Linked Life Data

12270717

Source:http://linkedlifedata.com/resource/pubmed/id/12270717

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2002-9-24
pubmed:abstractText
An elementary step in the assembly of adhesive type 1 pili of Escherichia coli is the folding of structural pilus subunits in the periplasm. The previously determined X-ray structure of the complex between the type 1 pilus adhesin FimH and the periplasmic pilus assembly chaperone FimC has shown that FimH consists of a N-terminal lectin domain and a C-terminal pilin domain, and that FimC exclusively interacts with the pilin domain. The pilin domain fold, which is common to all pilus subunits, is characterized by an incomplete beta-sheet that is completed by a donor strand from FimC in the FimC-FimH complex. This, together with unsuccessful attempts to refold isolated, urea-denatured FimH in vitro had suggested that folding of pilin domains strictly depends on sequence information provided by FimC. We have now analyzed in detail the folding of FimH and its two isolated domains in vitro. We find that not only the lectin domain, but also the pilin domain can fold autonomously and independently of FimC. However, the thermodynamic stability of the pilin domain is very low (8-10kJmol(-1)) so that a significant fraction of the domain is unfolded even in the absence of denaturant. This explains the high tendency of structural pilus subunits to aggregate non-specifically in the absence of stoichiometric amounts of FimC. Thus, pilus chaperones prevent non-specific aggregation of pilus subunits by native state stabilization after subunit folding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
322
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
827-40
pubmed:dateRevised
2008-6-17
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Chaperone-independent folding of type 1 pilus domains.
pubmed:affiliation
Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule Hönggerberg, CH-8093 Zurich, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't