Skip Navigation


Journal of Biochemistry Advance Access originally published online on December 13, 2006
Journal of Biochemistry 2007 141(2):201-211; doi:10.1093/jb/mvm020
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary data
Right arrow All Versions of this Article:
141/2/201    most recent
mvm020v1
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 Ohgaki, K.
Right arrow Articles by Kang, D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Ohgaki, K.
Right arrow Articles by Kang, D.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 2006 The Japanese Biochemical Society.

The C-terminal Tail of Mitochondrial Transcription Factor A Markedly Strengthens its General Binding to DNA

Kippei Ohgaki1, Tomotake Kanki1, Atsushi Fukuoh1, Hironori Kurisaki1, Yoshimasa Aoki1, Masaki Ikeuchi1,2, Sang Ho Kim1,3, Naotaka Hamasaki1 and Dongchon Kang1,*

1Department of Clinical Chemistry and Laboratory Medicine and 2Department of Cardiovascular Medicine, Kyushu University Graduate School of Medical Sciences, Fukuoka, Japan 3Department of Biology Education, Daegu University, Kyungsan, Korea

*To whom correspondence should be addressed. Tel: +81-92-642-5749, Fax: +81-92-642-5772, E-mail: kang{at}mailserver.med.kyushu-u.ac.jp

Received November 27, 2006; Accepted November 29, 2006


  Abstract

Mitochondrial transcription factor A (TFAM) contains a basic C-terminal tail which is essential for the promoter-specific transcription. TFAM is also a major component of a protein–mitochondrial DNA (mtDNA) complex, called nucleoid, as a non-specific DNA-binding protein. However, little is known about a role of the C-tail in the nucleoid. Overexpression of full-length TFAM decreased the amount of a D-loop form of mtDNA in cells, while overexpression of TFAM lacking its C-tail (TFAM-{Delta}C) did not, suggesting that the C-tail is involved in destabilization or formation of the D-loop. An mRNA for mtDNA-derived ND1 was hardly decreased in the former but rather decreased in the latter. Given that the D-loop formation is coupled with the transcription, the decrease in the D-loop is likely due to its destabilization. The recombinant full-length TFAM much strongly unwound DNA than TFAM-{Delta}C, which is consistent with the above idea because D-loop is resolved by unwinding of the supercoiling state. Notably, truncation of the C-tail decreased DNA-binding activity of TFAM by three orders of magnitude. Thus, the C-terminal tail of TFAM is important for the strong general binding to mtDNA. This strong DNA-binding conferred by the C-tail may play an important role in the nucleoid structure.

Key Words: D-loop, mitochondrial DNA, nucleoid, TFAM, transcription


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


This article has been cited by other articles:


Home page
 Mol. Biol. CellHome page
B. A. Kaufman, N. Durisic, J. M. Mativetsky, S. Costantino, M. A. Hancock, P. Grutter, and E. A. Shoubridge
The Mitochondrial Transcription Factor TFAM Coordinates the Assembly of Multiple DNA Molecules into Nucleoid-like Structures
Mol. Biol. Cell, September 1, 2007; 18(9): 3225 - 3236.
[Abstract] [Full Text] [PDF]


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.