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Binding of SecB to ribosome-bound polypeptides has the same characteristics as binding to full-length, denatured proteins
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology.
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1997 (English)In: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, ISSN 0027-8424, Vol. 94, no 3, 802-807 p.Article in journal (Other scientific) Published
Abstract [en]

The interaction of the chaperone SecB with ribosome-bound polypeptides that are in the process of elongation has been studied using an in vitro protein synthesis system. The binding is characterized by the same properties as those demonstrated for the bin

Place, publisher, year, edition, pages
NATL ACAD SCIENCES , 1997. Vol. 94, no 3, 802-807 p.
Keyword [en]
ESCHERICHIA-COLI SECB; CHAPERONE SECB; SELECTIVE BINDING; LEADER PEPTIDE; MATURE PORTION; EXPORT; INVITRO; INVIVO; RECOGNITION; LIGAND
Identifiers
URN: urn:nbn:se:uu:diva-79753OAI: oai:DiVA.org:uu-79753DiVA: diva2:107666
Note
Addresses: Randall LL, WASHINGTON STATE UNIV, DEPT BIOCHEM & BIOPHYS, POB 644660, PULLMAN, WA 99164. UNIV YORK, DEPT BIOL, YORK YO1 5DD, N YORKSHIRE, ENGLAND. UPPSALA UNIV, DEPT MOL BIOL, CTR BIOMED, S-75124 UPPSALA, SWEDEN.Available from: 2008-10-17 Created: 2008-10-17 Last updated: 2011-01-15

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