Structure of the Dispase Autolysis-inducing Protein from Streptomyces mobaraensis and Glutamine Cross-linking Sites for Transglutaminase.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
AbstractTransglutaminase from Streptomyces mobaraensis (MTG) is an important enzyme for cross-linking and modifying proteins. An intrinsic substrate of MTG is the dispase autolysis-inducing protein (DAIP). The amino acid sequence of DAIP contains 5 potential glutamines and 10 lysines for MTG-mediated cross-linking. The aim of the study was to determine the structure and glutamine cross-linking sites of the first physiological MTG substrate. A production procedure was established in Escherichia coli BL21 (DE3) to obtain high yields of recombinant DAIP. DAIP variants were prepared by replacing four of five glutamines for asparagines in various combinations via site-directed mutagenesis. Incorporation of biotin cadaverine revealed a preference of MTG for the DAIP glutamines in the order of Gln-39 ≫ Gln-298 > Gln-345 ∼ Gln-65 ≫ Gln-144. In the structure of DAIP the preferred glutamines do cluster at the top of the seven-bladed β-propeller. This suggests a targeted cross-linking of DAIP by MTG that may occur after self-assembly in the bacterial cell wall. Based on our biochemical and structural data of the first physiological MTG substrate, we further provide novel insight into determinants of MTG-mediated modification, specificity, and efficiency.
CitationStructure of the Dispase Autolysis-inducing Protein from Streptomyces mobaraensis and Glutamine Cross-linking Sites for Transglutaminase. 2016, 291 (39):20417-26 J. Biol. Chem.
AffiliationHelmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7, 38124 Braunschweig, Germany.
PubMed Central IDPMC5034039
The following license files are associated with this item:
Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by-nc-sa/4.0/
- A novel transglutaminase substrate from Streptomyces mobaraensis triggers autolysis of neutral metalloproteases.
- Authors: Sarafeddinov A, Schmidt S, Adolf F, Mainusch M, Bender A, Fuchsbauer HL
- Issue date: 2009 May
- Substrate specificity analysis of microbial transglutaminase using proteinaceous protease inhibitors as natural model substrates.
- Authors: Taguchi S, Nishihama KI, Igi K, Ito K, Taira H, Motoki M, Momose H
- Issue date: 2000 Sep
- Destructive twisting of neutral metalloproteases: the catalysis mechanism of the Dispase autolysis-inducing protein from Streptomyces mobaraensis DSM 40487.
- Authors: Fiebig D, Storka J, Roeder M, Meyners C, Schmelz S, Blankenfeldt W, Scrima A, Kolmar H, Fuchsbauer HL
- Issue date: 2018 Aug 31
- Engineered, highly reactive substrates of microbial transglutaminase enable protein labeling within various secondary structure elements.
- Authors: Rachel NM, Quaglia D, Lévesque É, Charette AB, Pelletier JN
- Issue date: 2017 Nov
- The transglutaminase activating metalloprotease inhibitor from Streptomyces mobaraensis is a glutamine and lysine donor substrate of the intrinsic transglutaminase.
- Authors: Schmidt S, Adolf F, Fuchsbauer HL
- Issue date: 2008 Sep 3