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Gewählte Publikation:

SHR Neuro Krebs Kardio Lipid

Hacker, C; Christ, NA; Duchardt-Ferner, E; Korn, S; Göbl, C; Berninger, L; Düsterhus, S; Hellmich, UA; Madl, T; Kötter, P; Entian, KD; Wöhnert, J.
The Solution Structure of the Lantibiotic Immunity Protein NisI and Its Interactions with Nisin.
J Biol Chem. 2015; 290(48):28869-28886 [OPEN ACCESS]
Web of Science PubMed PUBMED Central FullText FullText_MUG


Autor/innen der Med Uni Graz:
Madl Tobias

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Plum Analytics:
Number of Figures: 11
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Many Gram-positive bacteria produce lantibiotics, genetically encoded and posttranslationally modified peptide antibiotics, which inhibit the growth of other Gram-positive bacteria. To protect themselves against their own lantibiotics these bacteria express a variety of immunity proteins including the LanI lipoproteins. The structural and mechanistic basis for LanI-mediated lantibiotic immunity is not yet understood. Lactococcus lactis produces the lantibiotic nisin, which is widely used as a food preservative. Its LanI protein NisI provides immunity against nisin but not against structurally very similar lantibiotics from other species such as subtilin from Bacillus subtilis. To understand the structural basis for LanI-mediated immunity and their specificity we investigated the structure of NisI. We found that NisI is a two-domain protein. Surprisingly, each of the two NisI domains has the same structure as the LanI protein from B. subtilis, SpaI, despite the lack of significant sequence homology. The two NisI domains and SpaI differ strongly in their surface properties and function. Additionally, SpaI-mediated lantibiotic immunity depends on the presence of a basic unstructured N-terminal region that tethers SpaI to the membrane. Such a region is absent from NisI. Instead, the N-terminal domain of NisI interacts with membranes but not with nisin. In contrast, the C-terminal domain specifically binds nisin and modulates the membrane affinity of the N-terminal domain. Thus, our results reveal an unexpected structural relationship between NisI and SpaI and shed light on the structural basis for LanI mediated lantibiotic immunity. © 2015 by The American Society for Biochemistry and Molecular Biology, Inc.
Find related publications in this database (using NLM MeSH Indexing)
Bacillus subtilis -
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - metabolism
Bacteriocins - chemistry
Bacteriocins - genetics
Bacteriocins - metabolism
Lactococcus lactis - chemistry
Lactococcus lactis - genetics
Lactococcus lactis - metabolism
Lipoproteins - chemistry
Lipoproteins - genetics
Lipoproteins - metabolism
Membrane Proteins - chemistry
Membrane Proteins - genetics
Membrane Proteins - metabolism
Nisin - chemistry
Nisin - genetics
Nisin - metabolism
Protein Structure, Tertiary -
Structure-Activity Relationship -

Find related publications in this database (Keywords)
antibiotic resistance
nuclear magnetic resonance (NMR)
protein structure
nisin binding
small angle x-ray scattering
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