JCB logo
Quantitative Colocalization Analysis Software
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online January 22, 2007
doi:10.1083/jcb.200611121
The Journal of Cell Biology, Vol. 176, No. 3, 307-317
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Shimohata et al.
This Article
Right arrow Full Text
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Shimohata, N.
Right arrow Articles by Ito, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shimohata, N.
Right arrow Articles by Ito, K.
Right arrowPubmed/NCBI databases
*Gene*GEO Profiles
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Article

 SecY alterations that impair membrane protein folding and generate a membrane stress

Nobuyuki Shimohata1, Shushi Nagamori2, Yoshinori Akiyama1, H. Ronald Kaback2,3,4, and Koreaki Ito1

1 Institute for Virus Research, Kyoto University, Sakyo-ku, Kyoto 606-8507, Japan
2 Department of Physiology, 3 Department of Microbiology, Immunology, and Molecular Genetics, and 4 Molecular Biology Institute, University of California, Los Angeles, Los Angeles, CA 90095

Correspondence to Koreaki Ito: kito{at}virus.kyoto-u.ac.jp

We report on a class of Escherichia coli SecY mutants that impair membrane protein folding. The mutants also up-regulate the Cpx/{sigma}E stress response pathways. Similar stress induction was also observed in response to a YidC defect in membrane protein biogenesis but not in response to the signal recognition particle–targeting defect or in response to a simple reduction in the abundance of the translocon. Together with the previous contention that the Cpx system senses a protein abnormality not only at periplasmic and outer membrane locations but also at the plasma membrane, abnormal states of membrane proteins are postulated to be generated in these secY mutants. In support of this notion, in vitro translation, membrane integration, and folding of LacY reveal that mutant membrane vesicles allow the insertion of LacY but not subsequent folding into a normal conformation recognizable by conformation-specific antibodies. The results demonstrate that normal SecY function is required for the folding of membrane proteins after their insertion into the translocon.

N. Shimohata and S. Nagamori contributed equally to this paper.

N. Shimohata's present address is Department of Molecular Cell Biology, Graduate School of Medicine, Osaka City University, Abeno-ku, Osaka 545-8585, Japan.

Abbreviations used in this paper: IMV, inverted membrane vesicle; PSBT, 1.3 S subunit of Propionibacterium shermanii biotin transcarboxylase; SRP, signal recognition particle; TM, transmembrane.


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


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents