New fluorescent substrates of microbial transglutaminase and its application to peptide tag-directed covalent protein labeling

Noriho Kamiya, Hiroki Abe

Research output: Chapter in Book/Report/Conference proceedingChapter

5 Citations (Scopus)

Abstract

Transglutaminase (TGase) is an enzyme that catalyzes the post-translational covalent cross-linking of Gln-and Lys-containing peptides and/or proteins according to its substrate specificity. We have recently designed a variety of Gln-donor fluorescent substrates of microbial transglutaminase (MTG) from Streptomyces mobaraensis and evaluated their potential use in MTG-mediated covalent protein labeling. The newly designed substrates are based on the relatively broad substrate recognition of MTG for the substitution of the N-terminal group of a conventional TGase substrate, benzyloxycarbonyl-l-glutaminylglycine (Z-QG). It is revealed that MTG is capable of accepting a diverse range of fluorophores in place of the N-terminal moiety of Z-QG when linked via a suitable linker. Here, we show the potential utility of a new fluorescent substrate for peptide tag-directed covalent protein labeling by employing fluorescein-4-isothiocyanate-β-Ala-QG as a model Gln-donor substrate for MTG.

Original languageEnglish
Title of host publicationMethods in Molecular Biology
PublisherHumana Press Inc.
Pages81-94
Number of pages14
DOIs
Publication statusPublished - 2011

Publication series

NameMethods in Molecular Biology
Volume751
ISSN (Print)1064-3745

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Genetics

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