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Microbiology 152 (2006), 2779-2787; DOI  10.1099/mic.0.28971-0
© 2006 Society for General Microbiology

Involvement of the S-layer proteins Hpi and SlpA in the maintenance of cell envelope integrity in Deinococcus radiodurans R1

Heather Rothfuss1, Jimmie C. Lara2, Amy K. Schmid3,{dagger} and Mary E. Lidstrom1,2


1 Department of Chemical Engineering, University of Washington, Seattle, WA 98195, USA
2 Department of Microbiology, University of Washington, Seattle, WA 98195, USA
3 Program in Molecular and Cellular Biology, University of Washington, Seattle, WA 98195, USA

Correspondence
Mary E. Lidstrom
lidstrom{at}u.washington.edu

The potential functions have been investigated of two proteins in Deinococcus radiodurans R1 predicted to be involved in the maintenance and integrity of the S layer: the hexagonally packed intermediate (Hpi) protein, and SlpA (DR2577), a homologue of an S-layer SlpA protein in Thermus thermophilus. Deletion of the hpi gene had little effect on the structure of the cell envelope or on shear- or solvent-induced stress responses. However, deletion of the slpA gene caused substantial alterations in cell envelope structure, and a significant defect in resistance to solvent and shear stresses compared to the wild-type. Ultrastructural analysis of slpA mutant cells indicated loss of much of the outer Hpi protein carbohydrate coat, the ‘pink envelope’, and the membrane-like backing layer. Together these results suggest that the SlpA protein may be involved in attachment of the Hpi surface layer to the inner cell envelope, and that SlpA may play an important role in the maintenance of cell envelope integrity in D. radiodurans.

Abbreviations: HPI, hexagonally packed intermediate; S layer, surface layer; SEM, scanning electron microscopy; SLH, S-layer homology

{dagger}Present address: Institute for Systems Biology, 1441 N 34th St, Seattle, WA 98103, USA.






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