Skip Navigation



Journal of Biochemistry Advance Access published online on January 2, 2008
Journal of Biochemistry, doi:10.1093/jb/mvm243
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow Supplementary Data
Right arrow All Versions of this Article:
143/3/425    most recent
mvm243v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Ueta, M.
Right arrow Articles by Wada, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ueta, M.
Right arrow Articles by Wada, A.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2008 The Japanese Biochemical Society

Role of HPF (Hibernation promoting factor) in translational activity in Escherichia coli

Masami Ueta1, Ryosuke L Ohniwa2, Hideji Yoshida1, Yasushi Maki1, Chieko Wada2,3 and Akira Wada1,3,*

1Department of Physics, Osaka Medical College, Takatsuki, Osaka 569-8686, Japan
2Laboratory of Plasma Membrane and Nuclear Signaling, Graduate School of Biostudies, Kyoto University, Kitashirakawa-Oiwake, Sakyo, Kyoto 606-8502, Japan
3Yoshida Biological Laboratory, Yamashina, Kyoto 607-8081, Japan

*Corresponding author: Dr. Akira Wada, Present address: Department of Physics, Osaka Medical College, 2-7, Daigaku-Machi, Takatsuki, Osaka 569-8686, Japan, Phone: +81-72-684-7023, Fax: +81-72-684-7023, e-mail: phy003{at}art.osaka-med.ac.jp

Received October 24, 2007; Accepted December 4, 2007


  Abstract

During the stationary phase of growth in Escherichia coli, RMF (ribosome modulation factor) and HPF (hibernation promoting factor) dimerize most 70S ribosomes to form 100S ribosomes. The process of 100S formation has been termed "ribosomal hibernation". Here, the contributions of HPF to 100S formation and translation were analyzed in vitro. HPF bound to, but did not dimerize the 70S ribosome. RMF dimerized and formed immature 90S ribosomes. Binding of both HPF and RMF converted 90S ribosomes to mature 100S ribosomes, which is consistent with the in vivo data. The role of HPF in in vitro translation also was investigated. In an artificial mRNA poly (U)-dependent phenylalanine incorporation assay, HPF bound to ribosomal particles and inhibited translation. In contrast, in a natural MS2 mRNA-dependent leucine incorporation assay, bound HPF was removed and hardly inhibited normal translation. Multiple alignment and phylogenetic analyses indicates that the hibernation system mediated by the HPF homologue, RMF, and 100S ribosome formation may be specific to the proteobacteria gamma group. In contrast, most bacteria have at least one HPF homologue, and these homologues can be classified into three types, long HPF, short HPF, and YfiA.

Key Words: Hibernation promoting factor (HPF), 100S ribosome, ribosomal hibernation, stationary phase, translation


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer:
Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.