Archaeal surface appendages: their function and the critical role of N-linked glycosylation in their assembly

Ken F. Jarrell; Divya B. Nair; Gareth M. Jones; S.-I. Aizawa; James J. P. Chong; Meg Stark; Susan M. Logan; Evgeny Vinogradov; John F. Kelly

doi:10.1117/12.892939

23 September 2011 Archaeal surface appendages: their function and the critical role of N-linked glycosylation in their assembly

Ken F. Jarrell, Divya B. Nair, Gareth M. Jones, S.-I. Aizawa, James J. P. Chong, Meg Stark, Susan M. Logan, Evgeny Vinogradov, John F. Kelly

Author Affiliations +

Proceedings Volume 8152, Instruments, Methods, and Missions for Astrobiology XIV; 81520O (2011) https://doi.org/10.1117/12.892939
Event: SPIE Optical Engineering + Applications, 2011, San Diego, California, United States

Abstract

Many cultivated archaea are extremophiles and, as such, various archaea inhabit some of the most inhospitable niches on the planet in terms of temperature, pH, salinity and anaerobiosis. Different archaeal species have been shown to produce a number of unusual and sometimes unique surface structures. The best studied of these are flagella which are fundamentally different from bacterial flagella and instead bear numerous similarities to bacterial type IV pili in their structure and likely assembly. The major structural proteins, flagellins, are made as preproteins with type IV pilin-like signal peptides processed by a specific signal peptidase. In addition, the flagellins are glycoproteins with attached N-linked glycans. Both of these posttranslational modifications have been studied in the anaerobic archaeon, Methanococcus maripaludis, an organism which also possesses other surface appendages, an unusual version of type IV pili, whose major constituents are also glycoproteins. Analysis of mutants unable to make either or both of flagella and pili demonstrated that both are essential for attachment to surfaces. A number of mutants defective in the assembly and biosynthesis of the tetrasaccharide N-linked to the flagellins have been isolated. Investigations of these mutants by electron microscopy, mass spectrometry and motility assays have demonstrated that flagellins possessing no attached glycan or a glycan truncated to a single sugar cannot assemble flagella on their surface. Mutants which can attach a glycan of 2 or 3 sugars to flagellins assemble flagella but they are impaired in their swimming compared with wildtype cells which attach the tetrasaccharide to their flagellins.

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Ken F. Jarrell, Divya B. Nair, Gareth M. Jones, S.-I. Aizawa, James J. P. Chong, Meg Stark, Susan M. Logan, Evgeny Vinogradov, and John F. Kelly "Archaeal surface appendages: their function and the critical role of N-linked glycosylation in their assembly", Proc. SPIE 8152, Instruments, Methods, and Missions for Astrobiology XIV, 81520O (23 September 2011); https://doi.org/10.1117/12.892939

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