Isolation, gene structure, and comparative analysis of the S-layer gene sslA of Sporosarcina ureae ATCC 13881

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Contributors

Abstract

The surface (S)-layer of Sporosarcina ureae strain ATCC 13881, a periodic ordered structure with p4 square type symmetry, was recently reported to be an excellent biotemplate for the formation of highly ordered metal clusters. The S-layer is formed by self-assembly of a single subunit, the 116 kDa SslA protein. Here we report on the isolation and sequence analysis of the sslA gene. The protein sequence reveals a high degree of similarity to the sequences of other S-layer proteins that form self-assembly lattices with the p4 square type symmetry, especially to those of Bacillus sphaericus. Two conserved surface layer homology (SLH) domains in the extreme aminoterminal portion are likely to mediate attachment of the protein to secondary cell wall polymers. A central HisXXXHis motif and a cysteine residue in the carboxyl-terminal part of the protein, both extremely rare in S-layer proteins, may contribute to the high affinity for metal ions. The strong bias in the codon usage may explain that heterologous expression of SslA in E. coli is not very intense. With respect to the regulatory region we notice several features that are also present in other S-layer genes. The distance between the -35/-10 region and the ATG initiation codon is unusually long, and a 41 bp palindromic sequence is present in the immediate vicinity of the -35/-10 region.

Details

Original languageEnglish
Pages (from-to)255-265
Number of pages11
JournalGenetica
Volume131
Issue number3
Publication statusPublished - Nov 2007
Peer-reviewedYes

External IDs

Scopus 35448946393

Keywords

Keywords

  • surface layer, sporosarcina ureae, sslA, SLH domain, self-assembly, heterologous expression, CELL-WALL POLYMER, BACILLUS-STEAROTHERMOPHILUS PV72, METAL-BINDING PEPTIDES, SURFACE-LAYER, MOLECULAR CHARACTERIZATION, HETEROLOGOUS EXPRESSION, ESCHERICHIA-COLI, PROTEIN, DOMAIN, SECRETION