Next Article in Journal
Ionic Liquids as Solvents for Rhodium and Platinum Catalysts Used in Hydrosilylation Reaction
Next Article in Special Issue
Formation and Physiochemical Properties of Silver Nanoparticles with Various Exopolysaccharides of a Medicinal Fungus in Aqueous Solution
Previous Article in Journal
Efficient Synthesis of Fully Substituted Pyrrolidine-Fused 3-Spirooxindoles via 1,3-Dipolar Cycloaddition of Aziridine and 3-Ylideneoxindole
Previous Article in Special Issue
Preparation of Hydrochlorothiazide Nanoparticles for Solubility Enhancement
Article Menu
Issue 9 (September) cover image

Export Article

Open AccessArticle
Molecules 2016, 21(9), 1117; doi:10.3390/molecules21091117

Truncation Derivatives of the S-Layer Protein of Sporosarcina ureae ATCC 13881 (SslA): Towards Elucidation of the Protein Domain Responsible for Self-Assembly

Electronics Packaging Laboratory, Department of Electrical Engineering and Information Technology, Technische Universität Dresden, 01069 Dresden, Germany
Academic Editors: Ecaterina Andronescu and Alexandru Mihai Grumezescu
Received: 30 June 2016 / Revised: 12 August 2016 / Accepted: 19 August 2016 / Published: 24 August 2016
View Full-Text   |   Download PDF [3744 KB, uploaded 24 August 2016]   |  

Abstract

The cell surface of Sporosarcina ureae ATCC 13881 is covered by an S-layer (SslA) consisting of identical protein subunits that assemble into lattices exhibiting square symmetry. In this work the self-assembly properties of the recombinant SslA were characterised with an emphasis on the identification of protein regions responsible for self-assembly. To this end, recombinant mature SslA (aa 31-1097) and three SslA truncation derivatives (one N-terminal, one C-terminal and one CN-terminal) were produced in a heterologous expression system, isolated, purified and their properties analysed by in vitro recrystallisation experiments on a functionalised silicon wafer. As a result, recombinant mature SslA self-assembled into crystalline monolayers with lattices resembling the one of the wild-type SslA. The study identifies the central protein domain consisting of amino acids 341-925 self-sufficient for self-assembly. Neither the first 341 amino acids nor the last 172 amino acids of the protein sequence are required to self-assemble into lattices. View Full-Text
Keywords: surface layer protein; Sporosarcina ureae ATCC 13881; mutagenesis; self-assembly surface layer protein; Sporosarcina ureae ATCC 13881; mutagenesis; self-assembly
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Varga, M. Truncation Derivatives of the S-Layer Protein of Sporosarcina ureae ATCC 13881 (SslA): Towards Elucidation of the Protein Domain Responsible for Self-Assembly. Molecules 2016, 21, 1117.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]

Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top