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Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle.
Authors
Albanese
Beck
+45 more
Bernstein
Buskiewicz
Craig
Dalbey
de Gier
Deuerling
Eisner
Ellman
Etchells
Ferbitz
Flanagan
Genevaux
Gu
Halic
Halic
Harms
Houben
Houben
Houben
Jensen
Jong
Kebir
Kramer
Kramer
Kuroiwa
Kusters
Lee
Liebke
Lill
Lu
Luirink
Nissen
Pool
Raine
Scotti
Stoller
Teter
Ullers
Ullers
Urbanus
Valent
Vrontou
Woolhead
Ying
Young
Publication date
1 January 2006
Publisher
Doi
Cite
Abstract
As nascent polypeptides exit the ribosomal tunnel they immediately associate with chaperones, folding catalysts, and targeting factors. These interactions are decisive for the future conformation and destination of the protein that is being synthesized. Using Escherichia coli as a model organism, we have systematically analyzed how the earliest contacts of nascent polypeptides with cytosolic factors depend on the nature and future destination of the emerging sequence using a photo cross-linking approach. Together, the data suggest that the chaperone trigger factor is adjacent to emerging sequences by default, consistent with both its placement near the nascent chain exit site and its cellular abundance. The signal recognition particle (SRP) effectively competes the contact with TF when a signal anchor (SA) sequence of a nascent inner membrane protein appears outside the ribosome. The SRP remains in contact with the SA and downstream sequences during further synthesis of ∼30 amino acids. The contact with trigger factor is then restored unless another transmembrane segment reinitiates SRP binding. Importantly and in contrast to published data, the SRP appears perfectly capable of distinguishing SA sequences from signal sequences in secretory proteins at this early stage in biogenesis. © 2006 by The American Society for Biochemistry and Molecular Biology, Inc
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