Skip Navigation


Molecular Plant Advance Access originally published online on December 4, 2008
Molecular Plant 2009 2(2):336-343; doi:10.1093/mp/ssn077
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplementary Data
Right arrow All Versions of this Article:
2/2/336    most recent
ssn077v1
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 arrowRequest Permissions
Google Scholar
Right arrow Articles by Hosoya-Matsuda, N.
Right arrow Articles by Hisabori, T.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The Author 2008. Published by the Molecular Plant Shanghai Editorial Office in association with Oxford University Press on behalf of CSPP and IPPE, SIBS, CAS.

Roles of Thioredoxins in the Obligate Anaerobic Green Sulfur Photosynthetic Bacterium Chlorobaculum tepidum

Naomi Hosoya-Matsudaa, Kazuhito Inouea and Toru Hisaborib,1

a Department of Biological Sciences, Kanagawa University, Hiratsuka, Kanagawa 259-1293, Japan
b Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259–R1-8, Yokohama 226-8503, Japan

1 To whom correspondence should be addressed. E-mail thisabor{at}res.titech.ac.jp, fax 81-(0)45924-5234.

Thioredoxin is a small ubiquitous protein that is involved in the dithiol–disulfide exchange reaction, by way of two cysteine residues located on the molecule surface. In order to elucidate the role of thioredoxin in Chlorobaculum tepidum, an anaerobic green sulfur bacterium that uses various inorganic sulfur compounds and H2S as electron donors under strict anaerobic conditions for growth, we applied the thioredoxin affinity chromatography method (Motohashi et al., 2001). In this study, 37 cytoplasmic proteins were captured as thioredoxin target candidates, including proteins involved in sulfur assimilation. Furthermore, six of the candidate proteins were members of the reductive tricarboxylic acid cycle (pyruvate orthophosphate dikinase, pyruvate flavodoxin/ferredoxin oxidoreductase, {alpha}-oxoglutarate synthase, citrate lyase, citrate synthase, malate dehydrogenase). The redox sensitivity of three enzymes was then examined: citrate lyase, citrate synthase, and malate dehydrogenase, using their recombinant proteins. Based on the information relating to the target proteins, the significance of thioredoxin as a reductant for the metabolic pathway in the anaerobic photosynthetic bacteria is discussed.

Key Words: Thioredoxin • anaerobic green sulfur bacteria • redox regulation • reductive tricarboxylic acid cycle


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.