Premium
Modulation of domain–domain interaction and protein function by a charged linker: A case study of mycobacteriophage D29 endolysin
Author(s) -
Pohane Amol Arunrao,
Patidar Neelam Devidas,
Jain Vikas
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.01.036
Subject(s) - lysin , linker , peptidoglycan , escherichia coli , hydrolase , bacteriophage , chemistry , enzyme , function (biology) , biochemistry , biophysics , biology , microbiology and biotechnology , computer science , gene , operating system
Phage‐encoded cell wall peptidoglycan hydrolyzing enzymes, called endolysins, are essential for efficient release of virions from bacteria, and show species‐specific killing of the host. We have demonstrated previously that the interaction between N‐terminal catalytic and C‐terminal cell wall binding domains of mycobacteriophage D29 endolysin makes the enzyme inactive in Escherichia coli . Here, we demonstrate that such interaction occurs intramolecularly and is facilitated by a charged linker that connects the two domains. We also show that linker composition is crucial for the inactivation of PG hydrolase in E. coli . Such knowledge will immensely help in bioengineering of endolysins with narrow or broad spectrum antimicrobial activity.