HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) All Versions of this Article: ps.051752506v1 15/2/242    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Svetlov, M. S. Articles by Spirin, A. S. Search for Related Content PubMed PubMed Citation Articles by Svetlov, M. S. Articles by Spirin, A. S. Social Bookmarking                   What's this?

Effective cotranslational folding of firefly luciferase without chaperones of the Hsp70 family

Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia

(RECEIVED August 4, 2005; FINAL REVISION August 4, 2005; ACCEPTED October 27, 2005)

Molecular chaperones of the Hsp70 family (bacterial DnaK, DnaJ, and GrpE) were shown to be strictly required for refolding of firefly luciferase from a denatured state and thus for effective restoration of its activity. At the same time the luciferase was found to be synthesized in an Escherichia coli cell-free translation system in a highly active state in the extract with no chaperone activity. The addition of the chaperones to the extract during translation did not raise the activity of the enzyme. The abrupt arrest of translation by the addition of a translational inhibitor led to immediate cessation of the enzyme activity accumulation, indicating the cotranslational character of luciferase folding. The results presented suggest that the chaperones of the Hsp70 family are not required for effective cotranslational folding of firefly luciferase.

Keywords: cotranslational folding; specific activity; Hsp70 chaperones; trigger factor

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051752506.

Reprint requests to: Alexander S. Spirin, Institute of Protein Research, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia; e-mail: spirin{at}vega.protres.ru; fax: +7 (096) 773-1600.

CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				C. W. Kim, K. S. Han, K.-S. Ryu, B. H. Kim, K.-H. Kim, S. I. Choi, and B. L. Seong N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers Protein Sci., April 1, 2007; 16(4): 635 - 643. [Abstract] [Full Text] [PDF]