This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
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 Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hara, F.
Right arrow Articles by Yamagishi, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hara, F.
Right arrow Articles by Yamagishi, A.

 Previous Article  |  Next Article 

Journal of Bacteriology, March 2007, p. 2039-2045, Vol. 189, No. 5
0021-9193/07/$08.00+0     doi:10.1128/JB.01454-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

An Actin Homolog of the Archaeon Thermoplasma acidophilum That Retains the Ancient Characteristics of Eukaryotic Actin{triangledown}

Futoshi Hara,1 Kan Yamashiro,1 Naoki Nemoto,1 Yoshinori Ohta,2 Shin-ichi Yokobori,1 Takuo Yasunaga,2 Shin-ichi Hisanaga,3 and Akihiko Yamagishi1*

Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392,1 Department of Bioscience and Bioinformatics, Faculty of Computer Science and Systems Engineering, Kyushu Institute of Technology, 680-4, Ooaza-kawazu, Iizuka, Fukuoka, 820-8502,2 Department of Biological Sciences, Graduate School of Science, Tokyo Metropolitan University, 1-1 Minami-osawa, Hachioji, Tokyo 192-0397, Japan3

Received 14 September 2006/ Accepted 14 December 2006

Actin, a central component of the eukaryotic cytoskeleton, plays a crucial role in determining cell shape in addition to several other functions. Recently, the structure of the archaeal actin homolog Ta0583, isolated from the archaeon Thermoplasma acidophilum, which lacks a cell wall, was reported by Roeben et al. (J. Mol. Biol. 358:145-156, 2006). Here we show that Ta0583 assembles into bundles of filaments similar to those formed by eukaryotic actin. Specifically, Ta0583 forms a helix with a filament width of 5.5 nm and an axial repeating unit of 5.5 nm, both of which are comparable to those of eukaryotic actin. Eukaryotic actin shows a greater resemblance to Ta0583 than to bacterial MreB and ParM in terms of polymerization characteristics, such as the requirement for Mg2+, critical concentration, and repeating unit size. Furthermore, phylogenetic analysis also showed a closer relationship between Ta0583 and eukaryotic actin than between MreB or ParM and actin. However, the low specificity of Ta0583 for nucleotide triphosphates indicates that Ta0583 is more primitive than eukaryotic actin. Taken together, our results suggest that Ta0583 retains the ancient characteristics of eukaryotic actin.

* Corresponding author. Mailing address: Department of Molecular Biology, Tokyo University of Pharmacy and Life Science, 1432-1 Horinouchi, Hachioji, Tokyo 192-0392, Japan. Phone: 81-42-676-7139. Fax: 81-42-676-7145. E-mail: yamagish{at}LS.toyaku.ac.jp.

{triangledown} Published ahead of print on 22 December 2006.

Journal of Bacteriology, March 2007, p. 2039-2045, Vol. 189, No. 5
0021-9193/07/$08.00+0     doi:10.1128/JB.01454-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Reisler, E., Egelman, E. H. (2007). Actin Structure and Function: What We Still Do Not Understand. J. Biol. Chem. 282: 36133-36137 [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»