Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins

Leyton, Denisse L., Sevastsyanovich, Yanina R., Browning, Douglas F., Rossiter, Amanda E., Wells, Timothy J., Fitzpatrick, Rebecca E., Overduin, Michael, Cunningham, Adam F. and Henderson, Ian R. (2011) Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins. Journal of Biological Chemistry, 286 49: 42283-42291. doi:10.1074/jbc.M111.306118

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Author Leyton, Denisse L.
Sevastsyanovich, Yanina R.
Browning, Douglas F.
Rossiter, Amanda E.
Wells, Timothy J.
Fitzpatrick, Rebecca E.
Overduin, Michael
Cunningham, Adam F.
Henderson, Ian R.
Title Size and conformation limits to secretion of disulfide-bonded loops in autotransporter proteins
Journal name Journal of Biological Chemistry   Check publisher's open access policy
ISSN 0021-9258
Publication date 2011-12-09
Sub-type Article (original research)
DOI 10.1074/jbc.M111.306118
Open Access Status File (Publisher version)
Volume 286
Issue 49
Start page 42283
End page 42291
Total pages 9
Place of publication Bethesda, MD United States
Publisher American Society for Biochemistry and Molecular Biology
Language eng
Abstract Autotransporters are a superfamily of virulence factors typified by a channel-forming C terminus that facilitates translocation of the functional N-terminal passenger domain across the outer membrane of Gram-negative bacteria. This final step in the secretion of autotransporters requires a translocation-competent conformation for the passenger domain that differs markedly from the structure of the fully folded secreted protein. The nature of the translocation-competent conformation remains controversial, in particular whether the passenger domain can adopt secondary structural motifs, such as disulfide- bonded segments, while maintaining a secretion-competent state. Here, we used the endogenous and closely spaced cysteine residues of the plasmid-encoded toxin (Pet) from enteroaggregative Escherichia coli to investigate the effect of disulfide bond-induced folding on translocation of an auto-transporter passenger domain. We reveal that rigid structural elements within disulfide-bonded segments are resistant to autotransporter-mediated secretion. We define the size limit of disulfide-bonded segments tolerated by the autotransporter system demonstrating that, when present, cysteine pairs are intrinsically closely spaced to prevent congestion of the translocator pore by large disulfide-bonded regions. These latter data strongly support the hairpin mode of autotransporter biogenesis.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Non-UQ

Document type: Journal Article
Sub-type: Article (original research)
Collection: UQ Diamantina Institute Publications
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Created: Thu, 20 Oct 2016, 00:56:16 EST by Timothy J Wells on behalf of UQ Diamantina Institute