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 Chaban, B.
Right arrow Articles by Jarrell, K. F.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chaban, B.
Right arrow Articles by Jarrell, K. F.

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2009, p. 187-195, Vol. 191, No. 1
0021-9193/09/$08.00+0     doi:10.1128/JB.00885-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

AglC and AglK Are Involved in Biosynthesis and Attachment of Diacetylated Glucuronic Acid to the N-Glycan in Methanococcus voltae{triangledown}

Bonnie Chaban,1 Susan M. Logan,2 John F. Kelly,2 and Ken F. Jarrell1*

Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, K7L 3N6, Canada,1 Institute for Biological Sciences, National Research Council, Ottawa, Ontario, K1A 0R6, Canada2

Received 27 June 2008/ Accepted 19 October 2008

Recent advances in the field of prokaryotic N-glycosylation have established a foundation for the pathways and proteins involved in this important posttranslational protein modification process. To continue the study of the Methanococcus voltae N-glycosylation pathway, characteristics of known eukaryotic, bacterial, and archaeal proteins involved in the N-glycosylation process were examined and used to select candidate M. voltae genes for investigation as potential glycosyl transferase and flippase components. The targeted genes were knocked out via linear gene replacement, and the resulting effects on N-glycan assembly were identified through flagellin and surface (S) layer protein glycosylation defects. This study reports the finding that deletion of two putative M. voltae glycosyl transferase genes, designated aglC (for archaeal glycosylation) and aglK, interfered with proper N-glycosylation. This resulted in flagellin and S-layer proteins with significantly reduced apparent molecular masses, loss of flagellar assembly, and absence of glycan attachment. Given previous knowledge of both the N-glycosylation pathway in M. voltae and the general characteristics of N-glycosylation components, it appears that AglC and AglK are involved in the biosynthesis or transfer of diacetylated glucuronic acid within the glycan structure. In addition, a knockout of the putative flippase candidate gene (Mv891) had no effect on N-glycosylation but did result in the production of giant cells with diameters three to four times that of wild-type cells.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Queen's University, Kingston, Ontario, K7L 3N6, Canada. Phone: (613) 533-2456. Fax: (613) 533-6796. E-mail: jarrellk{at}queensu.ca

{triangledown} Published ahead of print on 31 October 2008.

Journal of Bacteriology, January 2009, p. 187-195, Vol. 191, No. 1
0021-9193/09/$08.00+0     doi:10.1128/JB.00885-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Yurist-Doutsch, S., Eichler, J. (2009). Manual Annotation, Transcriptional Analysis, and Protein Expression Studies Reveal Novel Genes in the agl Cluster Responsible for N Glycosylation in the Halophilic Archaeon Haloferax volcanii. J. Bacteriol. 191: 3068-3075 [Abstract] [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»