Skip Navigation

This Article
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 Email this article to a friend
Right arrow Similar articles in this journal
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 Kawaguchi, M.
Right arrow Articles by Syono, K.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Kawaguchi, M.
Right arrow Articles by Syono, K.
Agricola
Right arrow Articles by Kawaguchi, M.
Right arrow Articles by Syono, K.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Plant and Cell Physiology, 1990, Vol. 31, No. 4 449-455
© 1990

Article

Isolation of Rhizobium leguminosarum biovar viciae Variants with Indole-3-acetamide Hydrolase Activity

Masayoshi Kawaguchi1, Masami Sekine2 and Kunihiko Syono1

1Department of Pure and Applied Sciences, College of Arts and Sciences, The University of Tokyo Meguro-ku, Tokyo, 153 Japan
2Department of Fermentation Technology, Faculty of Engineering, Osaka University Suita, 565 Japan

The IAA biosynthetic pathway from tryptophan to IAA via IAM (IAM pathway) was investigated in Rhizobium spp. (fast-growing rhizobium). Southern hybridization with the bam gene, a structural gene for IAM hydrolase (the enzyme that converts IAM to IAA) cloned from Bradyrhizobium japonicum J1063, indicated that homologous sequences exist among wild-type Rhizobium spp. However the IAM pathway has not been detected biochemically in free-living bacteria. When 5-methyltryptophan-resistant strains were screened for Rhizobium leguminosarum biovar viciae K5 which has DNA sequences with high homology to the bam gene, spontaneous mutants showing IAM hydrolase activity were isolated. The results suggest the possibility that the activity of IAM hydrolase is suppressed in free-living state in Rhizobium leguminosarum biovar viciae K5. In addition we detected the peak at the same tR of IAM by HPLC analysis using two columns when a large amount of L-tryptophan was added to the suspension of 5-methyltryptophan-resistant variants. Whether or not tryptophan-2-monooxygenase activity, however, actually works in Rhizobium cells remained to be solved.

(Received September 20, 1989; Accepted March 6, 1990)
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.