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Wiley InterScience

FEMS Microbiology Letters

FEMS Microbiology Letters

Volume 266 Issue 1, Pages 98 - 102

Published Online: 13 Nov 2006

© 2010 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved



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Identification of the glycosyl transferase required for synthesis of the principal glycolipid characteristic of heterocysts of Anabaena sp. strain PCC 7120
Koichiro Awai 1 & C. Peter Wolk 2
  1 Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI, USA; and   2 MSU-DOE Plant Research Laboratory and Department of Plant Biology, Michigan State University, East Lansing, MI, USA
  Correspondence: C. Peter Wolk, MSU-DOE Plant Research Laboratory and Department of Plant Biology, Michigan State University, East Lansing, MI 48824, USA. Tel.: 1 517 353 2049; fax: 1 517 353 9168; e-mail: wolk@msu.edu

  Present address: Koichiro Awai, Graduate School of Science and Engineering, Saitama University, Sakura-ku, Saitama 338-8570, Japan.

 Editor: Karl Forchhammer

Copyright © 2006 Federation of European Microbiological Societies
KEYWORDS
heterocyst • glycosyl transferase • heterocyst envelope glycolipid

ABSTRACT

Nitrogenase is oxygen-labile. Cyanobacterial heterocysts can fix N2 in an oxic milieu because their interior is micro-oxic, for which the glycolipid layer of the heterocyst envelope is required. ORF all5341 of the Anabaena sp. genome predicts a glycosyl transferase. An insertional mutant of all5341 synthesized only a nonglycosylated form of heterocyst envelope glycolipid, and lacked a glycolipid layer. All5341 appears to be the transferase required to glycosylate the glycolipid aglycone.


Received 10 September 2006; revised 10 October 2006; accepted 11 October 2006.
First published online 13 November 2006.

DIGITAL OBJECT IDENTIFIER (DOI)
10.1111/j.1574-6968.2006.00512.x About DOI

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