MbtH-like proteins (MLPs) are required for soluble expression and/or optimal activity of some adenylation (A) domains of nonribosomal peptide synthetases. Because A domains can interact with noncognate MLP partners, how the function of an A domain, TioK, involved in the biosynthesis of the bisintercalator thiocoraline, is altered by noncognate MLPs has been investigated. Measuring TioK activity with 12 different MLPs from a variety of bacterial species by using a radiometric assay suggested that the A domain substrate promiscuity could be altered by foreign MLPs. Kinetic studies and bioinformatics analysis expanded the complexity of MLP functions and interactions.
|Number of pages||9|
|State||Published - Oct 18 2018|
Bibliographical noteFunding Information:
This work was supported by a NSF CAREER Award MCB-1149427 (to S.G.-T.); the Department of Pharmaceutical Sciences (to S.G.-T.); the Department of Molecular and Cellular Biochemistry at the University of Kentucky (to M.G.F.); and, in part, with Federal funds awarded to the Seattle Structural Genomics Center for Infectious Disease (SSGCID) from the National Institute of Allergy and Infectious Diseases, National Institutes of Health (NIH), Department of Health and Human Services, under contract no. HHSN272201200025C (to S.G.-T. and G.W.B). S.M. is a recipient of a 2018 long-term visit fellowship from the Yamada Science Foundation, Japan. We thank Dr. Robin Stacy for collaborating on this project. We thank Dr. Wenjing Chen for preliminary cloning and expression of TioK with some MLPs.
© 2018 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim
- protein–protein interactions
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology
- Organic Chemistry