfx. volcanii</italic>
substrates, supporting our previous <italic>in silico</italic>
predictions and confirming the diversity of predicted <italic>Hfx. volcanii</italic>
lipoproteins. Moreover, using extensive comparative secretome analyses, we identified genes encodining putative lipoproteins across a wide range of archaeal species. While our <italic>in silico</italic>
analyses, supported by <italic>in vivo</italic>
data, indicate that most haloarchaeal lipoproteins are Tat substrates, these analyses also predict that many crenarchaeal species lack lipoproteins altogether and that other archaea, such as nonhalophilic euryarchaeal species, transport lipoproteins via the Sec pathway. To facilitate the identification of genes that encode potential haloarchaeal Tat-lipoproteins, we have developed TatLipo, a bioinformatic tool designed to detect lipoboxes in haloarchaeal Tat signal peptides. Our results provide a strong foundation for future studies aimed at identifying components of the archaeal lipoprotein biogenesis pathway.</p>
</div>
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<tree><noCountry><name sortKey="Chen, Zhong Qiang" sort="Chen, Zhong Qiang" uniqKey="Chen Z" first="Zhong Qiang" last="Chen">Zhong Qiang Chen</name>
</noCountry>
<country name="États-Unis"><region name="Pennsylvanie"><name sortKey="Storf, Stefanie" sort="Storf, Stefanie" uniqKey="Storf S" first="Stefanie" last="Storf">Stefanie Storf</name>
</region>
<name sortKey="Dilks, Kieran" sort="Dilks, Kieran" uniqKey="Dilks K" first="Kieran" last="Dilks">Kieran Dilks</name>
<name sortKey="Imam, Saheed" sort="Imam, Saheed" uniqKey="Imam S" first="Saheed" last="Imam">Saheed Imam</name>
<name sortKey="Pohlschroder, Mechthild" sort="Pohlschroder, Mechthild" uniqKey="Pohlschroder M" first="Mechthild" last="Pohlschröder">Mechthild Pohlschröder</name>
</country>
<country name="Allemagne"><noRegion><name sortKey="Pfeiffer, Friedhelm" sort="Pfeiffer, Friedhelm" uniqKey="Pfeiffer F" first="Friedhelm" last="Pfeiffer">Friedhelm Pfeiffer</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>
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