Abstract：
:Many bacteria and most archaea possess a crystalline protein surface layer (S-layer), which surrounds their growing and topologically complicated outer surface. Constructing a macromolecular structure of this scale generally requires localized enzymatic machinery, but a regulatory framework for S-layer assembly has not been identified. By labeling, superresolution imaging, and tracking the S-layer protein (SLP) from C. crescentus, we show that 2D protein self-assembly is sufficient to build and maintain the S-layer in living cells by efficient protein crystal nucleation and growth. We propose a model supported by single-molecule tracking whereby randomly secreted SLP monomers diffuse on the lipopolysaccharide (LPS) outer membrane until incorporated at the edges of growing 2D S-layer crystals. Surface topology creates crystal defects and boundaries, thereby guiding S-layer assembly. Unsupervised assembly poses challenges for therapeutics targeting S-layers. However, protein crystallization as an evolutionary driver rationalizes S-layer diversity and raises the potential for biologically inspired self-assembling macromolecular nanomaterials.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Comerci CJ,Herrmann J,Yoon J,Jabbarpour F,Zhou X,Nomellini JF,Smit J,Shapiro L,Wakatsuki S,Moerner WEdoi
10.1038/s41467-019-10650-xsubject
Has Abstractpub_date
2019-06-21 00:00:00pages
2731issue
1issn
2041-1723pii
10.1038/s41467-019-10650-xjournal_volume
10pub_type
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