Structure of the Dispase Autolysis-inducing Protein from Streptomyces mobaraensis and Glutamine Cross-linking Sites for Transglutaminase.
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Authors
Fiebig, DavidSchmelz, Stefan
Zindel, Stephan
Ehret, Vera
Beck, Jan
Ebenig, Aileen
Ehret, Marina
Fröls, Sabrina
Pfeifer, Felicitas
Kolmar, Harald
Fuchsbauer, Hans-Lothar
Scrima, Andrea
Issue Date
2016
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Show full item recordAbstract
Transglutaminase 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.Citation
Structure of the Dispase Autolysis-inducing Protein from Streptomyces mobaraensis and Glutamine Cross-linking Sites for Transglutaminase. 2016, 291 (39):20417-26 J. Biol. Chem.Affiliation
Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7, 38124 Braunschweig, Germany.PubMed ID
27493205PubMed Central ID
PMC5034039Additional Links
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5034039/Type
ArticleLanguage
enISSN
1083-351Xae974a485f413a2113503eed53cd6c53
10.1074/jbc.M116.731109
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Except where otherwise noted, this item's license is described as http://creativecommons.org/licenses/by-nc-sa/4.0/
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